Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

Ursula Jakob; Johannes Buchner

doi:10.1016/0968-0004(94)90023-X

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

Ursula Jakob
, Johannes Buchner

University of Regensburg

Research output: Contribution to journal › Review article › peer-review

356 Scopus citations

Abstract

Hsp90 and small Hsps are two abundant types of eukaryotic stress protein whose function has remained largely enigmatic. In the cell, Hsp90 exists in a complex (with other Hsps and prolyl isomerases) possibly implicated in interactions with non-native proteins. Recent biochemical analysis of both Hsp90 and small Hsps has revealed that they may act as ATP-independent molecular chaperones involved in protein folding and unfolding events.

Original language	English
Pages (from-to)	205-211
Number of pages	7
Journal	Trends in Biochemical Sciences
Volume	19
Issue number	5
DOIs	https://doi.org/10.1016/0968-0004(94)90023-X
State	Published - May 1994
Externally published	Yes

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title = "Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones",

abstract = "Hsp90 and small Hsps are two abundant types of eukaryotic stress protein whose function has remained largely enigmatic. In the cell, Hsp90 exists in a complex (with other Hsps and prolyl isomerases) possibly implicated in interactions with non-native proteins. Recent biochemical analysis of both Hsp90 and small Hsps has revealed that they may act as ATP-independent molecular chaperones involved in protein folding and unfolding events.",

author = "Ursula Jakob and Johannes Buchner",

year = "1994",

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AU - Buchner, Johannes

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N2 - Hsp90 and small Hsps are two abundant types of eukaryotic stress protein whose function has remained largely enigmatic. In the cell, Hsp90 exists in a complex (with other Hsps and prolyl isomerases) possibly implicated in interactions with non-native proteins. Recent biochemical analysis of both Hsp90 and small Hsps has revealed that they may act as ATP-independent molecular chaperones involved in protein folding and unfolding events.

AB - Hsp90 and small Hsps are two abundant types of eukaryotic stress protein whose function has remained largely enigmatic. In the cell, Hsp90 exists in a complex (with other Hsps and prolyl isomerases) possibly implicated in interactions with non-native proteins. Recent biochemical analysis of both Hsp90 and small Hsps has revealed that they may act as ATP-independent molecular chaperones involved in protein folding and unfolding events.

UR - https://www.scopus.com/pages/publications/0028284571

U2 - 10.1016/0968-0004(94)90023-X

DO - 10.1016/0968-0004(94)90023-X

M3 - Review article

C2 - 7914036

AN - SCOPUS:0028284571

SN - 0968-0004

VL - 19

SP - 205

EP - 211

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 5

ER -

Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones

Abstract

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