Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation

E. P.M. Candido; S. Gräber; M. Gaestel; J. Buchner

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation

E. P.M. Candido, S. Gräber, M. Gaestel, J. Buchner

Lehrstuhl für Biotechnologie

Publikation: Beitrag in Fachzeitschrift › Übersichtsartikel › Begutachtung

1 Zitat (Scopus)

Abstract

This paper supports the hypothesis that the function of the small HSPs is to bind unfolded proteins in a relatively stable state which allows their subsequent transfer to other molecular chaperones for refolding.

Originalsprache	Englisch
Seiten (von - bis)	166-172
Seitenumfang	7
Fachzeitschrift	Chemtracts
Jahrgang	11
Ausgabenummer	3
Publikationsstatus	Veröffentlicht - März 1998

Andere Dateien und Links

Verknüpfung zur Publikation in Scopus

Dieses zitieren

@article{a1a6c95a576544de9fcb76906ba4a400,

title = "Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation",

abstract = "This paper supports the hypothesis that the function of the small HSPs is to bind unfolded proteins in a relatively stable state which allows their subsequent transfer to other molecular chaperones for refolding.",

author = "Candido, {E. P.M.} and S. Gr{\"a}ber and M. Gaestel and J. Buchner",

year = "1998",

month = mar,

language = "English",

volume = "11",

pages = "166--172",

journal = "Chemtracts",

issn = "1431-9268",

publisher = "Data Trace Publishing Co.",

number = "3",

}

TY - JOUR

T1 - Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation

AU - Candido, E. P.M.

AU - Gräber, S.

AU - Gaestel, M.

AU - Buchner, J.

PY - 1998/3

Y1 - 1998/3

N2 - This paper supports the hypothesis that the function of the small HSPs is to bind unfolded proteins in a relatively stable state which allows their subsequent transfer to other molecular chaperones for refolding.

AB - This paper supports the hypothesis that the function of the small HSPs is to bind unfolded proteins in a relatively stable state which allows their subsequent transfer to other molecular chaperones for refolding.

UR - http://www.scopus.com/inward/record.url?scp=0031769877&partnerID=8YFLogxK

M3 - Review article

AN - SCOPUS:0031769877

SN - 1431-9268

VL - 11

SP - 166

EP - 172

JO - Chemtracts

JF - Chemtracts

IS - 3

ER -

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation

Abstract

Andere Dateien und Links

Fingerprint

Dieses zitieren