Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

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

Date

Authors

Williams, Danielle M.

Ecroyd, Heath

Goodwin, Katy

Dai, Huanqin

Fu, Haian

Woodcock, Joanna M.

Zhang, Lixin

Carver, John

Publisher

Portland Press

Abstract

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

Keywords

Keywords: chaperone; phosphoserine; small heat shock protein; stratifin; amino acid sequence; article; binding affinity; carboxy terminal sequence; controlled study; genetic conservation; ligand binding; nonhuman; nuclear magnetic resonance spectroscopy; priority j 14-3-3 protein; Biophysical characterization; C-terminal flexibility; Molecular chaperone; Protein aggregation; Protein-protein interaction

URI

http://hdl.handle.net/1885/63355

Collections

ANU Research Publications

Source

Biochemical Journal

Type

Journal article

DOI

10.1042/BJ20102178

Restricted until

2037-12-31

Downloads

File

Description

01_Williams_NMR_spectroscopy_of_14-3-3ζ_2011.pdf (814.86 KB)