Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding (Q43572431)

24 November 2017

title

Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding (English)

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24 November 2017

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M Minami

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24 November 2017

M Nakamura

series ordinal

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24 November 2017

Y Emori

series ordinal

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24 November 2017

Y Minami

series ordinal

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24 November 2017

language of work or name

English

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publication date

1 April 2001

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24 November 2017

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24 November 2017

volume

268

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24 November 2017

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24 November 2017

page(s)

2520-2524

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Molecular chaperones in cellular protein folding

24 November 2017

cites work

1 reference

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Protein folding in vivo: the importance of molecular chaperones

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Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

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In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

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In vivo newly translated polypeptides are sequestered in a protected folding environment

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Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

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Protein folding and the regulation of signaling pathways

21 January 2018

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Hsp90 & Co. - a holding for folding

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Structure and in vivo function of Hsp90.

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In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

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Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

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Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

21 January 2018

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Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.

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Hsp90 as a capacitor for morphological evolution

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Hsc70/Hsp40 chaperone system mediates the Hsp90-dependent refolding of firefly luciferase.

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A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

21 January 2018

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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

21 January 2018

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

21 January 2018

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Hsp90 chaperones protein folding in vitro.

21 January 2018

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Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

21 January 2018

1 reference

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The base of the proteasome regulatory particle exhibits chaperone-like activity

21 January 2018

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Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

21 January 2018

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Recent Advances in the Study of hsp90 Structure and Mechanism of Action

21 January 2018

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Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor-hsp90 Heterocomplex Assembly

21 January 2018

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A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding

21 January 2018

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Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies

21 January 2018

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The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes

21 January 2018

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Interaction between casein kinase II and the 90-kDa stress protein, HSP90

21 January 2018

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In vitro evidence that hsp90 contains two independent chaperone sites

21 January 2018

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Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome

21 January 2018

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10.1046/J.1432-1327.2001.02145.X

21 January 2018

Identifiers

DOI

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24 November 2017

1 reference