NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ

Williams, Danielle M.; Ecroyd, Heath; Goodwin, Katy; Dai, Huanqin; Fu, Haian; Woodcock, Joanna M.; Zhang, Lixin; Carver, John

doi:10.1042/BJ20102178

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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
Date published:	2011
Type:	Journal article
URI:	http://hdl.handle.net/1885/63355
Source:	Biochemical Journal
DOI:	10.1042/BJ20102178

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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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