A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity (Q33940479)

30 July 2017

title

A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity (English)

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30 July 2017

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Feil IK

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30 July 2017

Malfois M

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30 July 2017

Hendle J

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30 July 2017

van Der Zandt H

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30 July 2017

Svergun DI

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30 July 2017

language of work or name

English

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publication date

12 January 2001

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Journal of Biological Chemistry

30 July 2017

published in

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30 July 2017

volume

276

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30 July 2017

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30 July 2017

page(s)

12024-12029

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Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of alpha-crystallin solutions

30 July 2017

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The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure

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Alpha-crystallin can function as a molecular chaperone

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Structures of Calmodulin and a Functional Myosin Light Chain Kinase in the Activated Complex: A Neutron Scattering Study†

21 January 2018

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The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbumin

21 January 2018

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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.

21 January 2018

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21 January 2018

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

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Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function

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21 January 2018

Identifiers

DOI

10.1074/JBC.M010856200

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30 July 2017

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