(Q45005891)

8 December 2017

Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function (English)

1 reference

8 December 2017

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Ashis Biswas

1

1 reference

PubMed ID

15292216

8 December 2017

Kali P Das

series ordinal

2

1 reference

PubMed ID

15292216

8 December 2017

language of work or name

English

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publication date

30 July 2004

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Journal of Biological Chemistry

8 December 2017

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8 December 2017

279

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8 December 2017

41

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8 December 2017

42648-42657

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

8 December 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Expression of the murine alpha B-crystallin gene is not restricted to the lens

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Alpha-crystallin can function as a molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

On the substrate specificity of alpha-crystallin as a molecular chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Crystal structure and assembly of a eukaryotic small heat shock protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

ATP causes small heat shock proteins to release denatured protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Molecular chaperones in cellular protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Alpha-crystallin/small heat shock protein has autokinase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Conversion from oligomers to tetramers enhances autophosphorylation by lens alpha A-crystallin. Specificity between alpha A- and alpha B-crystallin subunits.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Lens alpha-crystallin: chaperone-like properties

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Spectrofluorimetric assessment of the surface hydrophobicity of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Protein folding intermediates: native-state hydrogen exchange

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Future directions in folding: the multi-state nature of protein structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

A chaperonin from a thermophilic bacterium, Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

Chaperone-like activity of tubulin. binding and reactivation of unfolded substrate enzymes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M404444200

21 January 2018

Identifiers

DOI

10.1074/JBC.M404444200

1 reference

8 December 2017

1 reference

PubMed ID

15292216