hsp90: Twist and Fold

Klaus Richter; Johannes Buchner

doi:10.1016/j.cell.2006.10.004

hsp90: Twist and Fold

Klaus Richter, Johannes Buchner

Research output: Contribution to journal › Short survey › peer-review

50 Scopus citations

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.

Original language	English
Pages (from-to)	251-253
Number of pages	3
Journal	Cell
Volume	127
Issue number	2
DOIs	https://doi.org/10.1016/j.cell.2006.10.004
State	Published - 20 Oct 2006

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10.1016/j.cell.2006.10.004

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title = "hsp90: Twist and Fold",

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.",

author = "Klaus Richter and Johannes Buchner",

year = "2006",

month = oct,

day = "20",

doi = "10.1016/j.cell.2006.10.004",

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journal = "Cell",

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T2 - Twist and Fold

AU - Richter, Klaus

AU - Buchner, Johannes

PY - 2006/10/20

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N2 - 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.

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

M3 - Short survey

C2 - 17055424

AN - SCOPUS:33749983958

SN - 0092-8674

VL - 127

SP - 251

EP - 253

JO - Cell

JF - Cell

IS - 2

ER -

hsp90: Twist and Fold

Abstract

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