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Pathogenic mutations of human phosphorylation sites affect protein–protein interactions.
Rrustemi, T. and Meyer, K. and Roske, Y. and Uyar, B. and Akalin, A. and Imami, K. and Ishihama, Y. and Daumke, O. and Selbach, M.
Nature Communications 15 (1): 3146. 11 April 2024

Structural insights into the activation mechanism of antimicrobial GBP1.
Weismehl, M. and Chu, X. and Kutsch, M. and Lauterjung, P. and Herrmann, C. and Kudryashev, M. and Daumke, O.
EMBO Journal 43 (4): 615-636. 15 February 2024

GIMAP5 deficiency reveals a mammalian ceramide-driven longevity assurance pathway.
Park, A.Y. and Leney-Greene, M. and Lynberg, M. and Gabrielski, J.Q. and Xu, X. and Schwarz, B. and Zheng, L. and Balasubramaniyam, A. and Ham, H. and Chao, B. and Zhang, Y. and Matthews, H.F. and Cui, J. and Yao, Y. and Kubo, S. and Chanchu, J.M. and Morawski, A.R. and Cook, S.A. and Jiang, P. and Ravell, J.C. and Cheng, Y.H. and George, A. and Faruqi, A. and Pagalilauan, A.M. and Bergerson, J.R.E. and Ganesan, S. and Chauvin, S.D. and Aluri, J. and Edwards-Hicks, J. and Bohrnsen, E. and Tippett, C. and Omar, H. and Xu, L. and Butcher, G.W. and Pascall, J. and Karakoc-Aydiner, E. and Kiykim, A. and Maecker, H. and Tezcan, İ. and Esenboga, S. and Heredia, R.J. and Akata, D. and Tekin, S. and Kara, A. and Kuloglu, Z. and Unal, E. and Kendirli, T. and Dogu, F. and Karabiber, E. and Atkinson, T.P. and Cochet, C. and Filhol, O. and Bosio, C.M. and Davis, M.M. and Lifton, R.P. and Pearce, E.L. and Daumke, O. and Aytekin, C. and Şahin, G.E. and Aksu, A.Ü. and Uzel, G. and Koneti Rao, V. and Sari, S. and Boztug, K. and Cagdas, D. and Haskologlu, S. and Ikinciogullari, A. and Schwefel, D. and Vilarinho, S. and Baris, S. and Ozen, A. and Su, H.C. and Lenardo, M.J.
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. and Cappel, C. and Cremer, N. and Hoffmann, P. and Koudelka, T. and Tholey, A. and Heinemann, U. and Daumke, O. and Damme, M.
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. and Haglund, E.
Journal of Physical Chemistry B 128 (1): 117-124. 11 January 2024

Transcriptional reprogramming by mutated IRF4 in lymphoma.
Schleussner, N. and Cauchy, P. and Franke, V. and Giefing, M. and Fornes, O. and Vankadari, N. and Assi, S.A. and Costanza, M. and Weniger, M.A. and Akalin, A. and Anagnostopoulos, I. and Bukur, T. and Casarotto, M.G. and Damm, F. and Daumke, O. and Edginton-White, B. and Gebhardt, J.C.M. and Grau, M. and Grunwald, S. and Hansmann, M.L. and Hartmann, S. and Huber, L. and Kärgel, E. and Lusatis, S. and Noerenberg, D. and Obier, N. and Pannicke, U. and Fischer, A. and Reisser, A. and Rosenwald, A. and Schwarz, K. and Sundararaj, S. and Weilemann, A. and Winkler, W. and Xu, W. and Lenz, G. and Rajewsky, K. and Wasserman, W.W. and Cockerill, P.N. and Scheidereit, C. and Siebert, R. and Küppers, R. and Grosschedl, R. and Janz, M. and Bonifer, C. and Mathas, S.
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. and Stolzenberg, S. and Sticht, J. and Wieczorek, M. and Roske, Y. and Günther, M. and Dähn, S. and Boesen, B.B. and Calvo, M.M. and Biese, C. and Kuppler, F. and Medina-García, Á. and Álvaro-Benito, M. and Höfer, T. and Noé, F. and Freund, C.
Nature Chemical Biology 19 (10): 1196-1204. October 2023

A multimorphic mutation in IRF4 causes human autosomal dominant combined immunodeficiency.
Fornes, O. and Jia, A. and Kuehn, H.S. and Min, Q. and Pannicke, U. and Schleussner, N. and Thouenon, R. and Yu, Z. and de Los Angeles Astbury, M. and Biggs, C.M. and Galicchio, M. and Garcia-Campos, J.A. and Gismondi, S. and Gonzalez Villarreal, G. and Hildebrand, K.J. and Hönig, M. and Hou, J. and Moshous, D. and Pittaluga, S. and Qian, X. and Rozmus, J. and Schulz, A.S. and Staines-Boone, A.T. and Sun, B. and Sun, J. and Uwe, S. and Venegas-Montoya, E. and Wang, W. and Wang, X. and Ying, W. and Zhai, X. and Zhou, Q. and Akalin, A. and André, I. and Barth, T.F.E. and Baumann, B. and Brüstle, A. and Burgio, G. and Bustamante, J.C. and Casanova, J.L. and Casarotto, M.G. and Cavazzana, M. and Chentout, L. and Cockburn, I.A. and Costanza, M. and Cui, C. and Daumke, O. and Del Bel, K.L. and Eibel, H. and Feng, X. and Franke, V. and Gebhardt, J.C.M. and Götz, A. and Grunwald, S. and Hoareau, B. and Hughes, T.R. and Jacobsen, E.M. and Janz, M. and Jolma, A. and Lagresle-Peyrou, C. and Lai, N. and Li, Y. and Lin, S. and Lu, H.Y. and Lugo-Reyes, S.O. and Meng, X. and Möller, P. and Moreno-Corona, N. and Niemela, J.E. and Novakovsky, G. and Perez-Caraballo, J.J. and Picard, C. and Poggi, L. and Puig-Lombardi, M.E. and Randall, K.L. and Reisser, A. and Schmitt, Y. and Seneviratne, S. and Sharma, M. and Stoddard, J. and Sundararaj, S. and Sutton, H. and Tran, L.Q. and Wang, Y. and Wasserman, W.W. and Wen, Z. and Winkler, W. and Xiong, E. and Yang, A.W.H. and Yu, M. and Zhang, L. and Zhang, H. and Zhao, Q. and Zhen, X. and Enders, A. and Kracker, S. and Martinez-Barricarte, R. and Mathas, S. and Rosenzweig, S.D. and Schwarz, K. and 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. and Belabed, H. and Kücükdisli, M. and Metag, J. and Roske, Y. and Prokofeva, P. and Ohashi, Y. and Horatscheck, A. and Cirillo, D. and Krauss, M. and Schmied, C. and Neuenschwander, M. and von Kries, J.P. and Médard, G. and Kuster, Be. and Perisic, O. and Williams, R.L. and Daumke, O. and Payrastre, B. and Severin, S. and Nazaré, M. and Haucke, V.
Nature Chemical Biology 19 (1): 18-27. January 2023

Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.
Melo, A.A. and Sprink, T. and Noel, J.K. and Vázquez-Sarandeses, E. and van Hoorn, C. and Mohd, S. and Loerke, J. and Spahn, C.M.T. and Daumke, O.
Nature Communications 13 (1): 7641. 10 December 2022

Structural insights into crista junction formation by the Mic60-Mic19 complex.
Bock-Bierbaum, T. and Funck, K. and Wollweber, F. and Lisicki, E. and von der Malsburg, K. and von der Malsburg, A. and Laborenz, J. and Noel, J.K. and Hessenberger, M. and Jungbluth, S. and Bernert, C. and Kunz, S. and Riedel, D. and Lilie, H. and Jakobs, S. and van der Laan, M. and Daumke, O.
Science Advances 8 (35): eabo4946. 2 September 2022

GIMAP6 regulates autophagy, immune competence, and inflammation in mice and humans.
Yao, Y. and Du Jiang, P. and Chao, B.N. and Cagdas, D. and Kubo, S. and Balasubramaniyam, A. and Zhang, Y. and Shadur, B. and NaserEddin, A. and Folio, L.R. and Schwarz, B. and Bohrnsen, E. and Zheng, L. and Lynberg, M. and Gottlieb, S. and Leney-Greene, M.A. and Park, A.Y. and Tezcan, I. and Akdogan, A. and Gocmen, R. and Onder, S. and Rosenberg, A. and Soilleux, E.J. and Johnson, E. and Jackson, P.K. and Demeter, J. and Chauvin, S.D. and Paul, F. and Selbach, M. and Bulut, H. and Clatworthy, M.R. and Tuong, Z.K. and Zhang, H. and Stewart, B.J. and Bosio, C.M. and Stepensky, P. and Clare, S. and Ganesan, S. and Pascall, J.C. and Daumke, O. and Butcher, G.W. and McMichael, A.J. and Simon, A.K. and Lenardo, M.J.
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. and Jerke, U. and Rolle, S. and Daumke, O. and Kettritz, R.
Journal of Biological Chemistry 298 (3): 101598. March 2022

Structural basis of phosphatidylinositol 3-kinase C2α function.
Lo, W.T. and Zhang, Y. and Vadas, O. and Roske, Y. and Gulluni, F. and De Santis, M.C. and Zagar, A.V. and Stephanowitz, H. and Hirsch, E. and Liu, F. and Daumke, O. and Kudryashev, M. and Haucke, V.
Nature Structural & Molecular Biology 29 (3): 218-228. March 2022

SMOG 2 and OpenSMOG: extending the limits of structure-based models.
de Oliveira, A.B. and Contessoto, V.G. and Hassan, A. and Byju, S. and Wang, A. and Wang, Y. and Dodero-Rojas, E. and Mohanty, U. and Noel, J.K. and Onuchic, J.N. and Whitford, P.C.
Protein Science 31 (1): 158-172. January 2022

Lysine acetylation regulates the interaction between proteins and membranes.
Okada, A.K. and Teranishi, K. and Ambroso, M.R. and Isas, J.M. and Vazquez-Sarandeses, E. and Lee, J.Y. and Melo, A.A. and Pandey, P. and Merken, D. and Berndt, L. and Lammers, M. and Daumke, O. and Chang, K. and Haworth, I.S. and Langen, R.
Nature Communications 12 (1): 6466. 9 November 2021

A simple pressure-assisted method for MicroED specimen preparation.
Zhao, J. and Xu, H. and Lebrette, H. and Carroni, M. and Taberman, H. and Högbom, M. and Zou, X.
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. and Vancraenenbroeck, R. and Rosenblum, G. and Hofmann, H. and Mikhailov, A.S. and Daumke, O. and Noel, J.K.
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. and Tassinari, M. and Souza, D.P. and Naskar, S. and Noel, J.K. and Bohuszewicz, O. and Buck, M. and Williams, T.A. and 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 and Grunwald, S. and Gimber, N. and Popp, O. and Dittmar, G. and Arumughan, A. and Wanker, E.E. and Laeger, T. and Schmoranzer, J. and Daumke, O. and Schümann, A.
Molecular Metabolism 45 : 101151. March 2021

Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.
Grunwald, S. and Hopf, L.V.M. and Bock-Bierbaum, T. and Lally, C.C.M. and Spahn, C.M.T. and Daumke, O.
Nature Communications 11 (1): 5506. 2 November 2020

Monogenic variants in dystonia: an exome-wide sequencing study.
Zech, M. and Jech, R. and Boesch, S. and Škorvánek, M. and Weber, S. and Wagner, M. and Zhao, C. and Jochim, A. and Necpál, J. and Dincer, Y. and Vill, K. and Distelmaier, F. and Stoklosa, M. and Krenn, M. and Grunwald, S. and Bock-Bierbaum, T. and Fečíková, A. and Havránková, P. and Roth, J. and Příhodová, I. and Adamovičová, M. and Ulmanová, O. and Bechyně, K. and Danhofer, P. and Veselý, B. and Haň, V. and Pavelekova, P. and Gdovinová, Z. and Mantel, T. and Meindl, T. and Sitzberger, A. and Schröder, S. and Blaschek, A. and Roser, T. and Bonfert, M.V. and Haberlandt, E. and Plecko, B. and Leineweber, B. and Berweck, S. and Herberhold, T. and Langguth, B. and Švantnerová, J. and Minár, M. and Ramos-Rivera, G.A. and Wojcik, M.H. and Pajusalu, S. and Õunap, K. and Schatz, U.A. and Pölsler, L. and Milenkovic, I. and Laccone, F. and Pilshofer, V. and Colombo, R. and Patzer, S. and Iuso, A. and Vera, J. and Troncoso, M. and Fang, F. and Prokisch, H. and Wilbert, F. and Eckenweiler, M. and Graf, E. and Westphal, D.S. and Riedhammer, K.M. and Brunet, T. and Alhaddad, B. and Berutti, R. and Strom, T.M. and Hecht, M. and Baumann, M. and Wolf, M. and Telegrafi, A. and Person, R.E. and Zamora, F.M. and Henderson, L.B. and Weise, D. and Musacchio, T. and Volkmann, J. and Szuto, A. and Becker, J. and Cremer, K. and Sycha, T. and Zimprich, F. and Kraus, V. and Makowski, C. and Gonzalez-Alegre, P. and Bardakjian, T.M. and Ozelius, L.J. and Vetro, A. and Guerrini, R. and Maier, E. and Borggraefe, I. and Kuster, A. and Wortmann, S.B. and Hackenberg, A. and Steinfeld, R. and Assmann, B. and Staufner, C. and Opladen, T. and Růžička, E. and Cohn, R.D. and Dyment, D. and Chung, W.K. and Engels, H. and Ceballos-Baumann, A. and Ploski, R. and Daumke, O. and Haslinger, B. and Mall, V. and 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. and Al-Zeer, M.A. and Meyer, T.F. and Daumke, O.
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. and Noel, J.K. and Simien, J.M. and Duggan, B.M. and Oliveberg, M. and Onuchic, J.N. and 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. and Kaßmann, M. and Cui, Y. and Matthaeus, C. and Kunz, S. and Zhong, C. and Zhu, S. and Xie, Yu and Tsvetkov, D. and Daumke, O. and Huang, Yu and Gollasch, M.
Aging Cell 19 (4): e13134. April 2020

EHD2-mediated restriction of caveolar dynamics regulates cellular fatty acid uptake.
Matthaeus, C. and Lahmann, I. and Kunz, S. and Jonas, W. and Melo, A.A. and Lehmann, M. and Larsson, E. and Lundmark, R. and Kern, M. and Blüher, M. and Olschowski, H. and Kompa, J. and Brügger, B. and Müller, D.N. and Haucke, V. and Schürmann, A. and Birchmeier, C. and Daumke, O.
Proceedings of the National Academy of Sciences of the United States of America 117 (13): 7471-7481. 31 March 2020

Polymer-like model to study the dynamics of dynamin filaments on deformable membrane tubes.
Noel, J.K. and Noé, F. and Daumke, O. 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. and Lian, X. and Kunz, S. and Lehmann, M. and Zhong, C. and Bernert, C. and Lahmann, I. and Müller, D.N. and Gollasch, M. and Daumke, O.
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. and Rahjouei, A. and Andreani, M. and Tupiņa, D. and Balasubramanian, S. and Saha, T. and Delgado-Benito, V. and Coralluzzo, V. and Daumke, O. and Di Virgilio, M.
Cell Reports 28 (6): 1389-1399. 6 August 2019

Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1.
Faelber, K. and Dietrich, L. and Noel, J.K. and Wollweber, F. and Pfitzner, A.K. and Mühleip, A. and Sánchez, R. and Kudryashev, M. and Chiaruttini, N. and Lilie, H. and Schlegel, J. and Rosenbaum, E. and Hessenberger, M. and Matthaeus, C. and Kunz, S. and von der Malsburg, A. and Noé, F. and Roux, A. and van der Laan, M. and Kühlbrandt, W. and Daumke, O.
Nature 571 (7765): 429-433. 18 July 2019

Studying ribosome dynamics with simplified models.
Levi, M. and Noel, J.K. 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. and Witt, M. and Abert, C. and Bock-Bierbaum, T. and Su, M.Y. and Trapannone, R. and Sztacho, M. and Danieli, A. and Shi, X. and Zaffagnini, G. and Gamper, A. and Schuschnig, M. and Fracchiolla, D. and Bernklau, D. and Romanov, J. and Hartl, M. and Hurley, J.H. and Daumke, O. 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. and Kärgel, E. and Franke, V. and McShane, E. and Schulz-Beiss, K.W. and Patone, G. and Schleussner, N. and Kolesnichenko, M. and Hübner, N. and Daumke, O. and Selbach, M. and Akalin, A. and Mathas, S. and Scheidereit, C.
Blood 133 (13): 1489-1494. 28 March 2019

A SEPT1-based scaffold is required for Golgi integrity and function.
Song, K. and Gras, C. and Capin, G. and Gimber, N. and Lehmann, M. and Mohd, S. and Puchkov, D. and Rödiger, M. and Wilhelmi, I. and Daumke, O. and Schmoranzer, J. and 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. and Bandarkar, P. and Yang, H. and Wang, A. and Mohanty, U. and Noel, J.K. and Whitford, P.C.
Methods in Molecular Biology 2022 : 129-151. 2019

Atomistic simulations indicate the functional loop-to-coiled-coil transition in influenza hemagglutinin is not downhill.
Lin, X. and Noel, J.K. and Wang, Q. and 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. and Noel, J.K. 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. and Dick, A. and Sendker, F. and Barth, E. and Marz, M. and Daumke, O. 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. and Tröger, J. and Eldahshan, A. and Zühlke, K. and Abdul Azeez, K.R. and Elkins, J.M. and Neuenschwander, M. and Oder, A. and Elkewedi, M.M.H. and Jaksch, S. and Andrae, K. and Li, J. and Fernandes, J. and Müller, P.M. and Grunwald, S. and Marino, S.F. and Vukićević, T. and Eichhorst, J. and Wiesner, B. and Weber, M. and Kapiloff, M. and Rocks, O. and Daumke, O. and Wieland, T. and Knapp, S. and von Kries, J.P. and Klussmann, E.
PLoS ONE 13 (1): e0191423. 26 January 2018

Anisotropic fluctuations in the ribosome determine tRNA kinetics.
Yang, H. and Noel, J.K. and Whitford, P.C.
Journal of Physical Chemistry B 121 (47): 10593-10601. 30 November 2017

Molecular simulations suggest a force-dependent mechanism of vinculin activation.
Sun, L. and Noel, J.K. and 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. and Clinton, R.W. and Froehlich, C. and 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. and Xavier, A. and Abu Lubad, M. and Sigulla, J. and Kessler, M. and Hurwitz, R. and Meyer, T.F.
EBioMedicine 23 : 100-110. September 2017

Structural basis for aryl hydrocarbon receptor-mediated gene activation.
Schulte, K.W. and Green, E. and Wilz, A. and Platten, M. and Daumke, O.
Structure 25 (7): 1025-1033. 5 July 2017

Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions.
Hessenberger, M. and Zerbes, R.M. and Rampelt, H. and Kunz, S. and Xavier, A.H. and Purfürst, B. and Lilie, H. and Pfanner, N. and van der Laan, M. and Daumke, O.
Nature Communications 8 : 15258. 31 May 2017

Structural insights into the activation mechanism of dynamin-like EHD ATPases.
Melo, A.A. and Hegde, B.G. and Shah, C. and Larsson, E. and Isas, J.M. and Kunz, S. and Lundmark, R. and Langen, R. and Daumke, O.
Proceedings of the National Academy of Sciences of the United States of America 114 (22): 5629-5634. 30 May 2017

Characterization of the CD177 interaction with the ANCA antigen proteinase 3.
Jerke, U. and Marino, S.F. and Daumke, O. and Kettritz, R.
Scientific Reports 7 : 43328. 27 February 2017

Quantitative GTPase affinity purification identifies Rho family protein interaction partners.
Paul, F. and Zauber, H. and von Berg, L. and Rocks, O. and Daumke, O. and Selbach, M.
Molecular & Cellular Proteomics 16 (1): 73-85. 1 January 2017

How EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosome.
Noel, J.K. 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. and Roske, Y. and Barth, C. and Lleras Forero, L. and Bravo-Rodriguez, K. and Redel, Al. and Kostova, S. and McShane, E. and Opitz, R. and Faelber, K. and Rau, K. and Mielke, T. and Daumke, O. and Selbach, M. and Sanchez-Garcia, E. and Rocks, O. and Panáková, D. and Heinemann, U. and Wanker, E.E.
Nature Communications 7 : 13047. 20 October 2016

Bimodal antagonism of PKA signalling by ARHGAP36.
Eccles, R.L. and Czajkowski, M.T. and Barth, C. and Müller, P.M. and McShane, E. and Grunwald, S. and Beaudette, P. and Mecklenburg, N. and Volkmer, R. and Zühlke, K. and Dittmar, G. and Selbach, M. and Hammes, A. and Daumke, O. and Klussmann, E. and Urbé, S. and Rocks, O.
Nature Communications 7 : 12963. 7 October 2016

Lowered pH leads to fusion peptide release and a highly dynamic intermediate of influenza hemagglutinin.
Lin, X.C. and Noel, J.K. and Wang, Q.H. and Ma, J.P. and Onuchic, J.N.
Journal of Physical Chemistry B 120 (36): 9654-9660. 15 September 2016

AKAP18:PKA-RIIα structure reveals crucial anchor points for recognition of regulatory subunits of PKA.
Götz, F. and Roske, Y. and Schulz, M.S. and Autenrieth, K. and Bertinetti, D. and Faelber, K. and Zühlke, K. and Kreuchwig, A. and Kennedy, E. and Krause, G. and Daumke, O. and Herberg, F.W. and Heinemann, U. and Klussmann, E.
Biochemical Journal 473 (13): 1881-1894. 28 June 2016

SMOG 2: A versatile software package for generating structure-based models.
Noel, J.K. and Levi, M. and Raghunathan, M. and Lammert, H. and Hayes, R.L. and 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.
Cell Reports 14 (9): 2092-2099. 8 March 2016

The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion.
Schulte, K. and Pawlowski, N. and Faelber, K. and Fröhlich, C. and Howard, J. and Daumke, O.
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. and Olal, D. and Daumke, O.
Data in Brief 6 : 394-397. March 2016

Dynamics of the ligand binding domain layer during AMPA receptor activation.
Baranovic, J. and Chebli, M. and Salazar, H. and Carbone, A.L. and Faelber, K. and Lau, A.Y. and Daumke, O. and Plested, A.J.R.
Biophysical Journal 110 (4): 896-911. 23 February 2016

Crystal structure of the dynamin tetramer.
Reubold, T.F. and Faelber, K. and Plattner, N. and Posor, Y. and Ketel, K. and Curth, U. and Schlegel, J. and Anand, R. and Manstein, D.J. and Noé, F. and Haucke, V. and Daumke, O. 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. and Rosenbaum, E. and Shah, C. and Hamada-Nakahara, S. and Itoh, Y. and Yamamoto, K. and Hanawa-Suetsugu, K. and Daumke, O. 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. and Marino, S.F. and Brand, J. and Scheu, S. and Kriegel, C. and Olal, D. and Takvorian, A. and Westermann, J. and Yilmaz, B. and Hinz, M. and Daumke, O. and Höpken, U.E. and Müller, G. and Lipp, M.
Molecular Oncology 9 (7): 1348-1358. August 2015

New role for the (pro)renin receptor in T cell development.
Geisberger, S. and Maschke, U. and Gebhardt, M. and Kleinewietfeld, M. and Manzel, A. and Linker, R.A. and Chidgey, A. and Dechend, R. and Nguyen, G. and Daumke, O. and Muller, D.N. and Wright, M.D. and Binger, K.J.
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. and Graf, L. and Olal, D. and von der Malsburg, A. and Gao, S. and Kochs, G. and Daumke, O.
Journal of Biological Chemistry 290 (20): 12779-12792. 15 May 2015

Roquin binding to target mRNAs involves a winged helix-turn-helix motif.
Schuetz, A. and Murakawa, Y. and Rosenbaum, E. and Landthaler, M. and Heinemann, U.
Nature Communications 5 : 5701. 11 December 2014

Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein.
Olal, D. and Dick, A. and Woods, V.L. and Liu, T. and Li, S. and Devignot, S. and Weber, F. and Saphire, E.O. and Daumke, O.
Nucleic Acids Research 42 (9): 6025-6037. 14 May 2014

Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2.
Shah, C. and Hegde, B.G. and Morén, B. and Behrmann, E. and Mielke, T. and Moenke, G. and Spahn, C.M. and Lundmark, R. and Daumke, O. and Langen, R.
Structure 22 (3): 409-420. 4 March 2014

Functional mapping of human dynamin-1-like GTPase domain based on X-ray structure analyses.
Wenger, J. and Klinglmayr, E. and Fröhlich, C. and Eibl, C. and Gimeno, A. and Hessenberger, M. and Puehringer, S. and Daumke, O. 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. and Grabiger, S. and Schwefel, D. and Faelber, K. and Rosenbaum, E. and Mears, J. and Rocks, O. and Daumke, O.
EMBO Journal 32 (9): 1280-1292. 2 May 2013

Structural insights into the mechanism of GTPase activation in the GIMAP family.
Schwefel, D. and Arasu, B.S. and Marino, S.F. and Lamprecht, B. and Köchert, K. and Rosenbaum, E. and Eichhorst, J. and Wiesner, B. and Behlke, J. and Rocks, O. and Mathas, S. and Daumke, O.
Structure 21 (4): 550-559. 2 April 2013

Sarcolemmal repair is a slow process and includes EHD2.
Marg, A. and Schoewel, V. and Timmel, T. and Schulze, A. and Shah, C. and Daumke, O. and Spuler, S.
Traffic 13 (9): 1286-1294. September 2012

A stomatin dimer modulates the activity of acid-sensing ion channels.
Brand, J. and Smith, E.S.J. and Schwefel, D. and Lapatsina, L. and Poole, K. and Omerbasic, D. and Kozlenkov, A. and Behlke, J. and Lewin, G.R. and Daumke, O.
EMBO Journal 31 (17): 3635-3646. 29 August 2012

EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization.
Moren, B. and Shah, C. and Howes, M.T. and Schieber, N.L. and McMahon, H.T. and Parton, R.G. and Daumke, O. and Lundmark, R.
Molecular Biology of the Cell 23 (7): 1316-1329. 9 February 2012

Structure of myxovirus resistance protein A reveals intra- and intermolecular domain interactions required for the antiviral function.
Gao, S. and von der Malsburg, A. and Dick, A. and Faelber, K. and Schroeder, G.F. and Haller, O. and Kochs, G. and Daumke, O.
Immunity 35 (4): 514-525. 28 October 2011

Crystal structure of nucleotide-free dynamin.
Faelber, K. and Posor, Y. and Gao, S. and Held, M. and Roske, Y. and Schulze, D. and Haucke, V. and Noe, F. and Daumke, O.
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. and Bulut, H. and Scheffel, F.M. and Daumke, O. and Wehmeier, U.F. and Saenger, W. and Schneider, E. and Vahedi-Faridi, A.
Journal of Molecular Biology 406 (1): 92-105. 11 February 2011

GTP-dependent scaffold formation in the GTPase of Immunity Associated Protein family.
Schwefel, D. and Daumke, O.
Small GTPases 2 (1): 27-30. January 2011

Structure of a classical MHC class I molecule that binds "non-classical" ligands.
Hee, C.S. and Gao, S. and Loll, B. and Miller, M.M. and Uchanska-Ziegler, B. and Daumke, O. 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. and Froehlich, C. and Eichhorst, J. and Wiesner, B. and Behlke, J. and Aravind, L. and Daumke, O.
Proceedings of the National Academy of Sciences of the United States of America 107 (47): 20299-20304. 23 November 2010

Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module.
Daumke, O. and Gao, S. and von der Malsburg, A. and 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. and Froehlich, C. and Daumke, O.
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. and von der Malsburg, A. and Paeschke, S. and Behlke, J. and Haller, O. and Kochs, G. and Daumke, O.
Nature 465 (7297): 502-506. 27 May 2010

Host cell interactome of tyrosine-phosphorylated bacterial proteins.
Selbach, M. and Paul, F.E. and Brandt, S. and Guye, P. and Daumke, O. and Backert, S. and 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. and Gao, S. and Miller, M.M. and Goto, R.M. and Ziegler, A. and Daumke, O. and Uchanska-Ziegler, B.
Acta Crystallographica Section F 65 (Pt 4): 422-425. 1 April 2009

Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling.
Daumke, O. and Lundmark, R. and Vallis, Y. and Martens, S. and 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. and Kent, H.M. and Ford, M.G.J. and Hegde, B.G. and Daumke, O. and Butler, P.J.G. and Mittal, R. and Langen, R. and 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. and Daumke, O. and Suveyzdis, Y. and Koetting, C. and Gerwert, K. and Wittinghofer, A.
Journal of Molecular Biology 367 (4): 983-95. 6 April 2007

GAP1 family members constitute bifunctional Ras and Rap GTPase-activating proteins.
Kupzig, S. and Deaconescu, D. and Bouyoucef, D. and Walker, S.A. and Liu, Q. and Polte, C.L. and Daumke, O. and Ishizaki, T. and Lockyer, P.J. and Wittinghofer, A. and Cullen, P.J.
Journal of Biological Chemistry 281 (15): 9891-900. 14 April 2006

Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold.
Rossbach, M. and Daumke, O. and Klinger, C. and Wittinghofer, A. and Kaufmann, M.
BMC Structural Biology 5 : 7. 20 March 2005

Synthesis of GTP-derived Ras ligands.
Soulère, L. and Aldrich, C. and Daumke, O. and Gail, R. and Kissau, L. and Wittinghofer, A. and Waldmann, H.
ChemBioChem 5 (10): 1448-53. 4 October 2004

The GTPase-activating protein Rap1GAP uses a catalytic asparagine.
Daumke, O. and Weyand, M. and Chakrabarti, P.P. and 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. and Wittinghofer, A. and Weyand, M.
Acta Crystallographica Section D : Structural Biology 60 (Pt 4): 752-4. April 2004

Rap-specific GTPase activating protein follows an alternative mechanism.
Brinkmann, T. and Daumke, O. and Herbrand, U. and Kühlmann, D. and Stege, P. and Ahmadian, M.R. and Wittinghofer, A.
Journal of Biological Chemistry 277 (15): 12525-31. 12 April 2002

Functional asymmetry of the ATP-binding-cassettes of the ABC transporter TAP is determined by intrinsic properties of the nucleotide binding domains.
Daumke, O. 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. and Daumke, O. and Deverson, E.V. and Howard, J.C. and Knittler, M.R.
Current Biology 11 (4): 242-51. 20 February 2001

Review

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition).
Klionsky, D.J. and Abdel-Aziz, A.K. and Abdelfatah, S. and Abdellatif, M. and Abdoli, A. and Abel, S. and Abeliovich, H. and Abildgaard, M.H. and Abudu, Y.P. and Acevedo-Arozena, A. and Adamopoulos, I.E. and Adeli, K. and Adolph, T.E. and Adornetto, A. and Aflaki, E. and Agam, G. and Agarwal, A. and Aggarwal, B.B. and Agnello, M. and Agostinis, P. and Agrewala, J.N. and Agrotis, A. and Aguilar, P.V. and Ahmad, S.T. and Ahmed, Z.M. and Ahumada-Castro, U. and Aits, S. and Aizawa, S. and Akkoc, Y. and Akoumianaki, T. and Akpinar, H.A. and Al-Abd, A.M. and Al-Akra, L. and Al-Gharaibeh, A. and Alaoui-Jamali, M.A. and Alberti, S. and Alcocer-Gómez, E. and Alessandri, C. and Ali, M. and Alim Al-Bari, M.A. and Aliwaini, S. and Alizadeh, J. and Almacellas, E. and Almasan, A. and Alonso, A. and Alonso, G.D. and Altan-Bonnet, N. and Altieri, D.C. and Álvarez, E.M.C. and Alves, S. and Alves da Costa, C. and Alzaharna, M.M. and Amadio, M. and Amantini, C. and Amaral, C. and Ambrosio, S. and Amer, A.O. and Ammanathan, V. and An, Z. and Andersen, S.U. and Andrabi, S.A. and Andrade-Silva, M. and Andres, A.M. and Angelini, S. and Ann, D. and Anozie, U.C. and Ansari, M.Y. and Antas, P. and Antebi, A. and Antón, Z. and Anwar, T. and Apetoh, L. and Apostolova, N. and Araki, T. and Araki, Y. and Arasaki, K. and Araújo, W.L. and Araya, J. and Arden, C. and Arévalo, M.A. and Arguelles, S. and Arias, E. and Arikkath, J. and Arimoto, H. and Ariosa, A.R. and Armstrong-James, D. and Arnauné-Pelloquin, L. and Aroca, A. and Arroyo, D.S. and Arsov, I. and Artero, R. and Asaro, D.M.L. and Aschner, M. and Ashrafizadeh, M. and Ashur-Fabian, O. and Atanasov, A.G. and Au, A.K. and Auberger, P. and Auner, H.W. and Aurelian, L. and Autelli, R. and Avagliano, L. and Ávalos, Y. and Aveic, S. and Aveleira, C.A. and Avin-Wittenberg, T. and Aydin, Y. and Ayton, S. and Ayyadevara, S. and Azzopardi, M. and Baba, M.u and Backer, J.M. and Backues, S.K. and Bae, D.H. and Bae, O.N. and Bae, S.H. and Baehrecke, E.H. and Baek, A. and Baek, S.H. and Baek, S.H. and Bagetta, G. and Bagniewska-Zadworna, A. and Bai, H. and Bai, J. and Bai, X. and Bai, Y. and Bairagi, N. and Baksi, S. and Balbi, T. and Baldari, C.T. and Balduini, W. and Ballabio, A. and Ballester, M. and Balazadeh, S. and Balzan, R. and Bandopadhyay, R. and Banerjee, S. and Banerjee, S. and Bánréti, A. and Bao, Y. and Baptista, M.S. and Baracca, A. and Barbati, C. and Bargiela, A. and Barilà, D. and Barlow, P.G. and Barmada, S.J. and Barreiro, E. and Barreto, G.E. and Bartek, J. and Bartel, B. and Bartolome, A. and Barve, G.R. and Basagoudanavar, S.H. and Bassham, D.C. and Bast, R.C. and Basu, A. and Batoko, H. and Batten, I. and Baulieu, E.E. and Baumgarner, B.L. and Bayry, J. and Beale, R. and Beau, I. and Beaumatin, F. and Bechara, L.R.G. and Beck, G.R. and Beers, M.F. and Begun, J. and Behrends, C. and Behrens, G.M.N. and Bei, R. and Bejarano, E. and Bel, S. and Behl, C. and Belaid, A. and Belgareh-Touzé, N. and Bellarosa, C. and Belleudi, F. and Belló Pérez, M. and Bello-Morales, R. and Beltran, J.S.O. and Beltran, S. and Benbrook, D.M. and Bendorius, M. and Benitez, B.A. and Benito-Cuesta, I. and Bensalem, J. and Berchtold, M.W. and Berezowska, S. and Bergamaschi, D. and Bergami, M. and Bergmann, A. and Berliocchi, L. and Berlioz-Torrent, C. and Bernard, A. and Berthoux, L. and Besirli, C.G. and Besteiro, S. and Betin, V.M. and Beyaert, R. and Bezbradica, J.S. and Bhaskar, K. and Bhatia-Kissova, I. and Bhattacharya, R. and Bhattacharya, S. and Bhattacharyya, S. and Bhuiyan, M.S. and Bhutia, S.K. and Bi, L. and Bi, X. and Biden, T.J. and Bijian, K. and Billes, V.A. and Binart, N. and Bincoletto, C. and Birgisdottir, A.B. and Bjorkoy, G. and Blanco, G. and Blas-Garcia, A. and Blasiak, J. and Blomgran, R. and Blomgren, K. and Blum, J.S. and Boada-Romero, E. and Boban, M. and Boesze-Battaglia, K. and Boeuf, P. and Boland, B. and Bomont, P. and Bonaldo, P. and Bonam, S.R. and Bonfili, L. and Bonifacino, J.S. and Boone, B.A. and Bootman, M.D. and Bordi, M. and Borner, C. and Bornhauser, B.C. and Borthakur, G. and Bosch, J. and Bose, S. and Botana, L.M. and Botas, J. and Boulanger, C.M. and Boulton, M.E. and Bourdenx, M. and Bourgeois, B. and Bourke, N.M. and Bousquet, G. and Boya, P. and Bozhkov, P.V. and Bozi, L.H.M. and Bozkurt, T.O. and Brackney, D.E. and Brandts, C.H. and Braun, R.J. and Braus, G.H. and Bravo-Sagua, R. and Bravo-San Pedro, J.M. and Brest, P. and Bringer, M.A. and Briones-Herrera, A. and Broaddus, V.C. and Brodersen, P. and Brodsky, J.L. and Brody, S.L. and Bronson, P.G. and Bronstein, J.M. and Brown, C.N. and Brown, R.E. and Brum, P.C. and Brumell, J.H. and Brunetti-Pierri, N. and Bruno, D. and Bryson-Richardson, R.J. and Bucci, C. and Buchrieser, C. and Bueno, M. and Buitrago-Molina, L.E. and Buraschi, S. and Buch, S. and Buchan, J.R. and Buckingham, E.M. and Budak, H. and Budini, M. and Bultynck, G. and Burada, F. and Burgoyne, J.R. and Burón, M.I. and Bustos, V. and Büttner, S. and Butturini, E. and Byrd, A. and Cabas, I. and Cabrera-Benitez, S. and Cadwell, K. and Cai, J. and Cai, L. and Cai, Q. and Cairó, M. and Calbet, J.A. and Caldwell, G.A. and Caldwell, K.A. and Call, J.A. and Calvani, R. and Calvo, A.C. and Calvo-Rubio Barrera, M. and Camara, N.O. and Camonis, J.H. and Camougrand, N. and Campanella, M. and Campbell, E.M. and Campbell-Valois, F.X. and Campello, S. and Campesi, I. and Campos, J.C. and Camuzard, O. and Cancino, J. and Candido de Almeida, D. and Canesi, L. and Caniggia, I. and Canonico, B. and Cantí, C. and Cao, B. and Caraglia, M. and Caramés, B. and Carchman, E.H. and Cardenal-Muñoz, E. and Cardenas, C. and Cardenas, L. and Cardoso, S.M. and Carew, J.S. and Carle, G.F. and Carleton, G. and Carloni, S. and Carmona-Gutierrez, D. and Carneiro, L.A. and Carnevali, O. and Carosi, J.M. and Carra, S. and Carrier, A. and Carrier, L. and Carroll, B. and Carter, A.B. and Carvalho, A.N. and Casanova, M. and Casas, C. and Casas, J. and Cassioli, C. and Castillo, E.F. and Castillo, K. and Castillo-Lluva, S. and Castoldi, F. and Castori, M. and Castro, A.F. and Castro-Caldas, M. and Castro-Hernandez, J. and Castro-Obregon, S. and Catz, S.D. and Cavadas, C. and Cavaliere, F. and Cavallini, G. and Cavinato, M. and Cayuela, M.L. and Cebollada Rica, P. and Cecarini, V. and Cecconi, F. and Cechowska-Pasko, M. and Cenci, S. and Ceperuelo-Mallafré, V. and Cerqueira, J.J. and Cerutti, J.M. and Cervia, D. and Cetintas, V.B. and Cetrullo, S. and Chae, H.J. and Chagin, A.S. and Chai, C.Y. and Chakrabarti, G. and Chakrabarti, O. and Chakraborty, T. and Chakraborty, T. and Chami, M. and Chamilos, G. and Chan, D.W. and Chan, E.Y.W. and Chan, E.D. and Chan, H.Y.E. and Chan, H.H. and Chan, H. and Chan, M.T.V. and Chan, Y.S. and Chandra, P.K. and Chang, C.P. and Chang, C. and Chang, H.C. and Chang, K. and Chao, J. and Chapman, T. and Charlet-Berguerand, N. and Chatterjee, S. and Chaube, S.K. and Chaudhary, A. and Chauhan, S. and Chaum, E. and Checler, F. and Cheetham, M.E. and Chen, C.S. and Chen, G.C. and Chen, J.F. and Chen, L.L. and Chen, L. and Chen, L. and Chen, M. and Chen, M.K. and Chen, N. and Chen, Q. and Chen, R.H. and Chen, S. and Chen, W. and Chen, W. and Chen, X.M. and Chen, X.W. and Chen, X. and Chen, Y. and Chen, Y.G. and Chen, Y. and Chen, Y. and Chen, Y.J. and Chen, Y.Q. and Chen, Z.S. and Chen, Z. and Chen, Z.H. and Chen, Z.J. and Chen, Z. and Cheng, H. and Cheng, J. and Cheng, S.Y. and Cheng, W. and Cheng, X. and Cheng, X.T. and Cheng, Y. and Cheng, Z. and Chen, Z. and Cheong, H. and Cheong, J.K. and Chernyak, B.V. and Cherry, S. and Cheung, C.F.R. and Cheung, C.H.A. and Cheung, K.H. and Chevet, E. and Chi, R.J. and Chiang, A.K.S. and Chiaradonna, F. and Chiarelli, R. and Chiariello, M. and Chica, N. and Chiocca, S. and Chiong, M. and Chiou, S.H. and Chiramel, A.I. and Chiurchiù, V. and Cho, D.H. and Choe, S.K. and Choi, A.M.K. and Choi, M.E. and Choudhury, K.R. and Chow, N.S. and Chu, C.T. and 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A.V. and Czaja, M.J. and Czuczwar, S.J. and D'Adamo, S. and D'Amelio, M. and D'Arcangelo, D. and D'Lugos, A.C. and D'Orazi, G. and da Silva, J.A. and Dafsari, H.S. and Dagda, R.K. and Dagdas, Y. and Daglia, M. and Dai, X. and Dai, Y. and Dai, Y. and Dal Col, J. and Dalhaimer, P. and Dalla Valle, L. and Dallenga, T. and Dalmasso, G. and Damme, M. and Dando, I. and Dantuma, N.P. and Darling, A.L. and Das, H. and Dasarathy, S. and Dasari, S.K. and Dash, S. and Daumke, O. and Dauphinee, A.N. and Davies, J.S. and Dávila, V.A. and Davis, R.J. and Davis, T. and Dayalan Naidu, S. and De Amicis, F. and De Bosscher, K. and De Felice, F. and De Franceschi, L. and De Leonibus, C. and de Mattos Barbosa, M.G. and De Meyer, G.R.Y. and De Milito, A. and De Nunzio, C. and De Palma, C. and De Santi, M. and De Virgilio, C. and De Zio, D. and Debnath, J. and DeBosch, B.J. and Decuypere, J.P. and Deehan, M.A. and Deflorian, G. and DeGregori, J. and Dehay, B. and Del Rio, G. and Delaney, J.R. and Delbridge, 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Autophagy 17 (1): 1-382. 8 February 2021

Pathophysiological role of caveolae in hypertension.
Lian, X. and Matthaeus, C. and Kaßmann, M. and Daumke, O. and Gollasch, M.
Frontiers in Medicine 6 : 153. July 2019

Struktur und Funktion des mechanochemischen Motorproteins Dynamin.
Faelber, K. and Daumke, O.
BIOspektrum 24 (5): 481-483. September 2018

Membrane fission by dynamin: what we know and what we need to know.
Antonny, B. and Burd, C. and De Camilli, P. and Chen, E. and Daumke, O. and Faelber, K. and Ford, M. and Frolov, V.A. and Frost, A. and Hinshaw, J.E. and Kirchhausen, T. and Kozlov, M.M. and Lenz, M. and Low, H.H. and McMahon, H. and Merrifield, C. and Pollard, T.D. and Robinson, P.J. and Roux, A. and Schmid, S.
EMBO Journal 35 (21): 2270-2284. 2 November 2016

Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
Daumke, O. and Praefcke, G.J.
Biopolymers 105 (8): 580-593. August 2016

Sequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamics.
Noel, J.K. and Morcos, F. and Onuchic, J.N.
F1000 Research 5 (F1000 Faculty Rev): 106. 26 January 2016

BAR domain scaffolds in dynamin-mediated membrane fission.
Daumke, O. and Roux, A. and Haucke, V.
Cell 156 (5): 882-892. 27 February 2014

Oligomerization of dynamin superfamily proteins in health and disease.
Faelber, K. and Gao, S. and Held, M. and Posor, Y. and Haucke, V. and Noé, F. and Daumke, O.
Progress in Molecular Biology and Translational Science 117 : 411-443. 2013

Structural insights into dynamin-mediated membrane fission.
Faelber, K. and Held, M. and Gao, S. and Posor, Y. and Haucke, V. and Noe, F. and Daumke, O.
Structure 20 (10): 1621-1628. 10 October 2012

Stomatin-domain proteins.
Lapatsina, L. and Brand, J. and Poole, K. and Daumke, O. and Lewin, G.R.
European Journal of Cell Biology 91 (4): 240-245. April 2012

Dynamin-like MxA GTPase: Structural insights into oligomerization and implications for antiviral activity.
Haller, O. and Gao, S. and von der Malsburg, A. and Daumke, O. and Kochs, G.
Journal of Biological Chemistry 285 (37): 28419-28424. 10 September 2010

Editorial

SPFH protein cage - one ring to rule them all.
Daumke, O. and Lewin, G.R.
Cell Research 32 (2): 117-118. February 2022

How RB1CC1/FIP200 claws its way to autophagic engulfment of SQSTM1/p62-ubiquitin condensates.
Turco, E. and Witt, M. and Abert, C. and Bock-Bierbaum, T. and Su, M.Y. and Trapannone, R. and Sztacho, M. and Danieli, A. and Shi, X. and Zaffagnini, G. and Gamper, A. and Schuschnig, M. and Fracchiolla, D. and Bernklau, D. and Romanov, J. and Hartl, M. and Hurley, J.H. and Daumke, O. and Martens, S.
Autophagy 15 (8): 1475-1477. August 2019

Mitochondrial homeostasis: How do dimers of mitofusins mediate mitochondrial fusion?
Daumke, O. and Roux, A.
Current Biology 27 (9): R353-R356. 8 May 2017

Protein-mediated membrane remodeling.
Daumke, O. and Unger, V.M.
Journal of Structural Biology 196 (1): 1-2. October 2016

Structural insights into membrane fusion at the endoplasmic reticulum.
Daumke, O. and Praefcke, G.J.
Proceedings of the National Academy of Sciences of the United States of America 108 (6): 2175-2176. 8 February 2011

Preprint

Disrupting the CD177:proteinase 3 membrane complex reduces anti-PR3 antibody-induced neutrophil activation.
Marino, S.F. and Jerke, U. and Rolle, S. and Daumke, O. and Kettritz, R.
bioRxiv : 2021.05.17.444335. 17 May 2021

Mechanistic basis for motor-driven membrane constriction by dynamin.
Ganichkin, O. and Vancraenenbroeck, R. and Rosenblum, G. and Hofmann, H. and Mikhailov, A.S. and Daumke, O. and Noel, J.K.
bioRxiv : 2020.09.10.289546. 11 September 2020

Polymer-like model to study the dynamics of dynamin filaments on deformable membrane tubes.
Noel, J.K. and Noé, F. and Daumke, O. and Mikhailov, A.S.
bioRxiv : 686873. 28 June 2019

EHD2-mediated restriction of caveolar dynamics regulates cellular lipid uptake.
Matthäus, C. and Lahmann, I. and Kunz, S. and Jonas, W. and Alves Melo, A. and Lehmann, M. and Larsson, E. and Lundmark, R. and Kern, M. and Blüher, M. and Müller, D.N. and Haucke, V. and Schürmann, A. and Birchmeier, C. and Daumke, O.
bioRxiv : 511709. 7 March 2019