2026
Probing 3-amino-2H-azaindazoles as allosteric inhibitors of the protein tyrosine phosphatase SHP2.
Amoussa, Machoud, Efrém, Nina-Louisa, Li, Feng, Guo, Ziqiong, Roske, Yvette
ORCID: https://orcid.org/0000-0001-6237-388X, Frank, Katrin Jana, Pach, Szymon, Wolf, Clemens Alexander, Bo, Feng, Lesina, Marina, Kintzel, Mika, Alsalim, Rana, Zeitz, Victoria, Csorba, Noémi, Radetzki, Silke
ORCID: https://orcid.org/0000-0003-2688-2868, Keserű, György M., Daumke, Oliver
ORCID: https://orcid.org/0000-0002-6190-1414, Algül, Hana, Wolber, Gerhard, Li, Jia and Nazaré, Marc
ORCID: https://orcid.org/0000-0002-1602-2330
ChemMedChem 21
(11): e70341.
15 June 2026
Crystal structure of 3-hydroxypropionyl-CoA synthetase (ADP-forming) from Nitrosopumilus maritimus.
Johnson, Jerome, Tosun, Bilge, Yilmaz, Merve, Tolar, Bradley B., Yoshikuni, Yasuo, Francis, Christopher A., Doukov, Tzanko, Yokoi, Shun, Wakatsuki, Soichi and DeMirci, Hasan
Current Research in Structural Biology 11
: 100189.
June 2026
Mapping the SHP2 allosteric pocket with target-biased covalent fragments.
Efrém, Nina-Louisa, Csorba, Noémi, Amoussa, Machoud, Ábrányi-Balogh, Péter, Guo, Ziqiong, Petri, László, Bo, Feng, Di Lorenzo, Vincenzo, Roske, Yvette
ORCID: https://orcid.org/0000-0001-6237-388X, Szalai, Tibor Viktor
ORCID: https://orcid.org/0009-0000-4088-3117, Mihalovits, Levente, Simon, József, Li, Jia, Daumke, Oliver
ORCID: https://orcid.org/0000-0002-6190-1414, Keserű, György M. and Nazaré, Marc
ORCID: https://orcid.org/0000-0002-1602-2330
ChemBioChem 27
(8): e70310.
April 2026
Conservation and specificity in Bacillus biofilm dynamics: on structure and function of B. cereus Camelysins.
Diehl, Anne, Lindemann, Florian, Cremer, Nils, Roske, Yvette
ORCID: https://orcid.org/0000-0001-6237-388X, Hiller, Matthias, van Rossum, Barth, Leidert, Martina, Turgay, Kürşad and Oschkinat, Hartmut
Journal of Molecular Biology 438
(6): 169661.
15 March 2026
3-hydroxypropionyl-CoA Synthetase (ADP-forming) from Nitrosopumilus maritimus.
Johnson, J.A., Yilmaz, M., Tosun, B., Wakatsuki, S. and Demirci, H.
[Dataset]
11 March 2026
Towards crystal structures of filament forming proteins.
Roske, Yvette
ORCID: https://orcid.org/0000-0001-6237-388X, Leidert, Martina, Rehbein, Kristina and Diehl, Anne
ORCID: https://orcid.org/0000-0001-7295-9972
bioRxiv
: 2026.02.22.707290.
22 February 2026
Effect of temperature ramp in rapid folding of 3D DNA origami structures.
Dey, Anurit
ORCID: https://orcid.org/0009-0004-2272-5544, Al Hussain, Mohammed Mustafa A.
ORCID: https://orcid.org/0000-0001-7132-8482, Pham, Xuan‐Hung
ORCID: https://orcid.org/0000-0002-4927-7102, Loo, Jacky
ORCID: https://orcid.org/0000-0002-0355-8865, Natarajan, Ashwin Karthick
ORCID: https://orcid.org/0000-0001-7897-708X and Kuzyk, Anton
ORCID: https://orcid.org/0000-0001-8060-6122
Small Structures 7
(2): e202500682.
February 2026
Integrative modelling reveals the structure of the human Mic60-Mic19 subcomplex and its role as a diffusion barrier in mitochondria.
Nathanail, Evangelia
ORCID: https://orcid.org/0009-0004-9579-8074, Rolando, Edoardo
ORCID: https://orcid.org/0009-0001-8276-1406, Ruwolt, Max
ORCID: https://orcid.org/0009-0000-7220-406X, Zaporozhets, Iryna, Liu, Fan
ORCID: https://orcid.org/0000-0002-2358-549X, Clementi, Cecilia
ORCID: https://orcid.org/0000-0001-9221-2358 and Daumke, Oliver
ORCID: https://orcid.org/0000-0002-6190-1414
bioRxiv
: 2026.01.30.702776.
30 January 2026
2025
Structural studies suggest CCDC127 as a novel membrane contact site protein in the mitochondrial intermembrane space.
Bock-Bierbaum, Tobias
ORCID: https://orcid.org/0000-0003-0843-2716, von der Malsburg, Karina, Natarajan, Ashwin Karthick
ORCID: https://orcid.org/0000-0001-7897-708X, Zarges, Christine, Akkaya, Kerem Can, Aladawi, Amjad, Noll, Katja, Jungbluth, Sibylle, Schirra, Claudia, Zhu, Ying, Cremer, Nils, Bernert, Carola, Liu, Fan
ORCID: https://orcid.org/0000-0002-2358-549X, Lehmann, Martin
ORCID: https://orcid.org/0000-0002-8370-6353, Riemer, Jan
ORCID: https://orcid.org/0000-0002-7574-8457, van der Laan, Martin
ORCID: https://orcid.org/0000-0003-0789-9912 and Daumke, Oliver
ORCID: https://orcid.org/0000-0002-6190-1414
bioRxiv
: 2025.12.11.693622.
16 December 2025
Dynamic nanoscale architecture of synaptic vesicle fusion in mouse hippocampal neurons.
Kroll, Jana
ORCID: https://orcid.org/0000-0003-4243-4088, Kravčenko, Uljana
ORCID: https://orcid.org/0009-0004-7176-8444, Sadeghi, Mohsen
ORCID: https://orcid.org/0000-0002-7698-5630, Diebolder, Christoph A.
ORCID: https://orcid.org/0000-0001-7694-7362, Ivanov, Lia, Lubas, Małgorzata, Sprink, Thiemo
ORCID: https://orcid.org/0000-0002-0760-6828, Schacherl, Magdalena
ORCID: https://orcid.org/0000-0002-5478-2509, Kudryashev, Mikhail
ORCID: https://orcid.org/0000-0003-3550-6274 and Rosenmund, Christian
ORCID: https://orcid.org/0000-0002-3905-2444
Nature Communications 16
(1): 11131.
15 December 2025
Topology control by a conserved cysteine pair in the OMM-protein CCDC127 enables MICOS interaction.
Zarges, Christine, Schepsky, Pauline, Rothemann, Robin Alexander, Bock-Bierbaum, Tobias
ORCID: https://orcid.org/0000-0003-0843-2716, von der Malsburg, Alexander, Baumann, Linda, Trifunovic, Aleksandra
ORCID: https://orcid.org/0000-0002-5472-3517, Daumke, Oliver
ORCID: https://orcid.org/0000-0002-6190-1414, van der Laan, Martin
ORCID: https://orcid.org/0000-0003-0789-9912, von der Malsburg, Karina and Riemer, Jan
ORCID: https://orcid.org/0000-0002-7574-8457
bioRxiv
: 2025.12.12.693940.
15 December 2025
Molecular machineries shaping the mitochondrial inner membrane.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and van der Laan, M.
ORCID: https://orcid.org/0000-0003-0789-9912
Nature Reviews Molecular Cell Biology 26
(9): 706-724.
September 2025
Detergent-free reconstitution of transmembrane proteins in giant liposomes of complex curvature by the Synthetic Membrane Transfer.
Meena, Hemraj, Zdanowicz, Rafal
ORCID: https://orcid.org/0009-0005-5694-2704, Bock-Bierbaum, Tobias
ORCID: https://orcid.org/0000-0003-0843-2716, Stephan, Till
ORCID: https://orcid.org/0000-0002-4032-7644, Ottsen Knudsen, Sofie Dorothea, Jakobs, Stefan
ORCID: https://orcid.org/0000-0002-8028-3121, Daumke, Oliver
ORCID: https://orcid.org/0000-0002-6190-1414, Pedersen, Per A. and De Franceschi, Nicola
ORCID: https://orcid.org/0000-0002-7221-613X
bioRxiv
: 2025.08.23.671895.
23 August 2025
Structures of EHD2 filaments on curved membranes provide a model for caveolar neck stabilization.
Vázquez-Sarandeses, E., Mikirtumov, V.
ORCID: https://orcid.org/0009-0004-6849-4825, Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Kudryashev, M.
ORCID: https://orcid.org/0000-0003-3550-6274 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
bioRxiv
: 2025.06.05.658037.
7 June 2025
Penta-ALFA-tagged substrates for self-labelling tags allow signal enhancement in microscopy.
Ghosh, S.
ORCID: https://orcid.org/0000-0003-1224-5008, Birke, R., Natarajan, A.K.
ORCID: https://orcid.org/0000-0001-7897-708X and Broichhagen, J.
ORCID: https://orcid.org/0000-0003-3084-6595
Journal of Peptide Science 31
(5): e70015.
May 2025
Gene-editing in patient and humanized-mice primary muscle stem cells rescues dysferlin expression in dysferlin-deficient muscular dystrophy.
Escobar, H.
ORCID: https://orcid.org/0000-0002-8128-7845, Di Francescantonio, S.
ORCID: https://orcid.org/0000-0002-4815-491X, Smirnova, J., Graf, R.
ORCID: https://orcid.org/0000-0002-5400-9938, Müthel, S.
ORCID: https://orcid.org/0000-0002-3525-8859, Marg, A.
ORCID: https://orcid.org/0000-0003-3673-4244, Zhogov, A., Krishna, S.
ORCID: https://orcid.org/0009-0008-8974-0721, Metzler, E.
ORCID: https://orcid.org/0000-0003-1735-6364, Petkova, M., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Kühn, R.
ORCID: https://orcid.org/0000-0003-1694-9803 and Spuler, S.
ORCID: https://orcid.org/0000-0002-0155-1117
Nature Communications 16
(1): 120.
2 January 2025
2024
Generation of effective and specific human TCRs against tumor/testis antigen NY-ESO-1 in mice with humanized T cell recognition system.
Chen, X.T.
ORCID: https://orcid.org/0000-0002-5614-1406, Leisegang, M.
ORCID: https://orcid.org/0000-0003-3692-7142, Gavvovidis, I.
ORCID: https://orcid.org/0000-0001-5644-9788, Pollack, S.M., Lorenz, F.K.M.
ORCID: https://orcid.org/0000-0001-7826-0839, Schumacher, T.N., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Blankenstein, T.
ORCID: https://orcid.org/0000-0002-3357-4321
Frontiers in Immunology 15
: 1524629.
24 December 2024
Molecular architecture of synaptic vesicles.
Kravčenko, U.
ORCID: https://orcid.org/0009-0004-7176-8444, Ruwolt, M., Kroll, J.
ORCID: https://orcid.org/0000-0003-4243-4088, Yushkevich, A.
ORCID: https://orcid.org/0000-0002-8729-9281, Zenkner, M., Ruta, J.
ORCID: https://orcid.org/0009-0007-0524-6885, Lotfy, R., Wanker, E.E.
ORCID: https://orcid.org/0000-0001-8072-1630, Rosenmund, C.
ORCID: https://orcid.org/0000-0002-3905-2444, Liu, F. and Kudryashev, M.
ORCID: https://orcid.org/0000-0003-3550-6274
Proceedings of the National Academy of Sciences of the United States of America 121
(49): e2407375121.
3 December 2024
Sociality shapes mitochondrial adaptations supporting hypoxia tolerance.
Rossi, A.
ORCID: https://orcid.org/0000-0002-8819-9813, Ruwolt, M.
ORCID: https://orcid.org/0009-0000-7220-406X, Kakouri, P., Kosten, T., Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, Puchkov, D.
ORCID: https://orcid.org/0000-0001-8341-4847, Reznick, J.
ORCID: https://orcid.org/0000-0001-7921-5466, Purfürst, B.
ORCID: https://orcid.org/0000-0002-9887-7577, Omerbašić, D.
ORCID: https://orcid.org/0000-0003-1839-4856, Méndez Aranda, D.
ORCID: https://orcid.org/0000-0001-9668-941X, Carai, G., Mastrobuoni, G.
ORCID: https://orcid.org/0000-0003-4509-1295, Hart, D.W.
ORCID: https://orcid.org/0000-0002-4592-558X, Carraro, M.
ORCID: https://orcid.org/0000-0002-4573-9306, Tommasin, L.
ORCID: https://orcid.org/0000-0002-6029-0375, Bennett, N.C.
ORCID: https://orcid.org/0000-0001-9748-2947, Bégay, V.
ORCID: https://orcid.org/0000-0002-9002-4211, Faelber, K., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Bernardi, P.
ORCID: https://orcid.org/0000-0001-9187-3736, Park, T.J.
ORCID: https://orcid.org/0000-0002-2447-2948, Kempa, S.
ORCID: https://orcid.org/0000-0002-0696-9299, Liu, F. and Lewin, G.R.
ORCID: https://orcid.org/0000-0002-2890-6352
bioRxiv
: 2024.09.30.615914.
2 October 2024
Structure-based humanization of a therapeutic antibody for multiple myeloma.
Marino, S.F.
ORCID: https://orcid.org/0000-0001-5696-9679 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Journal of Molecular Medicine 102
(9): 1151-1161.
September 2024
Structural characterization of Thogoto Virus nucleoprotein provides insights into viral RNA encapsidation and RNP assembly.
Dick, A.
ORCID: https://orcid.org/0000-0003-0580-1897, Mikirtumov, V.
ORCID: https://orcid.org/0009-0004-6849-4825, Fuchs, J., Krupp, F.
ORCID: https://orcid.org/0000-0002-0402-8647, Olal, D., Bendl, E., Sprink, T.
ORCID: https://orcid.org/0000-0002-0760-6828, Diebolder, C.
ORCID: https://orcid.org/0000-0001-7694-7362, Kudryashev, M.
ORCID: https://orcid.org/0000-0003-3550-6274, Kochs, G., Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Structure 32
(8): 1068-1078.
8 August 2024
Identification of drug-like molecules targeting the ATPase activity of dynamin-like EHD4.
Mohd, S., Oder, A., Specker, E.
ORCID: https://orcid.org/0000-0002-9471-9520, Neuenschwander, M.
ORCID: https://orcid.org/0000-0002-3114-7975, von Kries, J.P.
ORCID: https://orcid.org/0000-0003-4716-4988 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
PLoS ONE 19
(7): e0302704.
29 July 2024
Fraternal twins at work: Structures of PLD3/4 reveal mechanism for lysosomal nucleic acid breakdown.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Damme, M.
Structure 32
(6): 645-647.
6 June 2024
Pathogenic mutations of human phosphorylation sites affect protein–protein interactions.
Rrustemi, T.
ORCID: https://orcid.org/0000-0002-9075-103X, Meyer, K.
ORCID: https://orcid.org/0000-0002-8244-6887, Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Uyar, B.
ORCID: https://orcid.org/0000-0002-3170-4890, Akalin, A.
ORCID: https://orcid.org/0000-0002-0468-0117, Imami, K.
ORCID: https://orcid.org/0000-0002-7451-4982, Ishihama, Y., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Selbach, M.
ORCID: https://orcid.org/0000-0003-2454-8751
Nature Communications 15
(1): 3146.
11 April 2024
Structural insights into the activation mechanism of antimicrobial GBP1.
Weismehl, M.
ORCID: https://orcid.org/0000-0001-7583-9095, Chu, X.
ORCID: https://orcid.org/0000-0001-6801-3949, Kutsch, M.
ORCID: https://orcid.org/0000-0002-9346-2196, Lauterjung, P., Herrmann, C.
ORCID: https://orcid.org/0000-0002-1824-3647, Kudryashev, M.
ORCID: https://orcid.org/0000-0003-3550-6274 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
EMBO Journal 43
(4): 615-636.
15 February 2024
GIMAP5 deficiency reveals a mammalian ceramide-driven longevity assurance pathway.
Park, A.Y.
ORCID: https://orcid.org/0000-0002-0130-1521, Leney-Greene, M., Lynberg, M., Gabrielski, J.Q.
ORCID: https://orcid.org/0000-0002-2953-2874, Xu, X., Schwarz, B., Zheng, L., Balasubramaniyam, A.
ORCID: https://orcid.org/0000-0003-4168-8617, Ham, H.
ORCID: https://orcid.org/0000-0002-8669-6875, Chao, B., Zhang, Y., Matthews, H.F., Cui, J., Yao, Y., Kubo, S.
ORCID: https://orcid.org/0000-0001-9693-9263, Chanchu, J.M.
ORCID: https://orcid.org/0009-0009-8024-8412, Morawski, A.R.
ORCID: https://orcid.org/0000-0001-5995-0527, Cook, S.A., Jiang, P., Ravell, J.C., Cheng, Y.H., George, A., Faruqi, A.
ORCID: https://orcid.org/0000-0002-4421-3767, Pagalilauan, A.M., Bergerson, J.R.E., Ganesan, S., Chauvin, S.D.
ORCID: https://orcid.org/0000-0003-0232-751X, Aluri, J., Edwards-Hicks, J., Bohrnsen, E., Tippett, C., Omar, H., Xu, L., Butcher, G.W., Pascall, J., Karakoc-Aydiner, E., Kiykim, A., Maecker, H.
ORCID: https://orcid.org/0000-0003-0795-9946, Tezcan, İ., Esenboga, S., Heredia, R.J., Akata, D., Tekin, S.
ORCID: https://orcid.org/0000-0003-2641-6293, Kara, A.
ORCID: https://orcid.org/0000-0001-7244-5031, Kuloglu, Z., Unal, E., Kendirli, T., Dogu, F., Karabiber, E., Atkinson, T.P., Cochet, C., Filhol, O.
ORCID: https://orcid.org/0000-0003-1964-7958, Bosio, C.M., Davis, M.M.
ORCID: https://orcid.org/0000-0001-6868-657X, Lifton, R.P., Pearce, E.L.
ORCID: https://orcid.org/0000-0001-5592-5439, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Aytekin, C.
ORCID: https://orcid.org/0000-0002-2921-5270, Şahin, G.E., Aksu, A.Ü., Uzel, G., Koneti Rao, V.
ORCID: https://orcid.org/0000-0002-7881-6902, Sari, S., Boztug, K., Cagdas, D., Haskologlu, S.
ORCID: https://orcid.org/0000-0002-2668-0441, Ikinciogullari, A., Schwefel, D., Vilarinho, S., Baris, S.
ORCID: https://orcid.org/0000-0002-4730-9422, Ozen, A., Su, H.C.
ORCID: https://orcid.org/0000-0002-5582-9110 and Lenardo, M.J.
ORCID: https://orcid.org/0000-0003-1584-468X
Nature Immunology 25
(2): 282-293.
February 2024
Structural analysis of PLD3 reveals insights into the mechanism of lysosomal 5' exonuclease-mediated nucleic acid degradation.
Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Cappel, C., Cremer, N., Hoffmann, P., Koudelka, T.
ORCID: https://orcid.org/0009-0008-2895-6051, Tholey, A., Heinemann, U.
ORCID: https://orcid.org/0000-0002-8191-3850, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Damme, M.
ORCID: https://orcid.org/0000-0002-9699-9351
Nucleic Acids Research 52
(1): 370-384.
11 January 2024
Topological reaction coordinate captures the folding transition state ensemble in a pierced lasso protein.
Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036 and Haglund, E.
ORCID: https://orcid.org/0000-0002-6629-2793
Journal of Physical Chemistry B 128
(1): 117-124.
11 January 2024
2023
Transcriptional reprogramming by mutated IRF4 in lymphoma.
Schleussner, N.
ORCID: https://orcid.org/0009-0001-3549-5600, Cauchy, P.
ORCID: https://orcid.org/0000-0002-0659-0799, Franke, V.
ORCID: https://orcid.org/0000-0003-3606-6792, Giefing, M., Fornes, O.
ORCID: https://orcid.org/0000-0002-5969-3054, Vankadari, N.
ORCID: https://orcid.org/0000-0001-9363-080X, Assi, S.A., Costanza, M.
ORCID: https://orcid.org/0000-0002-8959-1083, Weniger, M.A., Akalin, A.
ORCID: https://orcid.org/0000-0002-0468-0117, Anagnostopoulos, I.
ORCID: https://orcid.org/0000-0002-5043-6043, Bukur, T., Casarotto, M.G.
ORCID: https://orcid.org/0000-0002-0571-7671, Damm, F.
ORCID: https://orcid.org/0000-0001-5553-1173, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Edginton-White, B., Gebhardt, J.C.M.
ORCID: https://orcid.org/0000-0003-1900-600X, Grau, M., Grunwald, S.
ORCID: https://orcid.org/0000-0003-3978-6277, Hansmann, M.L., Hartmann, S.
ORCID: https://orcid.org/0000-0003-3424-1091, Huber, L., Kärgel, E., Lusatis, S., Noerenberg, D., Obier, N., Pannicke, U.
ORCID: https://orcid.org/0000-0002-0929-1794, Fischer, A.
ORCID: https://orcid.org/0000-0002-7145-2544, Reisser, A., Rosenwald, A., Schwarz, K.
ORCID: https://orcid.org/0000-0003-3178-5990, Sundararaj, S., Weilemann, A.
ORCID: https://orcid.org/0009-0001-1340-6486, Winkler, W.
ORCID: https://orcid.org/0000-0001-8807-9259, Xu, W., Lenz, G.
ORCID: https://orcid.org/0000-0002-4728-1693, Rajewsky, K.
ORCID: https://orcid.org/0000-0002-6633-6370, Wasserman, W.W.
ORCID: https://orcid.org/0000-0001-6098-6412, Cockerill, P.N.
ORCID: https://orcid.org/0000-0002-4410-8174, Scheidereit, C.
ORCID: https://orcid.org/0000-0002-0446-6129, Siebert, R., Küppers, R., Grosschedl, R.
ORCID: https://orcid.org/0000-0002-0058-1250, Janz, M.
ORCID: https://orcid.org/0000-0002-1127-0044, Bonifer, C.
ORCID: https://orcid.org/0000-0002-4267-0825 and Mathas, S.
ORCID: https://orcid.org/0000-0001-9626-1413
Nature Communications 14
(1): 6947.
7 November 2023
MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange.
Abualrous, E.T.
ORCID: https://orcid.org/0000-0001-9582-9089, Stolzenberg, S., Sticht, J.
ORCID: https://orcid.org/0000-0002-4307-4726, Wieczorek, M., Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Günther, M., Dähn, S., Boesen, B.B., Calvo, M.M.
ORCID: https://orcid.org/0009-0008-9179-127X, Biese, C., Kuppler, F., Medina-García, Á., Álvaro-Benito, M.
ORCID: https://orcid.org/0000-0002-6019-3567, Höfer, T.
ORCID: https://orcid.org/0000-0003-3560-8780, Noé, F.
ORCID: https://orcid.org/0000-0003-4169-9324 and Freund, C.
ORCID: https://orcid.org/0000-0001-7416-8226
Nature Chemical Biology 19
(10): 1196-1204.
October 2023
A multimorphic mutation in IRF4 causes human autosomal dominant combined immunodeficiency.
Fornes, O., Jia, A., Kuehn, H.S., Min, Q., Pannicke, U., Schleussner, N.
ORCID: https://orcid.org/0009-0001-3549-5600, Thouenon, R., Yu, Z., de Los Angeles Astbury, M., Biggs, C.M., Galicchio, M., Garcia-Campos, J.A., Gismondi, S., Gonzalez Villarreal, G., Hildebrand, K.J., Hönig, M., Hou, J., Moshous, D., Pittaluga, S., Qian, X., Rozmus, J., Schulz, A.S., Staines-Boone, A.T., Sun, B., Sun, J., Uwe, S., Venegas-Montoya, E., Wang, W., Wang, X., Ying, W., Zhai, X., Zhou, Q., Akalin, A.
ORCID: https://orcid.org/0000-0002-0468-0117, André, I., Barth, T.F.E., Baumann, B., Brüstle, A., Burgio, G., Bustamante, J.C., Casanova, J.L., Casarotto, M.G., Cavazzana, M., Chentout, L., Cockburn, I.A., Costanza, M.
ORCID: https://orcid.org/0000-0002-8959-1083, Cui, C., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Del Bel, K.L., Eibel, H., Feng, X., Franke, V.
ORCID: https://orcid.org/0000-0003-3606-6792, Gebhardt, J.C.M., Götz, A., Grunwald, S.
ORCID: https://orcid.org/0000-0003-3978-6277, Hoareau, B., Hughes, T.R., Jacobsen, E.M., Janz, M.
ORCID: https://orcid.org/0000-0002-1127-0044, Jolma, A., Lagresle-Peyrou, C., Lai, N., Li, Y., Lin, S., Lu, H.Y., Lugo-Reyes, S.O., Meng, X., Möller, P., Moreno-Corona, N., Niemela, J.E., Novakovsky, G., Perez-Caraballo, J.J., Picard, C., Poggi, L., Puig-Lombardi, M.E., Randall, K.L., Reisser, A., Schmitt, Y., Seneviratne, S., Sharma, M., Stoddard, J., Sundararaj, S., Sutton, H., Tran, L.Q., Wang, Y., Wasserman, W.W., Wen, Z., Winkler, W.
ORCID: https://orcid.org/0000-0001-8807-9259, Xiong, E., Yang, A.W.H., Yu, M., Zhang, L., Zhang, H., Zhao, Q., Zhen, X., Enders, A., Kracker, S., Martinez-Barricarte, R., Mathas, S.
ORCID: https://orcid.org/0000-0001-9626-1413, Rosenzweig, S.D., Schwarz, K., Turvey, S.E. and Wang, J.Y.
Science Immunology 8
(79): eade7953.
January 2023
Development of selective inhibitors of phosphatidylinositol 3-kinase C2α.
Lo, W.T., Belabed, H., Kücükdisli, M., Metag, J., Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Prokofeva, P., Ohashi, Y.
ORCID: https://orcid.org/0000-0002-2288-130X, Horatscheck, A.
ORCID: https://orcid.org/0000-0001-6485-6391, Cirillo, D.
ORCID: https://orcid.org/0000-0001-5133-0702, Krauss, M., Schmied, C.
ORCID: https://orcid.org/0000-0003-2058-1124, Neuenschwander, M.
ORCID: https://orcid.org/0000-0002-3114-7975, von Kries, J.P.
ORCID: https://orcid.org/0000-0003-4716-4988, Médard, G.
ORCID: https://orcid.org/0000-0002-4782-4029, Kuster, Be.
ORCID: https://orcid.org/0000-0002-9094-1677, Perisic, O., Williams, R.L.
ORCID: https://orcid.org/0000-0001-7754-4207, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Payrastre, B.
ORCID: https://orcid.org/0000-0002-8693-0190, Severin, S., Nazaré, M.
ORCID: https://orcid.org/0000-0002-1602-2330 and Haucke, V.
ORCID: https://orcid.org/0000-0003-3119-6993
Nature Chemical Biology 19
(1): 18-27.
January 2023
2022
Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.
Melo, A.A., Sprink, T.
ORCID: https://orcid.org/0000-0002-0760-6828, Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Vázquez-Sarandeses, E., van Hoorn, C.
ORCID: https://orcid.org/0000-0002-1319-847X, Mohd, S., Loerke, J.
ORCID: https://orcid.org/0000-0002-3424-8536, Spahn, C.M.T. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Nature Communications 13
(1): 7641.
10 December 2022
Structural insights into crista junction formation by the Mic60-Mic19 complex.
Bock-Bierbaum, T.
ORCID: https://orcid.org/0000-0003-0843-2716, Funck, K., Wollweber, F., Lisicki, E.
ORCID: https://orcid.org/0000-0001-5012-8377, von der Malsburg, K., von der Malsburg, A., Laborenz, J., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Hessenberger, M.
ORCID: https://orcid.org/0000-0003-3021-1100, Jungbluth, S., Bernert, C., Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, Riedel, D., Lilie, H., Jakobs, S., van der Laan, M. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Science Advances 8
(35): eabo4946.
2 September 2022
GIMAP6 regulates autophagy, immune competence, and inflammation in mice and humans.
Yao, Y.
ORCID: https://orcid.org/0000-0002-8890-2409, Du Jiang, P.
ORCID: https://orcid.org/0000-0002-9900-8277, Chao, B.N.
ORCID: https://orcid.org/0000-0002-0355-2332, Cagdas, D.
ORCID: https://orcid.org/0000-0003-2213-4627, Kubo, S.
ORCID: https://orcid.org/0000-0001-9693-9263, Balasubramaniyam, A.
ORCID: https://orcid.org/0000-0003-4168-8617, Zhang, Y.
ORCID: https://orcid.org/0000-0002-6904-0372, Shadur, B.
ORCID: https://orcid.org/0000-0003-0245-894X, NaserEddin, A.
ORCID: https://orcid.org/0000-0001-6995-3262, Folio, L.R., Schwarz, B.
ORCID: https://orcid.org/0000-0002-5894-953X, Bohrnsen, E.
ORCID: https://orcid.org/0000-0003-4327-5242, Zheng, L.
ORCID: https://orcid.org/0000-0002-8838-8665, Lynberg, M.
ORCID: https://orcid.org/0000-0003-1371-3002, Gottlieb, S.
ORCID: https://orcid.org/0000-0003-0550-4761, Leney-Greene, M.A.
ORCID: https://orcid.org/0000-0002-3259-1728, Park, A.Y.
ORCID: https://orcid.org/0000-0002-0130-1521, Tezcan, I.
ORCID: https://orcid.org/0000-0001-7257-4554, Akdogan, A., Gocmen, R.
ORCID: https://orcid.org/0000-0002-0223-9336, Onder, S.
ORCID: https://orcid.org/0000-0002-5523-0669, Rosenberg, A., Soilleux, E.J.
ORCID: https://orcid.org/0000-0002-4032-7249, Johnson, E.
ORCID: https://orcid.org/0000-0001-8435-9472, Jackson, P.K.
ORCID: https://orcid.org/0000-0002-1742-2539, Demeter, J., Chauvin, S.D.
ORCID: https://orcid.org/0000-0003-0232-751X, Paul, F.
ORCID: https://orcid.org/0000-0001-5181-3122, Selbach, M.
ORCID: https://orcid.org/0000-0003-2454-8751, Bulut, H.
ORCID: https://orcid.org/0000-0003-0262-6296, Clatworthy, M.R.
ORCID: https://orcid.org/0000-0002-3340-9828, Tuong, Z.K.
ORCID: https://orcid.org/0000-0002-6735-6808, Zhang, H., Stewart, B.J.
ORCID: https://orcid.org/0000-0003-4522-0085, Bosio, C.M.
ORCID: https://orcid.org/0000-0002-7332-9611, Stepensky, P.
ORCID: https://orcid.org/0000-0002-4923-3660, Clare, S.
ORCID: https://orcid.org/0000-0001-9368-6037, Ganesan, S.
ORCID: https://orcid.org/0000-0003-1132-2016, Pascall, J.C.
ORCID: https://orcid.org/0000-0002-9506-1441, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Butcher, G.W.
ORCID: https://orcid.org/0000-0002-3423-7124, McMichael, A.J.
ORCID: https://orcid.org/0000-0002-9101-7478, Simon, A.K.
ORCID: https://orcid.org/0000-0002-4077-7995 and Lenardo, M.J.
ORCID: https://orcid.org/0000-0003-1584-468X
Journal of Experimental Medicine 219
(6): e20201405.
6 June 2022
Competitively disrupting the neutrophil-specific receptor-autoantigen CD177:proteinase 3 membrane complex reduces anti-PR3 antibody-induced neutrophil activation.
Marino, S.F.
ORCID: https://orcid.org/0000-0001-5696-9679, Jerke, U., Rolle, S.
ORCID: https://orcid.org/0000-0002-1909-687X, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Kettritz, R.
ORCID: https://orcid.org/0000-0001-5821-6718
Journal of Biological Chemistry 298
(3): 101598.
March 2022
Structural basis of phosphatidylinositol 3-kinase C2α function.
Lo, W.T.
ORCID: https://orcid.org/0000-0001-7904-6834, Zhang, Y., Vadas, O.
ORCID: https://orcid.org/0000-0003-3511-6479, Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Gulluni, F., De Santis, M.C.
ORCID: https://orcid.org/0000-0003-2785-0665, Zagar, A.V., Stephanowitz, H., Hirsch, E., Liu, F.
ORCID: https://orcid.org/0000-0002-2358-549X, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Kudryashev, M.
ORCID: https://orcid.org/0000-0003-3550-6274 and Haucke, V.
ORCID: https://orcid.org/0000-0003-3119-6993
Nature Structural & Molecular Biology 29
(3): 218-228.
March 2022
SPFH protein cage - one ring to rule them all.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Lewin, G.R.
ORCID: https://orcid.org/0000-0002-2890-6352
Cell Research 32
(2): 117-118.
February 2022
SMOG 2 and OpenSMOG: extending the limits of structure-based models.
de Oliveira, A.B., Contessoto, V.G., Hassan, A., Byju, S., Wang, A., Wang, Y., Dodero-Rojas, E., Mohanty, U., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Onuchic, J.N. and Whitford, P.C.
ORCID: https://orcid.org/0000-0001-7104-2265
Protein Science 31
(1): 158-172.
January 2022
2021
Lysine acetylation regulates the interaction between proteins and membranes.
Okada, A.K.
ORCID: https://orcid.org/0000-0001-8338-9557, Teranishi, K., Ambroso, M.R., Isas, J.M., Vazquez-Sarandeses, E., Lee, J.Y.
ORCID: https://orcid.org/0000-0001-6616-5594, Melo, A.A., Pandey, P., Merken, D., Berndt, L., Lammers, M., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Chang, K., Haworth, I.S.
ORCID: https://orcid.org/0000-0002-3873-0899 and Langen, R.
Nature Communications 12
(1): 6466.
9 November 2021
A simple pressure-assisted method for MicroED specimen preparation.
Zhao, J.
ORCID: https://orcid.org/0000-0001-8444-6883, Xu, H.
ORCID: https://orcid.org/0000-0002-8271-3906, Lebrette, H., Carroni, M.
ORCID: https://orcid.org/0000-0002-7697-6427, Taberman, H.
ORCID: https://orcid.org/0000-0001-7595-4608, Högbom, M. and Zou, X.
ORCID: https://orcid.org/0000-0001-6748-6656
Nature Communications 12
(1): 5036.
19 August 2021
Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.
Ganichkin, O.M., Vancraenenbroeck, R.
ORCID: https://orcid.org/0000-0003-2685-2749, Rosenblum, G., Hofmann, H.
ORCID: https://orcid.org/0000-0003-1669-3158, Mikhailov, A.S.
ORCID: https://orcid.org/0000-0002-2416-8401, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036
Proceedings of the National Academy of Sciences of the United States of America 118
(28): e2101144118.
13 July 2021
Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily.
Liu, J., Tassinari, M., Souza, D.P., Naskar, S., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Bohuszewicz, O., Buck, M., Williams, T.A., Baum, B. and Low, H.H.
Cell 184
(14): 3660-3673.
8 July 2021
The ARFRP1-dependent Golgi scaffolding protein GOPC is required for insulin secretion from pancreatic β-cells.
Wilhelmi, Ilka, Grunwald, S.
ORCID: https://orcid.org/0000-0003-3978-6277, Gimber, N.
ORCID: https://orcid.org/0000-0001-9456-3063, Popp, O.
ORCID: https://orcid.org/0000-0001-6240-4666, Dittmar, G.
ORCID: https://orcid.org/0000-0003-3647-8623, Arumughan, A., Wanker, E.E.
ORCID: https://orcid.org/0000-0001-8072-1630, Laeger, T.
ORCID: https://orcid.org/0000-0002-2763-0497, Schmoranzer, J., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Schümann, A.
ORCID: https://orcid.org/0000-0002-4113-4377
Molecular Metabolism 45
: 101151.
March 2021
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition).
Klionsky, D.J., Abdel-Aziz, A.K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M.H., Abudu, Y.P., Acevedo-Arozena, A., Adamopoulos, I.E., Adeli, K., Adolph, T.E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B.B., Agnello, M., Agostinis, P., Agrewala, J.N., Agrotis, A., Aguilar, P.V., Ahmad, S.T., Ahmed, Z.M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H.A., Al-Abd, A.M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M.A., Alberti, S., Alcocer-Gómez, E., Alessandri, C., Ali, M., Alim Al-Bari, M.A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G.D., Altan-Bonnet, N., Altieri, D.C., Álvarez, E.M.C., Alves, S., Alves da Costa, C., Alzaharna, M.M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A.O., Ammanathan, V., An, Z., Andersen, S.U., Andrabi, S.A., Andrade-Silva, M., Andres, A.M., Angelini, S., Ann, D., Anozie, U.C., Ansari, M.Y., Antas, P., Antebi, A., Antón, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araújo, W.L., Araya, J., Arden, C., Arévalo, M.A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A.R., Armstrong-James, D., Arnauné-Pelloquin, L., Aroca, A., Arroyo, D.S., Arsov, I., Artero, R., Asaro, D.M.L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A.G., Au, A.K., Auberger, P., Auner, H.W., Aurelian, L., Autelli, R., Avagliano, L., Ávalos, Y., Aveic, S., Aveleira, C.A., Avin-Wittenberg, T., Aydin, Y., Ayton, S., Ayyadevara, S., Azzopardi, M., Baba, M.u, Backer, J.M., Backues, S.K., Bae, D.H., Bae, O.N., Bae, S.H., Baehrecke, E.H., Baek, A., Baek, S.H., Baek, S.H., Bagetta, G., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bai, Y., Bairagi, N., Baksi, S., Balbi, T., Baldari, C.T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banerjee, S., Bánréti, A., Bao, Y., Baptista, M.S., Baracca, A., Barbati, C., Bargiela, A., Barilà, D., Barlow, P.G., Barmada, S.J., Barreiro, E., Barreto, G.E., Bartek, J., Bartel, B., Bartolome, A., Barve, G.R., Basagoudanavar, S.H., Bassham, D.C., Bast, R.C., Basu, A., Batoko, H., Batten, I., Baulieu, E.E., Baumgarner, B.L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L.R.G., Beck, G.R., Beers, M.F., Begun, J., Behrends, C., Behrens, G.M.N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touzé, N., Bellarosa, C., Belleudi, F., Belló Pérez, M., Bello-Morales, R., Beltran, J.S.O., Beltran, S., Benbrook, D.M., Bendorius, M., Benitez, B.A., Benito-Cuesta, I., Bensalem, J., Berchtold, M.W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C.G., Besteiro, S., Betin, V.M., Beyaert, R., Bezbradica, J.S., Bhaskar, K., Bhatia-Kissova, I., Bhattacharya, R., Bhattacharya, S., Bhattacharyya, S., Bhuiyan, M.S., Bhutia, S.K., Bi, L., Bi, X., Biden, T.J., Bijian, K., Billes, V.A., Binart, N., Bincoletto, C., Birgisdottir, A.B., Bjorkoy, G., Blanco, G., Blas-Garcia, A., Blasiak, J., Blomgran, R., Blomgren, K., Blum, J.S., Boada-Romero, E., Boban, M., Boesze-Battaglia, K., Boeuf, P., Boland, B., Bomont, P., Bonaldo, P., Bonam, S.R., Bonfili, L., Bonifacino, J.S., Boone, B.A., Bootman, M.D., Bordi, M., Borner, C., Bornhauser, B.C., Borthakur, G., Bosch, J., Bose, S., Botana, L.M., Botas, J., Boulanger, C.M., Boulton, M.E., Bourdenx, M., Bourgeois, B., Bourke, N.M., Bousquet, G., Boya, P., Bozhkov, P.V., Bozi, L.H.M., Bozkurt, T.O., Brackney, D.E., Brandts, C.H., Braun, R.J., Braus, G.H., Bravo-Sagua, R., Bravo-San Pedro, J.M., Brest, P., Bringer, M.A., Briones-Herrera, A., Broaddus, V.C., Brodersen, P., Brodsky, J.L., Brody, S.L., Bronson, P.G., Bronstein, J.M., Brown, C.N., Brown, R.E., Brum, P.C., Brumell, J.H., Brunetti-Pierri, N., Bruno, D., Bryson-Richardson, R.J., Bucci, C., Buchrieser, C., Bueno, M., Buitrago-Molina, L.E., Buraschi, S., Buch, S., Buchan, J.R., Buckingham, E.M., Budak, H., Budini, M., Bultynck, G., Burada, F., Burgoyne, J.R., Burón, M.I., Bustos, V., Büttner, S., Butturini, E., Byrd, A., Cabas, I., Cabrera-Benitez, S., Cadwell, K., Cai, J., Cai, L., Cai, Q., Cairó, M., Calbet, J.A., Caldwell, G.A., Caldwell, K.A., Call, J.A., Calvani, R., Calvo, A.C., Calvo-Rubio Barrera, M., Camara, N.O., Camonis, J.H., Camougrand, N., Campanella, M., Campbell, E.M., Campbell-Valois, F.X., Campello, S., Campesi, I., Campos, J.C., Camuzard, O., Cancino, J., Candido de Almeida, D., Canesi, L., Caniggia, I., Canonico, B., Cantí, C., Cao, B., Caraglia, M., Caramés, B., Carchman, E.H., Cardenal-Muñoz, E., Cardenas, C., Cardenas, L., Cardoso, S.M., Carew, J.S., Carle, G.F., Carleton, G., Carloni, S., Carmona-Gutierrez, D., Carneiro, L.A., Carnevali, O., Carosi, J.M., Carra, S., Carrier, A., Carrier, L., Carroll, B., Carter, A.B., Carvalho, A.N., Casanova, M., Casas, C., Casas, J., Cassioli, C., Castillo, E.F., Castillo, K., Castillo-Lluva, S., Castoldi, F., Castori, M., Castro, A.F., Castro-Caldas, M., Castro-Hernandez, J., Castro-Obregon, S., Catz, S.D., Cavadas, C., Cavaliere, F., Cavallini, G., Cavinato, M., Cayuela, M.L., Cebollada Rica, P., Cecarini, V., Cecconi, F., Cechowska-Pasko, M., Cenci, S., Ceperuelo-Mallafré, V., Cerqueira, J.J., Cerutti, J.M., Cervia, D., Cetintas, V.B., Cetrullo, S., Chae, H.J., Chagin, A.S., Chai, C.Y., Chakrabarti, G., Chakrabarti, O., Chakraborty, T., Chakraborty, T., Chami, M., Chamilos, G., Chan, D.W., Chan, E.Y.W., Chan, E.D., Chan, H.Y.E., Chan, H.H., Chan, H., Chan, M.T.V., Chan, Y.S., Chandra, P.K., Chang, C.P., Chang, C., Chang, H.C., Chang, K., Chao, J., Chapman, T., Charlet-Berguerand, N., Chatterjee, S., Chaube, S.K., Chaudhary, A., Chauhan, S., Chaum, E., Checler, F., Cheetham, M.E., Chen, C.S., Chen, G.C., Chen, J.F., Chen, L.L., Chen, L., Chen, L., Chen, M., Chen, M.K., Chen, N., Chen, Q., Chen, R.H., Chen, S., Chen, W., Chen, W., Chen, X.M., Chen, X.W., Chen, X., Chen, Y., Chen, Y.G., Chen, Y., Chen, Y., Chen, Y.J., Chen, Y.Q., Chen, Z.S., Chen, Z., Chen, Z.H., Chen, Z.J., Chen, Z., Cheng, H., Cheng, J., Cheng, S.Y., Cheng, W., Cheng, X., Cheng, X.T., Cheng, Y., Cheng, Z., Chen, Z., Cheong, H., Cheong, J.K., Chernyak, B.V., Cherry, S., Cheung, C.F.R., Cheung, C.H.A., Cheung, K.H., Chevet, E., Chi, R.J., Chiang, A.K.S., Chiaradonna, F., Chiarelli, R., Chiariello, M., Chica, N., Chiocca, S., Chiong, M., Chiou, S.H., Chiramel, A.I., Chiurchiù, V., Cho, D.H., Choe, S.K., Choi, A.M.K., Choi, M.E., Choudhury, K.R., Chow, N.S., Chu, C.T., Chua, J.P., Chua, J.J.E., Chung, H., Chung, K.P., Chung, S., Chung, S.H., Chung, Y.L., Cianfanelli, V., Ciechomska, I.A., Cifuentes, M., Cinque, L., Cirak, S., Cirone, M., Clague, M.J., Clarke, R., Clementi, E., Coccia, E.M., Codogno, P., Cohen, E., Cohen, M.M, Colasanti, T., Colasuonno, F., Colbert, R.A., Colell, A., Čolić, M., Coll, N.S., Collins, M.O., Colombo, M.I., Colón-Ramos, D.A., Combaret, L., Comincini, S., Cominetti, M.R., Consiglio, A., Conte, A., Conti, F., Contu, V.R., Cookson, M.R., Coombs, K.M., Coppens, I., Corasaniti, M.T., Corkery, D.P., Cordes, N., Cortese, K., Costa, M.D.C., Costantino, S., Costelli, P., Coto-Montes, A., Crack, P.J., Crespo, J.L., Criollo, A., Crippa, V., Cristofani, R., Csizmadia, T., Cuadrado, A., Cui, B., Cui, J., Cui, Y., Cui, Y., Culetto, E., Cumino, A.C., Cybulsky, A.V., Czaja, M.J., Czuczwar, S.J., D'Adamo, S., D'Amelio, M., D'Arcangelo, D., D'Lugos, A.C., D'Orazi, G., da Silva, J.A., Dafsari, H.S., Dagda, R.K., Dagdas, Y., Daglia, M., Dai, X., Dai, Y., Dai, Y., Dal Col, J., Dalhaimer, P., Dalla Valle, L., Dallenga, T., Dalmasso, G., Damme, M., Dando, I., Dantuma, N.P., Darling, A.L., Das, H., Dasarathy, S., Dasari, S.K., Dash, S., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Dauphinee, A.N., Davies, J.S., Dávila, V.A., Davis, R.J., Davis, T., Dayalan Naidu, S., De Amicis, F., De Bosscher, K., De Felice, F., De Franceschi, L., De Leonibus, C., de Mattos Barbosa, M.G., De Meyer, G.R.Y., De Milito, A., De Nunzio, C., De Palma, C., De Santi, M., De Virgilio, C., De Zio, D., Debnath, J., DeBosch, B.J., Decuypere, J.P., Deehan, M.A., Deflorian, G., DeGregori, J., Dehay, B., Del Rio, G., Delaney, J.R., Delbridge, L.M.D., Delorme-Axford, E., Delpino, M.V., Demarchi, F., Dembitz, V., Demers, N.D., Deng, H., Deng, Z., Dengjel, J., Dent, P., Denton, D., DePamphilis, M.L., Der, C.J., Deretic, V., Descoteaux, A., Devis, L., Devkota, S., Devuyst, O., Dewson, G., Dharmasivam, M., Dhiman, R., di Bernardo, D., Di Cristina, M., Di Domenico, F., Di Fazio, P., Di Fonzo, A., Di Guardo, G., Di Guglielmo, G.M., Di Leo, L., Di Malta, C., Di Nardo, A., Di Rienzo, M., Di Sano, F., Diallinas, G., Diao, J., Diaz-Araya, G., Díaz-Laviada, I., Dickinson, J.M., Diederich, M., Dieudé, M., Dikic, I., Ding, S., Ding, W.X., Dini, L., Dinić, J., Dinic, M., Dinkova-Kostova, A.T., Dionne, M.S., Distler, J.H.W., Diwan, A., Dixon, I.M.C., Djavaheri-Mergny, M., Dobrinski, I., Dobrovinskaya, O., Dobrowolski, R., Dobson, R.C.J., Đokić, J., Dokmeci Emre, S., Donadelli, M., Dong, B., Dong, X., Dong, Z., Dorn Ii, G.W., Dotsch, V., Dou, H., Dou, J., Dowaidar, M., Dridi, S., Drucker, L., Du, A., Du, C., Du, G., Du, H.N., Du, L.L., du Toit, A., Duan, S.B., Duan, X., Duarte, S.P., Dubrovska, A., Dunlop, E.A., Dupont, N., Durán, R.V., Dwarakanath, B.S., Dyshlovoy, S.A., Ebrahimi-Fakhari, D., Eckhart, L., Edelstein, C.L., Efferth, T., Eftekharpour, E., Eichinger, L., Eid, N., Eisenberg, T., Eissa, N.T., Eissa, S., Ejarque, M., El Andaloussi, A., El-Hage, N., El-Naggar, S., Eleuteri, A.M., El-Shafey, E.S., Elgendy, M., Eliopoulos, A.G., Elizalde, M.M., Elks, P.M., Elsasser, H.P., Elsherbiny, E.S., Emerling, B.M., Emre, N.C.T., Eng, C.H., Engedal, N., Engelbrecht, A.M., Engelsen, A.S.T., Enserink, J.M., Escalante, R., Esclatine, A., Escobar-Henriques, M., Eskelinen, E.L., Espert, L., Eusebio, M.O., Fabrias, G., Fabrizi, C., Facchiano, A., Facchiano, F., Fadeel, B., Fader, C., Faesen, A.C., Fairlie, W.D., Falcó, A., Falkenburger, B.H., Fan, D., Fan, J., Fan, Y., Fang, E.F., Fang, Y., Fang, Y., Fanto, M., Farfel-Becker, T., Faure, M., Fazeli, G., Fedele, A.O., Feldman, A.M., Feng, D., Feng, J., Feng, L., Feng, Y., Feng, Y., Feng, W., Fenz Araujo, T., Ferguson, T.A., Fernández, A.F., Fernandez-Checa, J.C., Fernández-Veledo, S., Fernie, A.R., Ferrante, A.W., Ferraresi, A., Ferrari, M.F., Ferreira, J.C.B., Ferro-Novick, S., Figueras, A., Filadi, R., Filigheddu, N., Filippi-Chiela, E., Filomeni, G., Fimia, G.M., Fineschi, V., Finetti, F., Finkbeiner, S., Fisher, E.A., Fisher, P.B., Flamigni, F., Fliesler, S.J., Flo, T.H., Florance, I., Florey, O., Florio, T., Fodor, E., Follo, C., Fon, E.A., Forlino, A., Fornai, F., Fortini, P., Fracassi, A., Fraldi, A., Franco, B., Franco, R., Franconi, F., Frankel, L.B., Friedman, S.L., Fröhlich, L.F., Frühbeck, G., Fuentes, J.M., Fujiki, Y., Fujita, N., Fujiwara, Y., Fukuda, M., Fulda, S., Furic, L., Furuya, N., Fusco, C., Gack, M.U., Gaffke, L., Galadari, S., Galasso, A., Galindo, M.F., Gallolu Kankanamalage, S., Galluzzi, L., Galy, V., Gammoh, N., Gan, B., Ganley, I.G., Gao, F., Gao, H., Gao, M., Gao, P., Gao, S.J., Gao, W., Gao, X., Garcera, A., Garcia, M.N., Garcia, V.E., García-Del Portillo, F., Garcia-Escudero, V., Garcia-Garcia, A., Garcia-Macia, M., García-Moreno, D., Garcia-Ruiz, C., García-Sanz, P., Garg, A.D., Gargini, R., Garofalo, T., Garry, R.F., Gassen, N.C., Gatica, D., Ge, L., Ge, W., Geiss-Friedlander, R., Gelfi, C., Genschik, P., Gentle, I.E., Gerbino, V., Gerhardt, C., Germain, K., Germain, M., Gewirtz, D.A., Ghasemipour Afshar, E., Ghavami, S., Ghigo, A., Ghosh, M., Giamas, G., Giampietri, C., Giatromanolaki, A., Gibson, G.E., Gibson, S.B., Ginet, V., Giniger, E., Giorgi, C., Girao, H., Girardin, S.E., Giridharan, M., Giuliano, S., Giulivi, C., Giuriato, S., Giustiniani, J., Gluschko, A., Goder, V., Goginashvili, A., Golab, J., Goldstone, D.C., Golebiewska, A., Gomes, L.R., Gomez, R., Gómez-Sánchez, R., Gomez-Puerto, M.C., Gomez-Sintes, R., Gong, Q., Goni, F.M., González-Gallego, J., Gonzalez-Hernandez, T., Gonzalez-Polo, R.A., Gonzalez-Reyes, J.A., González-Rodríguez, P., Goping, I.S., Gorbatyuk, M.S., Gorbunov, N.V., Görgülü, K., Gorojod, R.M., Gorski, S.M., Goruppi, S., Gotor, C., Gottlieb, R.A., Gozes, I., Gozuacik, D., Graef, M., Gräler, M.H., Granatiero, V., Grasso, D., Gray, J.P., Green, D.R., Greenhough, A., Gregory, S.L., Griffin, E.F., Grinstaff, M.W., Gros, F., Grose, C., Gross, A.S., Gruber, F., Grumati, P., Grune, T., Gu, X., Guan, J.L., Guardia, C.M., Guda, K., Guerra, F., Guerri, C., Guha, P., Guillén, C., Gujar, S., Gukovskaya, A., Gukovsky, I., Gunst, J., Günther, A., Guntur, A.R., Guo, C., Guo, C., Guo, H., Guo, L.W., Guo, M., Gupta, P., Gupta, S.K., Gupta, S., Gupta, V.B., Gupta, V., Gustafsson, A.B., Gutterman, D.D., H B, R., Haapasalo, A., Haber, J.E., Hać, A., Hadano, S., Hafrén, A.J., Haidar, M., Hall, B.S., Halldén, G., Hamacher-Brady, A., Hamann, A., Hamasaki, M., Han, W., Hansen, M., Hanson, P.I., Hao, Z., Harada, M., Harhaji-Trajkovic, L., Hariharan, N., Haroon, N., Harris, J., Hasegawa, T., Hasima Nagoor, N., Haspel, J.A., Haucke, V., Hawkins, W.D., Hay, B.A., Haynes, C.M., Hayrabedyan, S.B., Hays, T.S., He, C., He, Q., He, R.R., He, Y.W., He, Y.Y., Heakal, Y., Heberle, A.M., Hejtmancik, J.F., Helgason, G.V., Henkel, V., Herb, M., Hergovich, A., Herman-Antosiewicz, A., Hernández, A., Hernandez, C., Hernandez-Diaz, S., Hernandez-Gea, V., Herpin, A., Herreros, J., Hervás, J.H., Hesselson, D., Hetz, C., Heussler, V.T., Higuchi, Y., Hilfiker, S., Hill, J.A., Hlavacek, W.S., Ho, E.A., Ho, I.H.T., Ho, P.W.L., Ho, S.L., Ho, W.Y., Hobbs, G.A., Hochstrasser, M., Hoet, P.H.M., Hofius, D., Hofman, P., Höhn, A., Holmberg, C.I., Hombrebueno, J.R., Yi-Ren Hong, C.W.H., Hooper, L.V., Hoppe, T., Horos, R., Hoshida, Y., Hsin, I.L., Hsu, H.Y., Hu, B., Hu, D., Hu, L.F., Hu, M.C., Hu, R., Hu, W., Hu, Y.C., Hu, Z.W., Hua, F., Hua, J., Hua, Y., Huan, C., Huang, C., Huang, C., Huang, C., Huang, C., Huang, H., Huang, K., Huang, M.L.H., Huang, R., Huang, S., Huang, T., Huang, X., Huang, Y.J., Huber, T.B., Hubert, V., Hubner, C.A., Hughes, S.M., Hughes, W.E., Humbert, M., Hummer, G., Hurley, J.H., Hussain, S., Hussain, S., Hussey, P.J., Hutabarat, M., Hwang, H.Y., Hwang, S., Ieni, A., Ikeda, F., Imagawa, Y., Imai, Y., Imbriano, C., Imoto, M., Inman, D.M., Inoki, K., Iovanna, J., Iozzo, R.V., Ippolito, G., Irazoqui, J.E., Iribarren, P., Ishaq, M., Ishikawa, M., Ishimwe, N., Isidoro, C., Ismail, N., Issazadeh-Navikas, S., Itakura, E., Ito, D., Ivankovic, D., Ivanova, S., Iyer, A.K.V., Izquierdo, J.M., Izumi, M., Jäättelä, M., Jabir, M.S., Jackson, W.T., Jacobo-Herrera, N., Jacomin, A.C., Jacquin, E., Jadiya, P., Jaeschke, H., Jagannath, C., Jakobi, A.J., Jakobsson, J., Janji, B., Jansen-Dürr, P., Jansson, P.J., Jantsch, J., Januszewski, S., Jassey, A., Jean, S., Jeltsch-David, H., Jendelova, P., Jenny, A., Jensen, T.E., Jessen, N., Jewell, J.L., Ji, J., Jia, L., Jia, R., Jiang, L., Jiang, Q., Jiang, R., Jiang, T., Jiang, X., Jiang, Y., Jimenez-Sanchez, M., Jin, E.J., Jin, F., Jin, H., Jin, L., Jin, L., Jin, M., Jin, S., Jo, E.K., Joffre, C., Johansen, T., Johnson, G.V.W., Johnston, S.A., Jokitalo, E., Jolly, M.K., Joosten, L.A.B., Jordan, J., Joseph, B., Ju, D., Ju, J.S., Ju, J., Juárez, E., Judith, D., Juhász, G., Jun, Y., Jung, C.H., Jung, S.C., Jung, Y.K., Jungbluth, H., Jungverdorben, J., Just, S., Kaarniranta, K., Kaasik, A., Kabuta, T., Kaganovich, D., Kahana, A., Kain, R., Kajimura, S., Kalamvoki, M., Kalia, M., Kalinowski, D.S., Kaludercic, N., Kalvari, I., Kaminska, J., Kaminskyy, V.O., Kanamori, H., Kanasaki, K., Kang, C., Kang, R., Kang, S.S., Kaniyappan, S., Kanki, T., Kanneganti, T.D., Kanthasamy, A.G., Kanthasamy, A., Kantorow, M., Kapuy, O., Karamouzis, M.V., Karim, M.D.R., Karmakar, P., Katare, R.G., Kato, M., Kaufmann, S.H.E., Kauppinen, A., Kaushal, G.P., Kaushik, S., Kawasaki, K., Kazan, K., Ke, P.Y., Keating, D.J., Keber, U., Kehrl, J.H., Keller, K.E., Keller, C.W., Kemper, J.K., Kenific, C.M., Kepp, O., Kermorgant, S., Kern, A., Ketteler, R., Keulers, T.G., Khalfin, B., Khalil, H., Khambu, B., Khan, S.Y., Khandelwal, V.K.M., Khandia, R., Kho, W., Khobrekar, N.V., Khuansuwan, S., Khundadze, M., Killackey, S.A., Kim, D., Kim, D.R., Kim, D.H., Kim, D.E., Kim, E.Y., Kim, E.K., Kim, H.R., Kim, H.S., Kim, H.R., Kim, J.H., Kim, J.K., Kim, J.H., Kim, J., Kim, J.H., Kim, K.I.I., Kim, P.K., Kim, S.J., Kimball, S.R., Kimchi, A., Kimmelman, A.C., Kimura, T., King, M.A., Kinghorn, K.J., Kinsey, C.G., Kirkin, V., Kirshenbaum, L.A., Kiselev, S.L., Kishi, S., Kitamoto, K., Kitaoka, Y., Kitazato, K., Kitsis, R.N., Kittler, J.T., Kjaerulff, O., Klein, P.S., Klopstock, T., Klucken, J., Knævelsrud, H., Knorr, R.L., Ko, B.C.B., Ko, F., Ko, J.L., Kobayashi, H., Kobayashi, S., Koch, I., Koch, J.C., Koenig, U., Kögel, D., Koh, Y.H., Koike, M., Kohlwein, S.D., Kocaturk, N.M., Komatsu, M., König, J., Kono, T., Kopp, B.T., Korcsmaros, T., Korkmaz, G., Korolchuk, V.I., Korsnes, M.S., Koskela, A., Kota, J., Kotake, Y., Kotler, M.L., Kou, Y., Koukourakis, M.I., Koustas, E., Kovacs, A.L., Kovács, T., Koya, D., Kozako, T., Kraft, C., Krainc, D., Krämer, H., Krasnodembskaya, A.D., Kretz-Remy, C., Kroemer, G., Ktistakis, N.T., Kuchitsu, K., Kuenen, S., Kuerschner, L., Kukar, T., Kumar, A., Kumar, A., Kumar, D., Kumar, D., Kumar, S., Kume, S., Kumsta, C., Kundu, C.N., Kundu, M., Kunnumakkara, A.B., Kurgan, L., Kutateladze, T.G., Kutlu, O., Kwak, S.A., Kwon, H.J., Kwon, T.K., Kwon, Y.T., Kyrmizi, I., La Spada, A., Labonté, P., Ladoire, S., Laface, I., Lafont, F., Lagace, D.C., Lahiri, V., Lai, Z., Laird, A.S., Lakkaraju, A., Lamark, T., Lan, S.H., Landajuela, A., Lane, D.J.R., Lane, J.D., Lang, C.H., Lange, C., Langel, Ü., Langer, R., Lapaquette, P., Laporte, J., LaRusso, N.F., Lastres-Becker, I., Lau, W.C.Y., Laurie, G.W., Lavandero, S., Law, B.Y.K., Law, H.K.W., Layfield, R., Le, W., Le Stunff, H., Leary, A.Y., Lebrun, J.J., Leck, L.Y.W., Leduc-Gaudet, J.P., Lee, C., Lee, C.P., Lee, D.H., Lee, E.B., Lee, E.F., Lee, G.M., Lee, H.J., Lee, H.K., Lee, J.M., Lee, J.S., Lee, J.A., Lee, J.Y., Lee, J.H., Lee, M., Lee, M.G., Lee, M.J., Lee, M.S., Lee, S.Y., Lee, S.J., Lee, S.Y., Lee, S.B., Lee, W.H., Lee, Y.R., Lee, Y.H., Lee, Y., Lefebvre, C., Legouis, R., Lei, Y.L., Lei, Y., Leikin, S., Leitinger, G., Lemus, L., Leng, S., Lenoir, O., Lenz, G., Lenz, H.J., Lenzi, P., León, Y., Leopoldino, A.M., Leschczyk, C., Leskelä, S., Letellier, E., Leung, C.T., Leung, P.S., Leventhal, J.S., Levine, B., Lewis, P.A., Ley, K., Li, B., Li, D.Q., Li, J., Li, J., Li, J., Li, K., Li, L., Li, M., Li, M., Li, M., Li, M., Li, M., Li, P.L., Li, M.Q., Li, Q., Li, S., Li, T., Li, W., Li, W., Li, X., Li, Y.P., Li, Y., Li, Z., Li, Z., Li, Z., Lian, J., Liang, C., Liang, Q., Liang, W., Liang, Y., Liang, Y.T., Liao, G., Liao, L., Liao, M., Liao, Y.F., Librizzi, M., Lie, P.P.Y., Lilly, M.A., Lim, H.J., Lima, T.R.R., Limana, F., Lin, C., Lin, C.W., Lin, D.S., Lin, F.C., Lin, J.D., Lin, K.M., Lin, K.H., Lin, L.T., Lin, P.H., Lin, Q., Lin, S., Lin, S.J., Lin, W., Lin, X., Lin, Y.X., Lin, Y.S., Linden, R., Lindner, P., Ling, S.C., Lingor, P., Linnemann, A.K., Liou, Y.C., Lipinski, M.M., Lipovšek, S., Lira, V.A., Lisiak, N., Liton, P.B., Liu, C., Liu, C.H., Liu, C.F., Liu, C.H., Liu, F., Liu, H., Liu, H.S., Liu, H.F., Liu, H., Liu, J., Liu, J., Liu, J., Liu, L., Liu, L., Liu, M., Liu, Q., Liu, W., Liu, W., Liu, X.H., Liu, X., Liu, X., Liu, X., Liu, X., Liu, Y., Liu, Y., Liu, Y., Liu, Y., Liu, Y., Livingston, J.A., Lizard, G., Lizcano, J.M., Ljubojevic-Holzer, S., LLeonart, M.E., Llobet-Navàs, D., Llorente, A., Lo, C.H., Lobato-Márquez, D., Long, Q., Long, Y.C., Loos, B., Loos, J.A., López, M.G., López-Doménech, G., López-Guerrero, J.A., López-Jiménez, A.T., López-Pérez, O., López-Valero, I., Lorenowicz, M.J., Lorente, M., Lorincz, P., Lossi, L., Lotersztajn, S., Lovat, P.E., Lovell, J.F., Lovy, A., Lőw, P., Lu, G., Lu, H., Lu, J.H., Lu, J.J., Lu, M., Lu, S., Luciani, A., Lucocq, J.M., Ludovico, P., Luftig, M.A., Luhr, M., Luis-Ravelo, D., Lum, J.J., Luna-Dulcey, L., Lund, A.H., Lund, V.K., Lünemann, J.D., Lüningschrör, P., Luo, H., Luo, R., Luo, S., Luo, Z., Luparello, C., Lüscher, B., Luu, L., Lyakhovich, A., Lyamzaev, K.G., Lystad, A.H., Lytvynchuk, L., Ma, A.C., Ma, C., Ma, M., Ma, N.F., Ma, Q.H., Ma, X., Ma, Y., Ma, Z., MacDougald, O.A., Macian, F., MacIntosh, G.C., MacKeigan, J.P., Macleod, K.F., Maday, S., Madeo, F., Madesh, M., Madl, T., Madrigal-Matute, J., Maeda, A., Maejima, Y., Magarinos, M., Mahavadi, P., Maiani, E., Maiese, K., Maiti, P., Maiuri, M.C., Majello, B., Major, M.B., Makareeva, E., Malik, F., Mallilankaraman, K., Malorni, W., Maloyan, A., Mammadova, N., Man, G.C.W., Manai, F., Mancias, J.D., Mandelkow, E.M., Mandell, M.A., Manfredi, A.A., Manjili, M.H., Manjithaya, R., Manque, P., Manshian, B.B., Manzano, R., Manzoni, C., Mao, K., Marchese, C., Marchetti, S., Marconi, A.M., Marcucci, F., Mardente, S., Mareninova, O.A., Margeta, M., Mari, M., Marinelli, S., Marinelli, O., Mariño, G., Mariotto, S., Marshall, R.S., Marten, M.R., Martens, S., Martin, A.P.J., Martin, K.R., Martin, S., Martin, S., Martín-Segura, A., Martín-Acebes, M.A., Martin-Burriel, I., Martin-Rincon, M., Martin-Sanz, P., Martina, J.A., Martinet, W., Martinez, A., Martinez, A., Martinez, J., Martinez Velazquez, M., Martinez-Lopez, N., Martinez-Vicente, M., Martins, D.O., Martins, J.O., Martins, W.K., Martins-Marques, T., Marzetti, E., Masaldan, S., Masclaux-Daubresse, C., Mashek, D.G., Massa, V., Massieu, L., Masson, G.R., Masuelli, L., Masyuk, A.I., Masyuk, T.V., Matarrese, P., Matheu, A., Matoba, S., Matsuzaki, S., Mattar, P., Matte, A., Mattoscio, D., Mauriz, J.L., Mauthe, M., Mauvezin, C., Maverakis, E., Maycotte, P., Mayer, J., Mazzoccoli, G., Mazzoni, C., Mazzulli, J.R., McCarty, N., McDonald, C., McGill, M.R., McKenna, S.L., McLaughlin, B.A., McLoughlin, F., McNiven, M.A., McWilliams, T.G., Mechta-Grigoriou, F., Medeiros, T.C., Medina, D.L., Megeney, L.Y., Megyeri, K., Mehrpour, M., Mehta, J.L., Meijer, A.J., Meijer, A.H., Mejlvang, J., Meléndez, A., Melk, A., Memisoglu, G., Mendes, A.F., Meng, D., Meng, F., Meng, T., Menna-Barreto, R., Menon, M.B., Mercer, C., Mercier, A.E., Mergny, J.L., Merighi, A., Merkley, S.D., Merla, G., Meske, V., Mestre, A.C., Metur, S.P., Meyer, C., Meyer, H., Mi, W., Mialet-Perez, J., Miao, J., Micale, L., Miki, Y., Milan, E., Milczarek, M., Miller, D.L., Miller, S.I., Miller, S., Millward, S.W., Milosevic, I., Minina, E.A., Mirzaei, H., Mirzaei, H.R., Mirzaei, M., Mishra, A., Mishra, N., Mishra, P.K., Misirkic Marjanovic, M., Misasi, R., Misra, A., Misso, G., Mitchell, C., Mitou, G., Miura, T., Miyamoto, S., Miyazaki, M., Miyazaki, M., Miyazaki, T., Miyazawa, K., Mizushima, N., Mogensen, T.H., Mograbi, B., Mohammadinejad, R., Mohamud, Y., Mohanty, A., Mohapatra, S., Möhlmann, T., Mohmmed, A., Moles, A., Moley, K.H., Molinari, M., Mollace, V., Møller, A.B., Mollereau, B., Mollinedo, F., Montagna, C., Monteiro, M.J., Montella, A., Montes, L.R., Montico, B., Mony, V.K., Monzio Compagnoni, G., Moore, M.N., Moosavi, M.A., Mora, A.L., Mora, M., Morales-Alamo, D., Moratalla, R., Moreira, P.I., Morelli, E., Moreno, S., Moreno-Blas, D., Moresi, V., Morga, B., Morgan, A.H., Morin, F., Morishita, H., Moritz, O.L., Moriyama, M., Moriyasu, Y., Morleo, M., Morselli, E., Moruno-Manchon, J.F., Moscat, J., Mostowy, S., Motori, E., Moura, A.F., Moustaid-Moussa, N., Mrakovcic, M., Muciño-Hernández, G., Mukherjee, A., Mukhopadhyay, S., Mulcahy Levy, J.M., Mulero, V., Muller, S., Münch, C., Munjal, A., Munoz-Canoves, P., Muñoz-Galdeano, T., Münz, C., Murakawa, T., Muratori, C., Murphy, B.M., Murphy, J.P., Murthy, A., Myöhänen, T.T., Mysorekar, I.U., Mytych, J., Nabavi, S.M., Nabissi, M., Nagy, P., Nah, J., Nahimana, A., Nakagawa, I., Nakamura, K., Nakatogawa, H., Nandi, S.S., Nanjundan, M., Nanni, M., Napolitano, G., Nardacci, R., Narita, M., Nassif, M., Nathan, I., Natsumeda, M., Naude, R.J., Naumann, C., Naveiras, O., Navid, F., Nawrocki, S.T., Nazarko, T.Y., Nazio, F., Negoita, F., Neill, T., Neisch, A.L., Neri, L.M., Netea, M.G., Neubert, P., Neufeld, T.P., Neumann, D., Neutzner, A., Newton, P.T., Ney, P.A., Nezis, I.P., Ng, C.C.W., Ng, T.B., Nguyen, H.T.T., Nguyen, L.T., Ni, H.M., Ní Cheallaigh, C., Ni, Z., Nicolao, M.C., Nicoli, F., Nieto-Diaz, M., Nilsson, P., Ning, S., Niranjan, R., Nishimune, H., Niso-Santano, M., Nixon, R.A., Nobili, A., Nobrega, C., Noda, T., Nogueira-Recalde, U., Nolan, T.M., Nombela, I., Novak, I., Novoa, B., Nozawa, T., Nukina, N., Nussbaum-Krammer, C., Nylandsted, J., O'Donovan, T.R., O'Leary, S.M., O'Rourke, E.J., O'Sullivan, M.P., O'Sullivan, T.E., Oddo, S., Oehme, I., Ogawa, M., Ogier-Denis, E., Ogmundsdottir, M.H., Ogretmen, B., Oh, G.T., Oh, S.H., Oh, Y.J., Ohama, T., Ohashi, Y., Ohmuraya, M., Oikonomou, V., Ojha, R., Okamoto, K., Okazawa, H., Oku, M., Oliván, S., Oliveira, J.M.A., Ollmann, M., Olzmann, J.A., Omari, S., Omary, M.B., Önal, G., Ondrej, M., Ong, S.B., Ong, S.G., Onnis, A., Orellana, J.A., Orellana-Muñoz, S., Ortega-Villaizan, M.D.M., Ortiz-Gonzalez, X.R., Ortona, E., Osiewacz, H.D., Osman, A.H.K., Osta, R., Otegui, M.S., Otsu, K., Ott, C., Ottobrini, L., Ou, J.H.J., Outeiro, T.F., Oynebraten, I., Ozturk, M., Pagès, G., Pahari, S., Pajares, M., Pajvani, U.B., Pal, R., Paladino, S., Pallet, N., Palmieri, M., Palmisano, G., Palumbo, C., Pampaloni, F., Pan, L., Pan, Q., Pan, W:, Pan, X., Panasyuk, G., Pandey, R., Pandey, U.B., Pandya, V., Paneni, F., Pang, S.Y., Panzarini, E., Papademetrio, D.L., Papaleo, E., Papinski, D., Papp, D., Park, E.C., Park, H.T., Park, J.M., Park, J.I., Park, J.T., Park, J., Park, S.C., Park, S.Y., Parola, A.H., Parys, J.B., Pasquier, A., Pasquier, B., Passos, J.F., Pastore, N., Patel, H.H., Patschan, D., Pattingre, S., Pedraza-Alva, G., Pedraza-Chaverri, J., Pedrozo, Z., Pei, G., Pei, J., Peled-Zehavi, H., Pellegrini, J.M., Pelletier, J., Peñalva, M.A., Peng, D., Peng, Y., Penna, F., Pennuto, M., Pentimalli, F., Pereira, C.M.F., Pereira, G.J.S., Pereira, L.C., Pereira de Almeida, L., Perera, N.D., Pérez-Lara, A., Perez-Oliva, A.B., Pérez-Pérez, M.E., Periyasamy, P., Perl, A., Perrotta, C., Perrotta, I., Pestell, R.G., Petersen, M., Petrache, I., Petrovski, G., Pfirrmann, T., Pfister, A.S., Philips, J.A., Pi, H., Picca, A., Pickrell, A.M., Picot, S., Pierantoni, G.M., Pierdominici, M., Pierre, P., Pierrefite-Carle, V., Pierzynowska, K., Pietrocola, F., Pietruczuk, M., Pignata, C., Pimentel-Muiños, F.X., Pinar, M., Pinheiro, R.O., Pinkas-Kramarski, R., Pinton, P., Pircs, K., Piya, S., Pizzo, P., Plantinga, T.S., Platta, H.W., Plaza-Zabala, A., Plomann, M., Plotnikov, E.Y., Plun-Favreau, H., Pluta, R., Pocock, R., Pöggeler, S., Pohl, C., Poirot, M., Poletti, A., Ponpuak, M., Popelka, H., Popova, B., Porta, H., Porte Alcon, S., Portilla-Fernandez, E., Post, M., Potts, M.B., Poulton, J., Powers, T., Prahlad, V., Prajsnar, T.K., Praticò, D., Prencipe, R., Priault, M., Proikas-Cezanne, T., Promponas, V.J., Proud, C.G., Puertollano, R., Puglielli, L., Pulinilkunnil, T., Puri, D., Puri, R., Puyal, J., Qi, X., Qi, Y., Qian, W., Qiang, L., Qiu, Y., Quadrilatero, J., Quarleri, J., Raben, N., Rabinowich, H., Ragona, D., Ragusa, M.J., Rahimi, N., Rahmati, M., Raia, V., Raimundo, N., Rajasekaran, N.S., Ramachandra Rao, S., Rami, A., Ramírez-Pardo, I., Ramsden, D.B., Randow, F., Rangarajan, P.N., Ranieri, D., Rao, H., Rao, L., Rao, R., Rathore, S., Ratnayaka, J.A., Ratovitski, E.A., Ravanan, P., Ravegnini, G., Ray, S.K., Razani, B., Rebecca, V., Reggiori, F., Régnier-Vigouroux, A., Reichert, A.S., Reigada, D., Reiling, J.H., Rein, T., Reipert, S., Rekha, R.S., Ren, H., Ren, J., Ren, W., Renault, T., Renga, G., Reue, K., Rewitz, K., Ribeiro de Andrade Ramos, B., Riazuddin, S.A., Ribeiro-Rodrigues, T.M., Ricci, J.E., Ricci, R., Riccio, V., Richardson, D.R., Rikihisa, Y., Risbud, M.V., Risueño, R.M., Ritis, K., Rizza, S., Rizzuto, R., Roberts, H.C., Roberts, L.D., Robinson, K.J., Roccheri, M.C., Rocchi, S., Rodney, G.G., Rodrigues, T., Rodrigues Silva, V.R., Rodriguez, A., Rodriguez-Barrueco, R., Rodriguez-Henche, N., Rodriguez-Rocha, H., Roelofs, J., Rogers, R.S., Rogov, V.V., Rojo, A.I., Rolka, K., Romanello, V., Romani, L., Romano, A., Romano, P.S., Romeo-Guitart, D., Romero, L.C., Romero, M., Roney, J.C., Rongo, C., Roperto, S., Rosenfeldt, M.T., Rosenstiel, P., Rosenwald, A.G., Roth, K.A., Roth, L., Roth, S., Rouschop, K.M.A., Roussel, B.D., Roux, S., Rovere-Querini, P., Roy, A., Rozieres, A., Ruano, D., Rubinsztein, D.C., Rubtsova, M.P., Ruckdeschel, K., Ruckenstuhl, C., Rudolf, E., Rudolf, R., Ruggieri, A., Ruparelia, A.A., Rusmini, P., Russell, R.R., Russo, G.L., Russo, M., Russo, R., Ryabaya, O.O., Ryan, K.M., Ryu, K.Y., Sabater-Arcis, M., Sachdev, U., Sacher, M., Sachse, C., Sadhu, A., Sadoshima, J., Safren, N., Saftig, P., Sagona, A.P., Sahay, G., Sahebkar, A., Sahin, M., Sahin, O., Sahni, S., Saito, N., Saito, S., Saito, T., Sakai, R., Sakai, Y., Sakamaki, J.I., Saksela, K., Salazar, G., Salazar-Degracia, A., Salekdeh, G.H., Saluja, A.K., Sampaio-Marques, B., Sanchez, M.C., Sanchez-Alcazar, J.A., Sanchez-Vera, V., Sancho-Shimizu, V., Sanderson, J.T., Sandri, M., Santaguida, S., Santambrogio, L., Santana, M.M., Santoni, G., Sanz, A., Sanz, P., Saran, S., Sardiello, M., Sargeant, T.J., Sarin, A., Sarkar, C., Sarkar, S., Sarrias, M.R., Sarkar, S., Sarmah, D.T., Sarparanta, J., Sathyanarayan, A., Sathyanarayanan, R., Scaglione, K.M., Scatozza, F., Schaefer, L., Schafer, Z.T., Schaible, U.E., Schapira, A.H.V., Scharl, M., Schatzl, H.M., Schein, C.H., Scheper, W., Scheuring, D., Schiaffino, M.V., Schiappacassi, M., Schindl, R., Schlattner, U., Schmidt, O., Schmitt, R., Schmidt, S.D., Schmitz, I., Schmukler, E., Schneider, A., Schneider, B.E., Schober, R., Schoijet, A.C., Schott, M.B., Schramm, M., Schröder, B., Schuh, K., Schüller, C., Schulze, R.L., Schürmanns, L., Schwamborn, J.C., Schwarten, M., Scialo, F., Sciarretta, S., Scott, M.J., Scotto, K.W., Scovassi, A.I., Scrima, A., Scrivo, A., Sebastian, D., Sebti, S., Sedej, S., Segatori, L., Segev, N., Seglen, P.O., Seiliez, I., Seki, E., Selleck, S.B., Sellke, F.W., Selsby, J.T., Sendtner, M., Senturk, S., Seranova, E., Sergi, C., Serra-Moreno, R., Sesaki, H., Settembre, C., Setty, S.R.G., Sgarbi, G., Sha, O., Shacka, J.J., Shah, J.A., Shang, D., Shao, C., Shao, F., Sharbati, S., Sharkey, L.M., Sharma, D., Sharma, G., Sharma, K., Sharma, P., Sharma, S., Shen, H.M., Shen, H., Shen, J., Shen, M., Shen, W., Shen, Z., Sheng, R., Sheng, Z., Sheng, Z.H., Shi, J., Shi, X., Shi, Y.H., Shiba-Fukushima, K., Shieh, J.J., Shimada, Y., Shimizu, S., Shimozawa, M., Shintani, T., Shoemaker, C.J., Shojaei, S., Shoji, I., Shravage, B.V., Shridhar, V., Shu, C.W., Shu, H.B., Shui, K., Shukla, A.K., Shutt, T.E., Sica, V., Siddiqui, A., Sierra, A., Sierra-Torre, V., Signorelli, S., Sil, P., Silva, B.J.A., Silva, J.D., Silva-Pavez, E., Silvente-Poirot, S., Simmonds, R.E., Simon, A.K.
ORCID: https://orcid.org/0000-0002-4077-7995, Simon, H.U., Simons, M., Singh, A., Singh, L.P., Singh, R., Singh, S.V., Singh, S.K., Singh, S.B., Singh, S., Singh, S.P., Sinha, D., Sinha, R.A., Sinha, S., Sirko, A., Sirohi, K., Sivridis, E.L., Skendros, P., Skirycz, A., Slaninová, I., Smaili, S.S., Smertenko, A., Smith, M.D., Soenen, S.J., Sohn, E.J., Sok, S.P.M., Solaini, G., Soldati, T., Soleimanpour, S.A., Soler, R.M., Solovchenko, A., Somarelli, J.A., Sonawane, A., Song, F., Song, H.K., Song, J.X., Song, K., Song, Z., Soria, L.R., Sorice, M., Soukas, A.A., Soukup, S.F., Sousa, D., Sousa, N., Spagnuolo, P.A., Spector, S.A., Srinivas Bharath, M.M., St Clair, D., Stagni, V., Staiano, L., Stalnecker, C.A., Stankov, M.V., Stathopulos, P.B., Stefan, K., Stefan, S.M., Stefanis, L., Steffan, J.S., Steinkasserer, A., Stenmark, H., Sterneckert, J., Stevens, C., Stoka, V., Storch, S., Stork, B., Strappazzon, F., Strohecker, A.M., Stupack, D.G., Su, H., Su, L.Yy, Su, L., Suarez-Fontes, A.M., Subauste, C.S., Subbian, S., Subirada, P.V., Sudhandiran, G., Sue, C.M., Sui, X., Summers, C., Sun, G., Sun, J., Sun, K., Sun, M.X., Sun, Q., Sun, Y., Sun, Z., Sunahara, K.K.S., Sundberg, E., Susztak, K., Sutovsky, P., Suzuki, H., Sweeney, G., Symons, J.D., Sze, S.C.W., Szewczyk, N.J., Tabęcka-Łonczynska, A., Tabolacci, C., Tacke, F., Taegtmeyer, H., Tafani, M., Tagaya, M., Tai, H., Tait, S.W.G., Takahashi, Y., Takats, S., Talwar, P., Tam, C., Tam, S.Y., Tampellini, D., Tamura, A., Tan, C.T., Tan, E.K., Tan, Y.Q., Tanaka, M., Tanaka, M., Tang, D., Tang, J., Tang, T.S., Tanida, I., Tao, Z., Taouis, M., Tatenhorst, L., Tavernarakis, N., Taylor, A., Taylor, G.A., Taylor, J.M., Tchetina, E., Tee, A.R., Tegeder, I., Teis, D., Teixeira, N., Teixeira-Clerc, F., Tekirdag, K.A., Tencomnao, T., Tenreiro, S., Tepikin, A.V., Testillano, P.S., Tettamanti, G., Tharaux, P.L., Thedieck, K., Thekkinghat, A.A., Thellung, S., Thinwa, J.W., Thirumalaikumar, V.P., Thomas, S.M., Thomes, P.G., Thorburn, A., Thukral, L., Thum, T., Thumm, M., Tian, L., Tichy, A., Till, A., Timmerman, V., Titorenko, V.I., Todi, S.V., Todorova, K., Toivonen, J.M., Tomaipitinca, L., Tomar, D., Tomas-Zapico, C., Tomić, S., Tong, B.C.K., Tong, C., Tong, X., Tooze, S.A., Torgersen, M.L., Torii, S., Torres-López, L., Torriglia, A., Towers, C.G., Towns, R., Toyokuni, S., Trajkovic, V., Tramontano, D., Tran, Q.G., Travassos, L.H., Trelford, C.B., Tremel, S., Trougakos, I.P., Tsao, B.P., Tschan, M.P., Tse, H.F., Tse, T.F., Tsugawa, H., Tsvetkov, A.S., Tumbarello, D.A., Tumtas, Y., Tuñón, M.J., Turcotte, S., Turk, B., Turk, V., Turner, B.J., Tuxworth, R.I., Tyler, J.K., Tyutereva, E.V., Uchiyama, Y., Ugun-Klusek, A., Uhlig, H.H., Ułamek-Kozioł, M., Ulasov, I.V., Umekawa, M., Ungermann, C., Unno, R., Urbe, S., Uribe-Carretero, E., Üstün, S., Uversky, V.N., Vaccari, T., Vaccaro, M.I., Vahsen, B.F., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, M.J., Valko, A., Vallee, R.B., Valverde, A.M., Van den Berghe, G., van der Veen, S., Van Kaer, L., van Loosdregt, J., van Wijk, S.J.L., Vandenberghe, W., Vanhorebeek, I., Vannier-Santos, M.A., Vannini, N., Vanrell, M.C., Vantaggiato, C., Varano, G., Varela-Nieto, I., Varga, M., Vasconcelos, M.H., Vats, S., Vavvas, D.G., Vega-Naredo, I., Vega-Rubin-de-Celis, S., Velasco, G., Velázquez, A.P., Vellai, T., Vellenga, E., Velotti, F., Verdier, M., Verginis, P., Vergne, I., Verkade, P., Verma, M., Verstreken, P., Vervliet, T., Vervoorts, J., Vessoni, A.T., Victor, V.M., Vidal, M., Vidoni, C., Vieira, O.V., Vierstra, R.D., Viganó, S., Vihinen, H., Vijayan, V., Vila, M., Vilar, M., Villalba, J.M., Villalobo, A., Villarejo-Zori, B., Villarroya, F., Villarroya, J., Vincent, O., Vindis, C., Viret, C., Viscomi, M.T., Visnjic, D., Vitale, I., Vocadlo, D.J., Voitsekhovskaja, O.V., Volonté, C., Volta, M., Vomero, M., Von Haefen, C., Vooijs, M.A., Voos, W., Vucicevic, L., Wade-Martins, R., Waguri, S., Waite, K.A., Wakatsuki, S., Walker, D.W., Walker, M.J., Walker, S.A., Walter, J., Wandosell, F.G., Wang, B., Wang, C.Y., Wang, C., Wang, C., Wang, C., Wang, C.Y., Wang, D., Wang, F., Wang, F., Wang, F., Wang, G., Wang, H., Wang, H., Wang, H., Wang, H.G., Wang, J., Wang, J., Wang, J., Wang, J., Wang, K., Wang, L., Wang, L., Wang, M.H., Wang, M., Wang, N., Wang, P., Wang, P., Wang, P., Wang, P., Wang, Q.J., Wang, Q., Wang, Q.K., Wang, Q.A., Wang, W.T., Wang, W., Wang, X., Wang, X., Wang, Y., Wang, Y., Wang, Y., Wang, Y.Y., Wang, Y., Wang, Y., Wang, Y., Wang, Y., Wang, Z., Wang, Z., Wang, Z., Warnes, G., Warnsmann, V., Watada, H., Watanabe, E., Watchon, M., Wawrzyńska, A., Weaver, T.E., Wegrzyn, G., Wehman, A.M., Wei, H., Wei, L., Wei, T., Wei, Y., Weiergräber, O.H., Weihl, C.C., Weindl, G., Weiskirchen, R., Wells, A., Wen, R.H., Wen, X., Werner, A., Weykopf, B., Wheatley, S.P., Whitton, J.L., Whitworth, A.J., Wiktorska, K., Wildenberg, M.E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R.S.B., Williams, R.L., Williamson, P.R., Wilson, R.A., Winner, B., Winsor, N.J., Witkin, S.S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J.H., Wong, R.W., Wong, V.K.W., Wong, W.L., Wu, A.G., Wu, C., Wu, J., Wu, J., Wu, K.K., Wu, M., Wu, S.Y., Wu, S., Wu, S.Y., Wu, S., Wu, W.K.K., Wu, X., Wu, X., Wu, Y.W., Wu, Y., Xavier, R.J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H.T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C.M., Xie, M., Xie, Y., Xie, Z., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, J.R., Xu, L., Xu, W.W., Xu, X., Xue, Y., Yakhine-Diop, S.M.S., Yamaguchi, M., Yamaguchi, O., Yamamoto, A., Yamashina, S., Yan, S., Yan, S.J., Yan, Z., Yanagi, Y., Yang, C., Yang, D.S., Yang, H., Yang, H.T., Yang, H., Yang, J.M., Yang, J., Yang, J., Yang, L., Yang, L., Yang, M., Yang, P.M., Yang, Q., Yang, S., Yang, S., Yang, S.F., Yang, W., Yang, W.Y., Yang, X., Yang, X., Yang, Y., Yang, Y., Yao, H., Yao, S., Yao, X., Yao, Y.G., Yao, Y.M., Yasui, T., Yazdankhah, M., Yen, P.M., Yi, C., Yin, X.M., Yin, Y., Yin, Z., Yin, Z., Ying, M., Ying, Z., Yip, C.K., Yiu, S.P.T., Yoo, Y.H., Yoshida, K., Yoshii, S.R., Yoshimori, T., Yousefi, B., Yu, B., Yu, H., Yu, J., Yu, J., Yu, L., Yu, M.L., Yu, S.W., Yu, V.C., Yu, W.H., Yu, Z., Yu, Z., Yuan, J., Yuan, L.Q., Yuan, S., Yuan, S.S.F., Yuan, Y., Yuan, Z., Yue, J., Yue, Z., Yun, J., Yung, R.L., Zacks, D.N., Zaffagnini, G., Zambelli, V.O., Zanella, I., Zang, Q.S., Zanivan, S., Zappavigna, S., Zaragoza, P., Zarbalis, K.S., Zarebkohan, A., Zarrouk, A., Zeitlin, S.O., Zeng, J., Zeng, J.D., Žerovnik, E., Zhan, L., Zhang, B., Zhang, D.D., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H., Zhang, H.L., Zhang, J., Zhang, J., Zhang, J.P., Zhang, K.Y.B., Zhang, L.W., Zhang, L., Zhang, L., Zhang, L., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X.W., Zhang, X., Zhang, X., Zhang, X., Zhang, X., Zhang, X.D., Zhang, Y., Zhang, Y., Zhang, Y., Zhang, Y.D., Zhang, Y., Zhang, Y.Y., Zhang, Y., Zhang, Z., Zhang, Z., Zhang, Z., Zhang, Z., Zhang, Z., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X.F., Zhao, Y., Zhao, Y., Zhao, Y., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X.L., Zheng, Y., Zheng, Z.G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, H., Zhou, H., Zhou, J., Zhou, J., Zhou, J., Zhou, J., Zhou, K., Zhou, R., Zhou, X.J., Zhou, Y., Zhou, Y., Zhou, Y., Zhou, Z.Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G.Q., Zhu, H., Zhu, H., Zhu, H., Zhu, W.G., Zhu, Y., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C.M., Ziviani, E., Zoladek, T., Zong, W.X., Zorov, D.B., Zorzano, A., Zou, W., Zou, Z., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X.C., Kenchappa, C.S., Li, Z., Lin, Y., Oshima, S., Rong, Y., Sluimer, J.C., Stallings, C.L. and Tong, C.K.
Autophagy 17
(1): 1-382.
8 February 2021
2020
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.
Grunwald, S.
ORCID: https://orcid.org/0000-0003-3978-6277, Hopf, L.V.M.
ORCID: https://orcid.org/0000-0002-4372-694X, Bock-Bierbaum, T.
ORCID: https://orcid.org/0000-0003-0843-2716, Lally, C.C.M., Spahn, C.M.T. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Nature Communications 11
(1): 5506.
2 November 2020
Monogenic variants in dystonia: an exome-wide sequencing study.
Zech, M., Jech, R., Boesch, S., Škorvánek, M., Weber, S., Wagner, M., Zhao, C., Jochim, A., Necpál, J., Dincer, Y., Vill, K., Distelmaier, F., Stoklosa, M., Krenn, M., Grunwald, S.
ORCID: https://orcid.org/0000-0003-3978-6277, Bock-Bierbaum, T.
ORCID: https://orcid.org/0000-0003-0843-2716, Fečíková, A., Havránková, P., Roth, J., Příhodová, I., Adamovičová, M., Ulmanová, O., Bechyně, K., Danhofer, P., Veselý, B., Haň, V., Pavelekova, P., Gdovinová, Z., Mantel, T., Meindl, T., Sitzberger, A., Schröder, S., Blaschek, A., Roser, T., Bonfert, M.V., Haberlandt, E., Plecko, B., Leineweber, B., Berweck, S., Herberhold, T., Langguth, B., Švantnerová, J., Minár, M., Ramos-Rivera, G.A., Wojcik, M.H., Pajusalu, S., Õunap, K., Schatz, U.A., Pölsler, L., Milenkovic, I., Laccone, F., Pilshofer, V., Colombo, R., Patzer, S., Iuso, A., Vera, J., Troncoso, M., Fang, F., Prokisch, H., Wilbert, F., Eckenweiler, M., Graf, E., Westphal, D.S., Riedhammer, K.M., Brunet, T., Alhaddad, B., Berutti, R., Strom, T.M., Hecht, M., Baumann, M., Wolf, M., Telegrafi, A., Person, R.E., Zamora, F.M., Henderson, L.B., Weise, D., Musacchio, T., Volkmann, J., Szuto, A., Becker, J., Cremer, K., Sycha, T., Zimprich, F., Kraus, V., Makowski, C., Gonzalez-Alegre, P., Bardakjian, T.M., Ozelius, L.J., Vetro, A., Guerrini, R., Maier, E., Borggraefe, I., Kuster, A., Wortmann, S.B., Hackenberg, A., Steinfeld, R., Assmann, B., Staufner, C., Opladen, T., Růžička, E., Cohn, R.D., Dyment, D., Chung, W.K., Engels, H., Ceballos-Baumann, A., Ploski, R., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Haslinger, B., Mall, V., Oexle, K. and Winkelmann, J.
Lancet Neurology 19
(11): 908-918.
November 2020
hGBP1 coordinates chlamydia restriction and inflammasome activation through sequential GTP hydrolysis.
Xavier, A., Al-Zeer, M.A., Meyer, T.F. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Cell Reports 31
(7): 107667.
19 May 2020
The pierced lasso topology leptin has a bolt on dynamic domain composed by the disordered loops I and III.
Danielsson, J., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Simien, J.M., Duggan, B.M., Oliveberg, M., Onuchic, J.N., Jennings, P.A. and Haglund, E.
Journal of Molecular Biology 432
(9): 3050-3063.
17 April 2020
Age attenuates the T-type Ca(V) 3.2-RyR axis in vascular smooth muscle.
Fan, G.
ORCID: https://orcid.org/0000-0003-1894-3253, Kaßmann, M.
ORCID: https://orcid.org/0000-0002-4785-6530, Cui, Y., Matthaeus, C.
ORCID: https://orcid.org/0000-0003-3242-1195, Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, Zhong, C., Zhu, S., Xie, Yu, Tsvetkov, D.
ORCID: https://orcid.org/0000-0002-6472-971X, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Huang, Yu and Gollasch, M.
ORCID: https://orcid.org/0000-0003-2797-1934
Aging Cell 19
(4): e13134.
April 2020
EHD2-mediated restriction of caveolar dynamics regulates cellular fatty acid uptake.
Matthaeus, C.
ORCID: https://orcid.org/0000-0003-3242-1195, Lahmann, I.
ORCID: https://orcid.org/0000-0003-0640-4519, Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, Jonas, W., Melo, A.A., Lehmann, M., Larsson, E., Lundmark, R., Kern, M., Blüher, M., Olschowski, H., Kompa, J., Brügger, B., Müller, D.N.
ORCID: https://orcid.org/0000-0003-3650-5644, Haucke, V.
ORCID: https://orcid.org/0000-0003-3119-6993, Schürmann, A.
ORCID: https://orcid.org/0000-0002-4113-4377, Birchmeier, C.
ORCID: https://orcid.org/0000-0002-2041-8872 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Proceedings of the National Academy of Sciences of the United States of America 117
(13): 7471-7481.
31 March 2020
2019
Polymer-like model to study the dynamics of dynamin filaments on deformable membrane tubes.
Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Noé, F., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Mikhailov, A.S.
Biophysical Journal 117
(10): 1870-1891.
19 November 2019
eNOS-NO-induced small blood vessel relaxation requires EHD2-dependent caveolae stabilization.
Matthaeus, C.
ORCID: https://orcid.org/0000-0003-3242-1195, Lian, X., Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, Lehmann, M., Zhong, C., Bernert, C., Lahmann, I.
ORCID: https://orcid.org/0000-0003-0640-4519, Müller, D.N.
ORCID: https://orcid.org/0000-0003-3650-5644, Gollasch, M.
ORCID: https://orcid.org/0000-0003-2797-1934 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
PLoS ONE 14
(10): e0223620.
10 October 2019
53BP1 supports immunoglobulin class switch recombination independently of its DNA double-strand break end protection function.
Sundaravinayagam, D.
ORCID: https://orcid.org/0000-0003-0717-7530, Rahjouei, A.
ORCID: https://orcid.org/0000-0003-3973-6333, Andreani, M.
ORCID: https://orcid.org/0000-0003-1426-5854, Tupiņa, D.
ORCID: https://orcid.org/0000-0003-3376-1159, Balasubramanian, S.
ORCID: https://orcid.org/0000-0003-1830-5737, Saha, T., Delgado-Benito, V.
ORCID: https://orcid.org/0000-0002-0077-1935, Coralluzzo, V., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Di Virgilio, M.
ORCID: https://orcid.org/0000-0001-5189-0793
Cell Reports 28
(6): 1389-1399.
6 August 2019
How RB1CC1/FIP200 claws its way to autophagic engulfment of SQSTM1/p62-ubiquitin condensates.
Turco, E., Witt, M., Abert, C., Bock-Bierbaum, T.
ORCID: https://orcid.org/0000-0003-0843-2716, Su, M.Y., Trapannone, R., Sztacho, M., Danieli, A., Shi, X., Zaffagnini, G.
ORCID: https://orcid.org/0000-0002-6554-7352, Gamper, A., Schuschnig, M., Fracchiolla, D., Bernklau, D., Romanov, J., Hartl, M.
ORCID: https://orcid.org/0000-0002-4970-7336, Hurley, J.H., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Martens, S.
ORCID: https://orcid.org/0000-0003-3786-8199
Autophagy 15
(8): 1475-1477.
August 2019
Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1.
Faelber, K., Dietrich, L., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Wollweber, F., Pfitzner, A.K., Mühleip, A., Sánchez, R., Kudryashev, M.
ORCID: https://orcid.org/0000-0003-3550-6274, Chiaruttini, N., Lilie, H., Schlegel, J., Rosenbaum, E., Hessenberger, M.
ORCID: https://orcid.org/0000-0003-3021-1100, Matthaeus, C.
ORCID: https://orcid.org/0000-0003-3242-1195, Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, von der Malsburg, A., Noé, F., Roux, A., van der Laan, M., Kühlbrandt, W. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Nature 571
(7765): 429-433.
18 July 2019
Pathophysiological role of caveolae in hypertension.
Lian, X., Matthaeus, C.
ORCID: https://orcid.org/0000-0003-3242-1195, Kaßmann, M.
ORCID: https://orcid.org/0000-0002-4785-6530, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Gollasch, M.
ORCID: https://orcid.org/0000-0003-2797-1934
Frontiers in Medicine 6
: 153.
July 2019
Studying ribosome dynamics with simplified models.
Levi, M., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036 and Whitford, P.C.
Methods 162-163
: 128-140.
1 June 2019
FIP200 claw domain binding to p62 promotes autophagosome formation at ubiquitin condensates.
Turco, E., Witt, M., Abert, C., Bock-Bierbaum, T.
ORCID: https://orcid.org/0000-0003-0843-2716, Su, M.Y., Trapannone, R., Sztacho, M., Danieli, A., Shi, X., Zaffagnini, G., Gamper, A., Schuschnig, M., Fracchiolla, D., Bernklau, D., Romanov, J., Hartl, M., Hurley, J.H., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Martens, S.
Molecular Cell 74
(2): 330-346.
18 April 2019
Autocrine LTA signaling drives NF-κB and JAK-STAT activity and myeloid gene expression in Hodgkin lymphoma.
von Hoff, L., Kärgel, E., Franke, V.
ORCID: https://orcid.org/0000-0003-3606-6792, McShane, E.
ORCID: https://orcid.org/0000-0002-7806-2063, Schulz-Beiss, K.W., Patone, G.
ORCID: https://orcid.org/0000-0002-7242-0341, Schleussner, N.
ORCID: https://orcid.org/0009-0001-3549-5600, Kolesnichenko, M.
ORCID: https://orcid.org/0000-0001-7366-9061, Hübner, N.
ORCID: https://orcid.org/0000-0002-1218-6223, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Selbach, M.
ORCID: https://orcid.org/0000-0003-2454-8751, Akalin, A.
ORCID: https://orcid.org/0000-0002-0468-0117, Mathas, S.
ORCID: https://orcid.org/0000-0001-9626-1413 and Scheidereit, C.
ORCID: https://orcid.org/0000-0002-0446-6129
Blood 133
(13): 1489-1494.
28 March 2019
A SEPT1-based scaffold is required for Golgi integrity and function.
Song, K., Gras, C.
ORCID: https://orcid.org/0000-0002-2845-4181, Capin, G., Gimber, N.
ORCID: https://orcid.org/0000-0001-9456-3063, Lehmann, M., Mohd, S., Puchkov, D., Rödiger, M., Wilhelmi, I., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Schmoranzer, J., Schürmann, A. and Krauss, M.
Journal of Cell Science 132
(3): jcs225557.
1 February 2019
Using SMOG 2 to simulate complex biomolecular assemblies.
Levi, M., Bandarkar, P., Yang, H., Wang, A., Mohanty, U., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036 and Whitford, P.C.
Methods in Molecular Biology 2022
: 129-151.
2019
2018
Struktur und Funktion des mechanochemischen Motorproteins Dynamin.
Faelber, K. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
BIOspektrum 24
(5): 481-483.
September 2018
Atomistic simulations indicate the functional loop-to-coiled-coil transition in influenza hemagglutinin is not downhill.
Lin, X., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Wang, Q., Ma, J. and Onuchic, J.N.
Proceedings of the National Academy of Sciences of the United States of America 115
(34): E7905-E7913.
21 August 2018
Structural basis for membrane tethering by a bacterial dynamin-like pair.
Liu, J., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036 and Low, H.H.
Nature Communications 9
(1): 3345.
21 August 2018
Effects of allelic variations in the human myxovirus resistance protein A on its antiviral activity.
Graf, L., Dick, A.
ORCID: https://orcid.org/0000-0003-0580-1897, Sendker, F., Barth, E., Marz, M., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Kochs, G.
Journal of Biological Chemistry 293
(9): 3056-3072.
2 March 2018
An AKAP-Lbc-RhoA interaction inhibitor promotes the translocation of aquaporin-2 to the plasma membrane of renal collecting duct principal cells.
Schrade, K., Tröger, J., Eldahshan, A., Zühlke, K., Abdul Azeez, K.R., Elkins, J.M., Neuenschwander, M.
ORCID: https://orcid.org/0000-0002-3114-7975, Oder, A., Elkewedi, M.M.H., Jaksch, S., Andrae, K., Li, J., Fernandes, J., Müller, P.M.
ORCID: https://orcid.org/0000-0001-9056-4114, Grunwald, S.
ORCID: https://orcid.org/0000-0003-3978-6277, Marino, S.F.
ORCID: https://orcid.org/0000-0001-5696-9679, Vukićević, T., Eichhorst, J., Wiesner, B., Weber, M., Kapiloff, M., Rocks, O.
ORCID: https://orcid.org/0000-0001-6349-9193, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Wieland, T., Knapp, S., von Kries, J.P.
ORCID: https://orcid.org/0000-0003-4716-4988 and Klussmann, E.
ORCID: https://orcid.org/0000-0003-4004-5003
PLoS ONE 13
(1): e0191423.
26 January 2018
2017
Anisotropic fluctuations in the ribosome determine tRNA kinetics.
Yang, H.
ORCID: https://orcid.org/0000-0003-3286-3292, Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036 and Whitford, P.C.
ORCID: https://orcid.org/0000-0001-7104-2265
Journal of Physical Chemistry B 121
(47): 10593-10601.
30 November 2017
Molecular simulations suggest a force-dependent mechanism of vinculin activation.
Sun, L., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Levine, H. and Onuchic, J.N.
Biophysical Journal 113
(8): 1697-1710.
17 October 2017
Cryo-EM studies of Drp1 reveal cardiolipin interactions that activate the helical oligomer.
Francy, C.A., Clinton, R.W., Froehlich, C.
ORCID: https://orcid.org/0000-0002-2930-4097, Murphy, C. and Mears, J.A.
Scientific Reports 7
(1): 10744.
6 September 2017
Chlamydia trachomatis prevents apoptosis via activation of PDPK1-MYC and enhanced mitochondrial binding of hexokinase II.
Al-Zeer, M.A., Xavier, A., Abu Lubad, M., Sigulla, J., Kessler, M., Hurwitz, R. and Meyer, T.F.
EBioMedicine 23
: 100-110.
September 2017
Structural basis for aryl hydrocarbon receptor-mediated gene activation.
Schulte, K.W., Green, E., Wilz, A., Platten, M. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Structure 25
(7): 1025-1033.
5 July 2017
Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions.
Hessenberger, M.
ORCID: https://orcid.org/0000-0003-3021-1100, Zerbes, R.M., Rampelt, H., Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, Xavier, A.H., Purfürst, B.
ORCID: https://orcid.org/0000-0002-9887-7577, Lilie, H., Pfanner, N., van der Laan, M. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Nature Communications 8
: 15258.
31 May 2017
Structural insights into the activation mechanism of dynamin-like EHD ATPases.
Melo, A.A., Hegde, B.G., Shah, C., Larsson, E., Isas, J.M., Kunz, S.
ORCID: https://orcid.org/0000-0002-0131-3506, Lundmark, R., Langen, R. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Proceedings of the National Academy of Sciences of the United States of America 114
(22): 5629-5634.
30 May 2017
Mitochondrial homeostasis: How do dimers of mitofusins mediate mitochondrial fusion?
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Roux, A.
Current Biology 27
(9): R353-R356.
8 May 2017
Characterization of the CD177 interaction with the ANCA antigen proteinase 3.
Jerke, U., Marino, S.F.
ORCID: https://orcid.org/0000-0001-5696-9679, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Kettritz, R.
ORCID: https://orcid.org/0000-0001-5821-6718
Scientific Reports 7
: 43328.
27 February 2017
Quantitative GTPase affinity purification identifies Rho family protein interaction partners.
Paul, F.
ORCID: https://orcid.org/0000-0001-5181-3122, Zauber, H.
ORCID: https://orcid.org/0000-0003-2595-1147, von Berg, L., Rocks, O.
ORCID: https://orcid.org/0000-0001-6349-9193, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Selbach, M.
ORCID: https://orcid.org/0000-0003-2454-8751
Molecular & Cellular Proteomics 16
(1): 73-85.
1 January 2017
2016
Membrane fission by dynamin: what we know and what we need to know.
Antonny, B., Burd, C., De Camilli, P., Chen, E., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Faelber, K., Ford, M., Frolov, V.A., Frost, A., Hinshaw, J.E., Kirchhausen, T., Kozlov, M.M., Lenz, M., Low, H.H., McMahon, H., Merrifield, C., Pollard, T.D., Robinson, P.J., Roux, A. and Schmid, S.
EMBO Journal 35
(21): 2270-2284.
2 November 2016
How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome.
Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036 and Whitford, P.C.
Nature Communications 7
: 13314.
31 October 2016
Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.
Arumughan, A., Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Barth, C., Lleras Forero, L., Bravo-Rodriguez, K., Redel, Al., Kostova, S.
ORCID: https://orcid.org/0000-0002-6842-6732, McShane, E.
ORCID: https://orcid.org/0000-0002-7806-2063, Opitz, R.
ORCID: https://orcid.org/0000-0003-3143-0997, Faelber, K., Rau, K., Mielke, T., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Selbach, M.
ORCID: https://orcid.org/0000-0003-2454-8751, Sanchez-Garcia, E., Rocks, O.
ORCID: https://orcid.org/0000-0001-6349-9193, Panáková, D.
ORCID: https://orcid.org/0000-0002-8739-6225, Heinemann, U.
ORCID: https://orcid.org/0000-0002-8191-3850 and Wanker, E.E.
ORCID: https://orcid.org/0000-0001-8072-1630
Nature Communications 7
: 13047.
20 October 2016
Bimodal antagonism of PKA signalling by ARHGAP36.
Eccles, R.L.
ORCID: https://orcid.org/0000-0002-8209-5650, Czajkowski, M.T.
ORCID: https://orcid.org/0000-0002-0122-1943, Barth, C., Müller, P.M.
ORCID: https://orcid.org/0000-0001-9056-4114, McShane, E.
ORCID: https://orcid.org/0000-0002-7806-2063, Grunwald, S.
ORCID: https://orcid.org/0000-0003-3978-6277, Beaudette, P., Mecklenburg, N., Volkmer, R., Zühlke, K., Dittmar, G.
ORCID: https://orcid.org/0000-0003-3647-8623, Selbach, M.
ORCID: https://orcid.org/0000-0003-2454-8751, Hammes, A.
ORCID: https://orcid.org/0000-0003-1663-8378, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Klussmann, E.
ORCID: https://orcid.org/0000-0003-4004-5003, Urbé, S. and Rocks, O.
ORCID: https://orcid.org/0000-0001-6349-9193
Nature Communications 7
: 12963.
7 October 2016
Protein-mediated membrane remodeling.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Unger, V.M.
Journal of Structural Biology 196
(1): 1-2.
October 2016
Lowered pH leads to fusion peptide release and a highly dynamic intermediate of influenza hemagglutinin.
Lin, X.C., Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Wang, Q.H., Ma, J.P. and Onuchic, J.N.
Journal of Physical Chemistry B 120
(36): 9654-9660.
15 September 2016
Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Praefcke, G.J.
Biopolymers 105
(8): 580-593.
August 2016
AKAP18:PKA-RIIα structure reveals crucial anchor points for recognition of regulatory subunits of PKA.
Götz, F., Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Schulz, M.S., Autenrieth, K., Bertinetti, D., Faelber, K., Zühlke, K., Kreuchwig, A., Kennedy, E., Krause, G., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Herberg, F.W., Heinemann, U.
ORCID: https://orcid.org/0000-0002-8191-3850 and Klussmann, E.
ORCID: https://orcid.org/0000-0003-4004-5003
Biochemical Journal 473
(13): 1881-1894.
28 June 2016
SMOG 2: A versatile software package for generating structure-based models.
Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Levi, M., Raghunathan, M., Lammert, H., Hayes, R.L., Onuchic, J.N. and Whitford, P.C.
PLoS Computational Biology 12
(3): e1004794.
10 March 2016
Structure of the hantavirus nucleoprotein provides insights into the mechanism of RNA encapsidation.
Olal, D. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Cell Reports 14
(9): 2092-2099.
8 March 2016
The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion.
Schulte, K., Pawlowski, N., Faelber, K., Fröhlich, C.
ORCID: https://orcid.org/0000-0002-2930-4097, Howard, J. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
BMC Biology 14
(1): 14.
2 March 2016
A complex water network contributes to high-affinity binding in an antibody-antigen interface.
Marino, S.F.
ORCID: https://orcid.org/0000-0001-5696-9679, Olal, D. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Data in Brief 6
: 394-397.
March 2016
Dynamics of the ligand binding domain layer during AMPA receptor activation.
Baranovic, J., Chebli, M., Salazar, H., Carbone, A.L., Faelber, K., Lau, A.Y., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Plested, A.J.R.
Biophysical Journal 110
(4): 896-911.
23 February 2016
Sequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamics.
Noel, J.K.
ORCID: https://orcid.org/0000-0003-3168-6036, Morcos, F. and Onuchic, J.N.
F1000 Research 5
(F1000 Faculty Rev): 106.
26 January 2016
2015
Crystal structure of the dynamin tetramer.
Reubold, T.F., Faelber, K., Plattner, N., Posor, Y., Ketel, K., Curth, U., Schlegel, J., Anand, R., Manstein, D.J., Noé, F., Haucke, V., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Eschenburg, S.
Nature 525
(7569): 404-408.
17 September 2015
Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane.
Senju, Y., Rosenbaum, E., Shah, C., Hamada-Nakahara, S., Itoh, Y., Yamamoto, K., Hanawa-Suetsugu, K., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Suetsugu, S.
Journal of Cell Science 128
(15): 2766-2780.
1 August 2015
Potent anti-tumor response by targeting B cell maturation antigen (BCMA) in a mouse model of multiple myeloma.
Oden, F., Marino, S.F.
ORCID: https://orcid.org/0000-0001-5696-9679, Brand, J., Scheu, S., Kriegel, C., Olal, D., Takvorian, A., Westermann, J., Yilmaz, B., Hinz, M.
ORCID: https://orcid.org/0000-0003-2611-4121, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Höpken, U.E.
ORCID: https://orcid.org/0000-0002-0776-4893, Müller, G. and Lipp, M.
ORCID: https://orcid.org/0000-0002-0087-2672
Molecular Oncology 9
(7): 1348-1358.
August 2015
New role for the (pro)renin receptor in T cell development.
Geisberger, S.
ORCID: https://orcid.org/0000-0001-6477-1312, Maschke, U., Gebhardt, M., Kleinewietfeld, M.
ORCID: https://orcid.org/0000-0002-2832-3149, Manzel, A., Linker, R.A., Chidgey, A., Dechend, R.
ORCID: https://orcid.org/0000-0001-6636-3080, Nguyen, G., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Muller, D.N.
ORCID: https://orcid.org/0000-0003-3650-5644, Wright, M.D. and Binger, K.J.
ORCID: https://orcid.org/0000-0003-1139-3308
Blood 126
(4): 504-507.
23 July 2015
Role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity.
Dick, A.
ORCID: https://orcid.org/0000-0003-0580-1897, Graf, L., Olal, D., von der Malsburg, A., Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, Kochs, G. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Journal of Biological Chemistry 290
(20): 12779-12792.
15 May 2015
2014
Roquin binding to target mRNAs involves a winged helix-turn-helix motif.
Schuetz, A.
ORCID: https://orcid.org/0000-0002-0606-2574, Murakawa, Y., Rosenbaum, E., Landthaler, M.
ORCID: https://orcid.org/0000-0002-1075-8734 and Heinemann, U.
ORCID: https://orcid.org/0000-0002-8191-3850
Nature Communications 5
: 5701.
11 December 2014
Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein.
Olal, D., Dick, A.
ORCID: https://orcid.org/0000-0003-0580-1897, Woods, V.L., Liu, T., Li, S., Devignot, S., Weber, F., Saphire, E.O. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Nucleic Acids Research 42
(9): 6025-6037.
14 May 2014
Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2.
Shah, C., Hegde, B.G., Morén, B., Behrmann, E., Mielke, T., Moenke, G., Spahn, C.M., Lundmark, R., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Langen, R.
Structure 22
(3): 409-420.
4 March 2014
BAR domain scaffolds in dynamin-mediated membrane fission.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Roux, A. and Haucke, V.
Cell 156
(5): 882-892.
27 February 2014
2013
Functional mapping of human dynamin-1-like GTPase domain based on X-ray structure analyses.
Wenger, J., Klinglmayr, E., Fröhlich, C.
ORCID: https://orcid.org/0000-0002-2930-4097, Eibl, C., Gimeno, A., Hessenberger, M.
ORCID: https://orcid.org/0000-0003-3021-1100, Puehringer, S., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Goettig, P.
PLoS ONE 8
(8): e71835.
19 August 2013
Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein.
Fröhlich, C.
ORCID: https://orcid.org/0000-0002-2930-4097, Grabiger, S., Schwefel, D., Faelber, K., Rosenbaum, E., Mears, J., Rocks, O.
ORCID: https://orcid.org/0000-0001-6349-9193 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
EMBO Journal 32
(9): 1280-1292.
2 May 2013
Structural insights into the mechanism of GTPase activation in the GIMAP family.
Schwefel, D., Arasu, B.S.
ORCID: https://orcid.org/0000-0003-4168-8617, Marino, S.F.
ORCID: https://orcid.org/0000-0001-5696-9679, Lamprecht, B., Köchert, K.
ORCID: https://orcid.org/0000-0002-5548-2022, Rosenbaum, E., Eichhorst, J., Wiesner, B., Behlke, J., Rocks, O.
ORCID: https://orcid.org/0000-0001-6349-9193, Mathas, S.
ORCID: https://orcid.org/0000-0001-9626-1413 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Structure 21
(4): 550-559.
2 April 2013
Oligomerization of dynamin superfamily proteins in health and disease.
Faelber, K., Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, Held, M., Posor, Y., Haucke, V., Noé, F. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Progress in Molecular Biology and Translational Science 117
: 411-443.
2013
2012
Structural insights into dynamin-mediated membrane fission.
Faelber, K., Held, M., Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, Posor, Y., Haucke, V., Noe, F. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Structure 20
(10): 1621-1628.
10 October 2012
Sarcolemmal repair is a slow process and includes EHD2.
Marg, A.
ORCID: https://orcid.org/0000-0003-3673-4244, Schoewel, V.
ORCID: https://orcid.org/0000-0002-5924-3088, Timmel, T., Schulze, A., Shah, C., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Spuler, S.
ORCID: https://orcid.org/0000-0002-0155-1117
Traffic 13
(9): 1286-1294.
September 2012
A stomatin dimer modulates the activity of acid-sensing ion channels.
Brand, J., Smith, E.S.J.
ORCID: https://orcid.org/0000-0002-2699-1979, Schwefel, D., Lapatsina, L., Poole, K.
ORCID: https://orcid.org/0000-0003-0879-6093, Omerbasic, D.
ORCID: https://orcid.org/0000-0003-1839-4856, Kozlenkov, A., Behlke, J., Lewin, G.R.
ORCID: https://orcid.org/0000-0002-2890-6352 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
EMBO Journal 31
(17): 3635-3646.
29 August 2012
Stomatin-domain proteins.
Lapatsina, L., Brand, J., Poole, K.
ORCID: https://orcid.org/0000-0003-0879-6093, Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Lewin, G.R.
ORCID: https://orcid.org/0000-0002-2890-6352
European Journal of Cell Biology 91
(4): 240-245.
April 2012
EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization.
Moren, B., Shah, C., Howes, M.T., Schieber, N.L., McMahon, H.T., Parton, R.G., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Lundmark, R.
Molecular Biology of the Cell 23
(7): 1316-1329.
9 February 2012
2011
Structure of myxovirus resistance protein A reveals intra- and intermolecular domain interactions required for the antiviral function.
Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, von der Malsburg, A., Dick, A.
ORCID: https://orcid.org/0000-0003-0580-1897, Faelber, K., Schroeder, G.F., Haller, O., Kochs, G. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Immunity 35
(4): 514-525.
28 October 2011
Crystal structure of nucleotide-free dynamin.
Faelber, K., Posor, Y., Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, Held, M., Roske, Y.
ORCID: https://orcid.org/0000-0001-6237-388X, Schulze, D., Haucke, V., Noe, F. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Nature 477
(7366): 556-560.
29 September 2011
Crystal structures of the bacterial solute receptor AcbH displaying an exclusive substrate preference for beta-D-galactopyranose.
Licht, A., Bulut, H.
ORCID: https://orcid.org/0000-0003-0262-6296, Scheffel, F.M., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Wehmeier, U.F., Saenger, W., Schneider, E. and Vahedi-Faridi, A.
Journal of Molecular Biology 406
(1): 92-105.
11 February 2011
Structural insights into membrane fusion at the endoplasmic reticulum.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Praefcke, G.J.
Proceedings of the National Academy of Sciences of the United States of America 108
(6): 2175-2176.
8 February 2011
GTP-dependent scaffold formation in the GTPase of Immunity Associated Protein family.
Schwefel, D. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Small GTPases 2
(1): 27-30.
January 2011
2010
Structure of a classical MHC class I molecule that binds "non-classical" ligands.
Hee, C.S., Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, Loll, B., Miller, M.M., Uchanska-Ziegler, B., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Ziegler, A.
PLoS Biology 8
(12): e1000557.
7 December 2010
Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2).
Schwefel, D., Froehlich, C.
ORCID: https://orcid.org/0000-0002-2930-4097, Eichhorst, J., Wiesner, B., Behlke, J., Aravind, L. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Proceedings of the National Academy of Sciences of the United States of America 107
(47): 20299-20304.
23 November 2010
Dynamin-like MxA GTPase: Structural insights into oligomerization and implications for antiviral activity.
Haller, O., Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, von der Malsburg, A., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Kochs, G.
Journal of Biological Chemistry 285
(37): 28419-28424.
10 September 2010
Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, von der Malsburg, A., Haller, O. and Kochs, G.
Small GTPases 1
(1): 62-64.
July 2010
Purification, crystallization and preliminary X-ray analysis of human GIMAP2.
Schwefel, D., Froehlich, C.
ORCID: https://orcid.org/0000-0002-2930-4097 and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Acta Crystallographica Section F 66
(6): 725-729.
1 June 2010
Structural basis of oligomerization in the stalk region of dynamin-like MxA.
Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, von der Malsburg, A., Paeschke, S., Behlke, J., Haller, O., Kochs, G. and Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414
Nature 465
(7297): 502-506.
27 May 2010
2009
Host cell interactome of tyrosine-phosphorylated bacterial proteins.
Selbach, M.
ORCID: https://orcid.org/0000-0003-2454-8751, Paul, F.E.
ORCID: https://orcid.org/0000-0001-5181-3122, Brandt, S., Guye, P., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Backert, S., Dehio, C. and Mann, M.
Cell Host & Microbe 5
(4): 397-403.
23 April 2009
Expression, purification and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule YF1*7.1.
Hee, C.S., Gao, S.
ORCID: https://orcid.org/0000-0001-7427-6681, Miller, M.M., Goto, R.M., Ziegler, A., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Uchanska-Ziegler, B.
Acta Crystallographica Section F 65
(Pt 4): 422-425.
1 April 2009
2007
Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Lundmark, R., Vallis, Y., Martens, S., Butler, P.J.G. and McMahon, H.T.
Nature 449
(7164): 923-927.
3 October 2007
Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature.
Henne, W.M., Kent, H.M., Ford, M.G.J., Hegde, B.G., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Butler, P.J.G., Mittal, R., Langen, R., Evans, P.R. and McMahon, H.T.
Structure 15
(7): 839-52.
July 2007
Insight into catalysis of a unique GTPase reaction by a combined biochemical and FTIR approach.
Chakrabarti, P.P., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Suveyzdis, Y., Koetting, C., Gerwert, K. and Wittinghofer, A.
Journal of Molecular Biology 367
(4): 983-95.
6 April 2007
2006
GAP1 family members constitute bifunctional Ras and Rap GTPase-activating proteins.
Kupzig, S., Deaconescu, D., Bouyoucef, D., Walker, S.A., Liu, Q., Polte, C.L., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Ishizaki, T., Lockyer, P.J., Wittinghofer, A. and Cullen, P.J.
Journal of Biological Chemistry 281
(15): 9891-900.
14 April 2006
2005
Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold.
Rossbach, M., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Klinger, C., Wittinghofer, A. and Kaufmann, M.
BMC Structural Biology 5
: 7.
20 March 2005
2004
Synthesis of GTP-derived Ras ligands.
Soulère, L., Aldrich, C., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Gail, R., Kissau, L., Wittinghofer, A. and Waldmann, H.
ChemBioChem 5
(10): 1448-53.
4 October 2004
The GTPase-activating protein Rap1GAP uses a catalytic asparagine.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Weyand, M., Chakrabarti, P.P., Vetter, I.R. and Wittinghofer, A.
Nature 429
(6988): 197-201.
13 May 2004
Purification, crystallization and preliminary structural characterization of human Rap1GAP.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Wittinghofer, A. and Weyand, M.
Acta Crystallographica Section D - Biological Crystallography 60
(Pt 4): 752-4.
April 2004
2002
Rap-specific GTPase activating protein follows an alternative mechanism.
Brinkmann, T., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Herbrand, U., Kühlmann, D., Stege, P., Ahmadian, M.R. and Wittinghofer, A.
Journal of Biological Chemistry 277
(15): 12525-31.
12 April 2002
2001
Functional asymmetry of the ATP-binding-cassettes of the ABC transporter TAP is determined by intrinsic properties of the nucleotide binding domains.
Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414 and Knittler, M.R.
European Journal of Biochemistry 268
(17): 4776-86.
September 2001
Distinct functional properties of the TAP subunits coordinate the nucleotide-dependent transport cycle.
Alberts, P., Daumke, O.
ORCID: https://orcid.org/0000-0002-6190-1414, Deverson, E.V., Howard, J.C. and Knittler, M.R.
Current Biology 11
(4): 242-51.
20 February 2001
This list was generated on Mon Jun 22 22:40:19 2026 UTC.