The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Hsp90: Chaperoning signal transduction
Open accessAbstract
Hsp90 is an ATP dependent molecular chaperone involved in the folding and activation of an unknown number of substrate proteins. These substrate proteins include protein kinases and transcription factors. Consistent with this task, Hsp90 is an essential protein in all eucaryotes. The interaction of Hsp90 with its substrate proteins involves the transient formation of multiprotein complexes with a set of highly conserved partner proteins. The specific function of each component in the processing of substrates is still unknown. Large ATP‐dependent conformational changes of Hsp90 occur during the hydrolysis reaction and these changes are thought to drive the chaperone cycle. Natural inhibitors of the ATPase activity, like geldanamycin and radicicol, block the processing of Hsp90 substrate proteins. As many of these substrates are critical elements in signal transduction, Hsp90 seems to introduce an additional level of regulation. © 2001 Wiley‐Liss, Inc.
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Cites
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
Roe, S. M., Prodromou, C., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm980403y · Cited by 1,004
Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
Stepanova, L., Leng, X., Parker, S. B., & Harper, J. W. (1996) · Genes & Development · doi:10.1101/gad.10.12.1491 · Cited by 483 · cited 4×
“…al. (1997) Fak Ochel et al. (1999) Serine-threonine Kinases Raf Stancato et al. (1993) Gag-Mil Lovric et al. (1994) MEK Stancato et al. (1997) Cdk4 Stepanova et al. (1996) eEF 2a-kinase Palmquist et al. (1994) eIF 2a-kinase Rose et al. (1987) Protein kinase CK-II Dougherty et al. (1987); Miyata…”
InfluentialMutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423 · cited 1×
“Temperature-sensitive mutants of yeast Hsp90 showed that disruption of the Hsp90 system is not toxic to the cell but induces a growth arrest until permissive temperatures allowed the Hsp90 mutants to gain back their function (Kimura et al., 1994; Nathan and Lindquist, 1995).”
BackgroundSmith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300
Aligue, R., Akhavan‐Niak, H., & Russell, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06956.x · Cited by 261
Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
Scheibel, T., Weikl, T., & Buchner, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1495 · Cited by 243
Cited by
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
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
Mishra, S. K., Tripp, J., Winkelhaus, S., Tschiersch, B., Theres, K., Nover, L., & Scharf, K.-D. (2002) · Genes & Development · doi:10.1101/gad.228802 · Cited by 603
Shiau, A. K., Harris, S. F., Southworth, D. R., & Agard, D. A. (2006) · Cell · doi:10.1016/j.cell.2006.09.027 · Cited by 455
The Hsp90 molecular chaperone: an open and shut case for treatment
Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal · doi:10.1042/bj20071640 · Cited by 447
Metadata
- Authors
- Richter, K., & Buchner, J.
- Venue
- Journal of Cellular Physiology
- Publisher
- Wiley
- Published
- 2001-07-20
- Volume
- 188
- Issue
- 3
- Pages
- 281-290
- ISSN
- 0021-9541 (ISSN-L)
- 1097-4652
- OpenAlex
- W2067529967
- Cited by
- 570
- References
- 15
- FWCI
- 15.85
- Type
- journal article
- Language
- en
- Open access
- bronze
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