Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites. - Wikidata - awgldk - TriplyDB

Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites.

Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites.

http://www.wikidata.org/entity/Q31897258

about

Phe71 is essential for chaperone-like function in alpha A-crystallin Tryptophan and Non-Tryptophan Fluorescence of the Eye Lens Proteins Provides Diagnostics of Cataract at the Molecular Level Differential response of C57BL/6J mouse and DBA/2J mouse to optic nerve crush Cataract-causing αAG98R-crystallin mutant dissociates into monomers having chaperone activity.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Reversal of amyloid-induced heart disease in desmin-related cardiomyopathy.Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallin Novel roles for α-crystallins in retinal function and disease.Electrostatic origin of in vitro aggregation of human γ-crystallin.Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins.The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human alphaB-crystallin.Insights into the domains required for dimerization and assembly of human alphaB crystallin.Age-dependent racemization of serine residues in a human chaperone protein A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins.Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins.Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function.Heterologous expression and topography of the main intrinsic protein (MIP) from rat lens.pH-Dependent channel activity of heterologously-expressed main intrinsic protein (MIP) from rat lens.Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity.An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins.

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P2860

Chaperone function of mutant versions of alpha A- and alpha B-crystallin prepared to pinpoint chaperone binding sites.

http://www.wikidata.org/entity/Q31897258

description

2001 nî lūn-bûn

@nan

2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Chaperone function of mutant v ...... point chaperone binding sites.

@ast

Chaperone function of mutant v ...... point chaperone binding sites.

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type

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Chaperone function of mutant v ...... point chaperone binding sites.

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Chaperone function of mutant v ...... point chaperone binding sites.

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Chaperone function of mutant v ...... point chaperone binding sites.

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Chaperone function of mutant v ...... point chaperone binding sites.

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P356

J.1432-1327.2001.01929.X

P1433

P1476

Chaperone function of mutant v ...... point chaperone binding sites.

@en

P2093

B K Derham

http://www.w3.org/2001/XMLSchema#string

H W Hepburne-Scott

http://www.w3.org/2001/XMLSchema#string

J Horwitz

http://www.w3.org/2001/XMLSchema#string

J I Clark

http://www.w3.org/2001/XMLSchema#string

J J Harding

http://www.w3.org/2001/XMLSchema#string

M A van Boekel

http://www.w3.org/2001/XMLSchema#string

M J Crabbe

http://www.w3.org/2001/XMLSchema#string

P J Muchowski

http://www.w3.org/2001/XMLSchema#string

W W de Jong

http://www.w3.org/2001/XMLSchema#string

P2860

Cloning, expression, and chaperone-like activity of human alphaA-crystallin

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Alpha-crystallin can function as a molecular chaperone

The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.

Monoclonal antibodies reveal evolutionary conservation of alternative splicing of the alpha A-crystallin primary transcript.

Alpha-crystallin as a molecular chaperone.

Identification of the posttranslational modifications of bovine lens alpha B-crystallins by mass spectrometry.

Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin.

Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha B-crystallin.

Mutation R120G in alphaB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function

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713-721

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scholarly article

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10.1046/J.1432-1327.2001.01929.X

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3

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2001-02-01T00:00:00Z

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P921

molecular chaperones