hsp90: Twist and Fold

Klaus Richter; Johannes Buchner

doi:10.1016/j.cell.2006.10.004

hsp90: Twist and Fold

Klaus Richter, Johannes Buchner

Publikation: Beitrag in Fachzeitschrift › Kurzer Abriss › Begutachtung

48 Zitate (Scopus)

Abstract

Molecular chaperones are cellular machines that facilitate protein folding. The crystal structures of HtpG, the Escherichia coli homolog of hsp90, reported in this issue (Shiau et al., 2006) together with the recently published structures of an hsp90-cochaperone complex (Ali et al., 2006) and an hsp90-client protein complex (Vaughan et al., 2006), reveal exciting insights into the hsp90 reaction cycle.

Originalsprache	Englisch
Seiten (von - bis)	251-253
Seitenumfang	3
Fachzeitschrift	Cell
Jahrgang	127
Ausgabenummer	2
DOIs	https://doi.org/10.1016/j.cell.2006.10.004
Publikationsstatus	Veröffentlicht - 20 Okt. 2006

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10.1016/j.cell.2006.10.004

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abstract = "Molecular chaperones are cellular machines that facilitate protein folding. The crystal structures of HtpG, the Escherichia coli homolog of hsp90, reported in this issue (Shiau et al., 2006) together with the recently published structures of an hsp90-cochaperone complex (Ali et al., 2006) and an hsp90-client protein complex (Vaughan et al., 2006), reveal exciting insights into the hsp90 reaction cycle.",

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AU - Buchner, Johannes

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AB - Molecular chaperones are cellular machines that facilitate protein folding. The crystal structures of HtpG, the Escherichia coli homolog of hsp90, reported in this issue (Shiau et al., 2006) together with the recently published structures of an hsp90-cochaperone complex (Ali et al., 2006) and an hsp90-client protein complex (Vaughan et al., 2006), reveal exciting insights into the hsp90 reaction cycle.

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U2 - 10.1016/j.cell.2006.10.004

DO - 10.1016/j.cell.2006.10.004

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SN - 0092-8674

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hsp90: Twist and Fold

Abstract

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