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| Item Type: | Article |
|---|---|
| Title: | The amino-terminus of nitric oxide sensitive guanylyl cyclase alpha(1) does not affect dimerization but influences subcellular localization |
| Creators Name: | Kraehling, J.R., Busker, M., Haase, T., Haase, N., Koglin, M., Linnenbaum, M. and Behrends, S. |
| Abstract: | Nitric oxide sensitive guanylyl cyclase (NOsGC) is a heterodimeric enzyme formed by an alpha- and a beta(1)-subunit. A splice variant (C-alpha(1)) of the alpha(1)-subunit, lacking at least the first 236 amino acids has been described by Sharina et al. 2008 and has been shown to be expressed in differentiating human embryonic cells. Wagner et al. 2005 have shown that the amino acids 61-128 of the alpha(1)-subunit are mandatory for quantitative heterodimerization implying that the C-alpha(1)-splice variant should lose its capacity to dimerize quantitatively. |
| Keywords: | Cell Line, Fluorescence Resonance Energy Transfer, Guanylate Cyclase, Protein Multimerization, Protein Subunits |
| Source: | PLoS ONE |
| ISSN: | 1932-6203 |
| Publisher: | Public Library of Science |
| Volume: | 6 |
| Number: | 9 |
| Page Range: | e25772 |
| Date: | 30 September 2011 |
| Official Publication: | https://doi.org/10.1371/journal.pone.0025772 |
| PubMed: | View item in PubMed |
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