Hsp90

Young, Jason C.; Moarefi, Ismail; Hartl, F. Ulrich

doi:10.1083/jcb.200104079

Cited by 822

The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.

Hsp90

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Young, Jason C., Moarefi, Ismail, Hartl, F. Ulrich·2001·The Journal of Cell Biology

DOI 10.1083/jcb.200104079

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Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.

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Hsp90 as a capacitor for morphological evolution
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Self-citation
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BackgroundInfluential
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BackgroundInfluential
Heat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416 · cited 4×
“, 1990; for review see Pratt and Toft, 1997), several tyrosine and serine/ threonine kinases such as pp60/v-src, Wee-1, Cdk4, and Raf (Xu and Lindquist, 1993; Aligue et al., 1994; Stepanova et al., 1996; van der Straten et al., 1997), and disparate proteins such as nitric oxide synthase and calcineurin (Garon S etem e…”
BackgroundInfluential
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Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370 · cited 3×
“In fulfilling its role, Hsp90 operates as part of a multichaperone machinery in the cytosol, which includes Hsp70 as mentioned above but also peptidyl-prolyl isomerases and other cochaperones (Bose et al., 1996; Freeman et al., 1996).”
Background
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Aligue, R., Akhavan‐Niak, H., & Russell, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06956.x · Cited by 261
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Scheibel, T., Weikl, T., & Buchner, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1495 · Cited by 243
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
Freeman, B. C., Felts, S. J., Toft, D. O., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.14.4.422 · Cited by 168 · cited 1×
“The recently reported Hsp90-independent effects of p23 on steroid hormone receptor signaling (Freeman et al., 2000) may arise from this chaperone domain.”
Background

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Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
Wang, W., Vinocur, B., Shoseyov, O., & Altman, A. (2004) · Trends in Plant Science · doi:10.1016/j.tplants.2004.03.006 · Cited by 2,759
Hsp90 as a capacitor of phenotypic variation
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Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
Young, J. C., Hoogenraad, N. J., & Hartl, F. U. (2003) · Cell · doi:10.1016/s0092-8674(02)01250-3 · Cited by 915
Self-citation
Hsp90 Potentiates the Rapid Evolution of New Traits: Drug Resistance in Diverse Fungi
Cowen, L. E., & Lindquist, S. (2005) · Science · doi:10.1126/science.1118370 · Cited by 698
CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein
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See all 822

Authors: Young, J. C., Moarefi, I., & Hartl, F. U.
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2001-07-23
Volume: 154
Issue: 2
Pages: 267-274
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.200104079
OpenAlex: W2097840941
Cited by: 822
References: 14
FWCI: 16.50
Type: journal article
Language: en
Open access: green

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Hsp90

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