(Q74251218)

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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

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9 November 2019

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1 May 2002

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9 November 2019

Journal of Molecular Biology

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9 November 2019

319

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9 November 2019

2

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9 November 2019

517-526

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9 November 2019

Alpha-crystallin can function as a molecular chaperone

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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

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Subunit exchange of alphaA-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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7 January 2021

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 alpha-crystallin

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7 January 2021

Antigenic diversity of Mycobacterium tuberculosis and Mycobacterium bovis detected by means of monoclonal antibodies

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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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7 January 2021

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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7 January 2021

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 the number and relative molecular mass of subunits in an oligomeric protein by two-dimensional electrophoresis. Application to the subunit structure analysis of rat liver amidophosphoribosyltransferase

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7 January 2021

Site-directed spin labeling study of subunit interactions in the alpha-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in alphaA-crystallin, HSP 27, and HSP 16.3.

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Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins

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Examination of the secondary structure of proteins by deconvolved FTIR spectra

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

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On the thermal stability of alpha-crystallin: a new insight from infrared spectroscopy

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7 January 2021

Effect of heat-induced structural perturbation of secondary and tertiary structures on the chaperone activity of alpha-crystallin

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7 January 2021

Small heat shock protein of Methanococcus jannaschii, a hyperthermophile

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N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers

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Mycobacterial stationary phase induced by low oxygen tension: cell wall thickening and localization of the 16-kilodalton alpha-crystallin homolog.

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New insight into protein secondary structure from resolution-enhanced infrared spectra

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Identifiers

10.1016/S0022-2836(02)00311-X

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

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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