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The amino-terminus of nitric oxide sensitive guanylyl cyclase alpha(1) does not affect dimerization but influences subcellular localization

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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. and Busker, M. and Haase, T. and Haase, N. and Koglin, M. and 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 (U.S.A.)
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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