NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ
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Williams, Danielle M.; Ecroyd, Heath; Goodwin, Katy; Dai, Huanqin; Fu, Haian; Woodcock, Joanna M.; Zhang, Lixin; Carver, John
Description
Intracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell signalling and disease progression. The 14-3-3ζ isoform is a molecular chaperone, preventing the stressinduced aggre
Collections | ANU Research Publications |
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Date published: | 2011 |
Type: | Journal article |
URI: | http://hdl.handle.net/1885/63355 |
Source: | Biochemical Journal |
DOI: | 10.1042/BJ20102178 |
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01_Williams_NMR_spectroscopy_of_14-3-3ζ_2011.pdf | 814.86 kB | Adobe PDF | Request a copy |
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