(Q44610052)

English

Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity

scientific article published on 7 October 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

4 December 2017

Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity (English)

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

molecular chaperones

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author name string

Saloni Yatin Pasta

1

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

Bakthisaran Raman

2

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

Tangirala Ramakrishna

3

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

Ch Mohan Rao

4

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

language of work or name

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publication date

7 October 2003

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Europe PubMed Central

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4 December 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

4 December 2017

278

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Europe PubMed Central

PubMed publication ID

4 December 2017

51

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

51159-51166

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

Complete structure of the alpha B-crystallin gene: conservation of the exon-intron distribution in the two nonlinked alpha-crystallin genes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

alphaB-crystallin exists as an independent protein in the heart and in the lens

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Immunoreactive alpha A crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Alpha B-crystallin is a small heat shock protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Alpha-crystallin can function as a molecular chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Hypertonic stress induces alpha B-crystallin expression

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Small Heat Shock Proteins and Protection Against Ischemic Injury in Cardiac Myocytes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Small heat-shock proteins and their potential role in human disease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Genealogy of the alpha-crystallin--small heat-shock protein superfamily

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Expression and aggregation of recombinant alpha A-crystallin and its two domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

How to measure and predict the molar absorption coefficient of a protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Crystal structure and assembly of a eukaryotic small heat shock protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Circular dichroism and optical rotatory dispersion of the aggregates of purified polypeptides of alpha-crystallin.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

4,4'-Bis[8-(phenylamino)naphthalene-1-sulfonate] binding to human thrombins: a sensitive exo site fluorescent affinity probe

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

A dynamic quaternary structure of bovine alpha-crystallin as indicated from intermolecular exchange of subunits.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Subunit Exchange of αA-Crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Intermolecular Exchange and Stabilization of Recombinant Human αA- and αB-Crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Subunit exchange of lens alpha-crystallin: a fluorescence energy transfer study with the fluorescent labeled alphaA-crystallin mutant W9F as a probe

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Phosphorylation-induced change of the oligomerization state of alpha B-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Thermal activation of the bovine Hsc70 molecular chaperone at physiological temperatures: physical evidence of a molecular thermometer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Heat-induced chaperone activity of HSP90.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Exploiting the past and the future in protein secondary structure prediction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

An algorithm for secondary structure determination in proteins based on sequence similarity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Improvements in protein secondary structure prediction by an enhanced neural network

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

The PSIPRED protein structure prediction server

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

GOR method for predicting protein secondary structure from amino acid sequence.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Empirical Predictions of Protein Conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Differential Temperature-dependent Chaperone-like Activity of αA- and αB-crystallin Homoaggregates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Temperature dependent chaperone-like activity of alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Identification of possible regions of chaperone activity in lens alpha-crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Molecular Chaperones Protect Catalase Against Thermal Stress

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Complete protection by alpha-crystallin of lens sorbitol dehydrogenase undergoing thermal stress

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Structure and Function of the Conserved Domain in αA-Crystallin. Site-Directed Spin Labeling Identifies a β-Strand Located near a Subunit Interface

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Spectroscopic investigations of bovine lens crystallins. 1. Circular dichroism and intrinsic fluorescence

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Amino acid sequence homology applied to the prediction of protein secondary structures, and joint prediction with existing methods

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Evolutionary similarity among peptide segments is a basis for prediction of protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M307523200

21 January 2018

Identifiers

10.1074/JBC.M307523200

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

4 December 2017

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