Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity (Q74251218)

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scientific article published on 01 May 2002

Language	Label	Description	Also known as
English	Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity	scientific article published on 01 May 2002

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9 November 2019

Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity (English)

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9 November 2019

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Liangcai Gu

1

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9 November 2019

Abuduaini Abulimiti

2

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9 November 2019

Wen Li

3

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9 November 2019

Zengyi Chang

4

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9 November 2019

publication date

1 May 2002

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9 November 2019

Journal of Molecular Biology

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9 November 2019

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9 November 2019

2

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9 November 2019

517-526

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9 November 2019

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Subunit Exchange of αA-Crystallin

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Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies

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Crystal structure of a small heat-shock protein

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Hsp26: a temperature-regulated chaperone

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Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein

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Self-similarity properties of alpha-crystallin supramolecular aggregates.

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Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation

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The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species

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Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations

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Crystal structure and assembly of a eukaryotic small heat shock protein

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Structure-Function Studies on Small Heat Shock Protein Oligomeric Assembly and Interaction with Unfolded Polypeptides

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Chaperone-like Activity and Temperature-induced Structural Changes of α-Crystallin

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The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity

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Preheat treatment for Mycobacterium tuberculosis Hsp16.3: correlation between a structural phase change at 60 degrees C and a dramatic increase in chaperone-like activity

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Probing the roles of the only universally conserved leucine residue (Leu122) in the oligomerization and chaperone-like activity of Mycobacterium tuberculosis small heat shock protein Hsp16.3.

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Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment

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7 January 2021

Effect of Heat-Induced Structural Perturbation of Secondary and Tertiary Structures on the Chaperone Activity of α-Crystallin

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Identifiers

10.1016/S0022-2836(02)00311-X

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12051925%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12051925%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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