Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity-Reference-Cited by-同舟云学术

Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity

Published:2018-01 Issue:1 Volume:293 Page:89-99
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Woodcock Joanna M.^ORCID,Goodwin Katy L.,Sandow Jarrod J.,Coolen Carl,Perugini Matthew A.^ORCID,Webb Andrew I.,Pitson Stuart M.^ORCID,Lopez Angel F.^ORCID,Carver John A.^ORCID

Funder

National Health and Medical Research Council

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference32 articles.

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3. The alternative role of 14-3-3 zeta as a sweeper of misfolded proteins in disease conditions;Kaneko;Med. Hypotheses,2006

4. 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;Biochem. J,2011

5. Structural determinants of 14-3-3 binding specificites and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms;Gardino;Semin. Cancer Biol,2006

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