The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne
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Citations
Cites
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
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · cited 3×
“The glucocorticoid and progesterone receptors and, to a lesser extent, the oestrogen receptor, have been shown to require Hsp90 in order to assemble and maintain a high-af®nity, ligand-binding state.(7,8,15) The interaction between Hsp90 and the glucocorticoid receptor has been shown to localise to the ligand-binding…”
BackgroundMutational 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×
“The glucocorticoid and progesterone receptors and, to a lesser extent, the oestrogen receptor, have been shown to require Hsp90 in order to assemble and maintain a high-af®nity, ligand-binding state.(7,8,15) The interaction between Hsp90 and the glucocorticoid receptor has been shown to localise to the ligand-binding…”
BackgroundHeat-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
Structure and in vivo function of Hsp90
Pearl, L. H., & Prodromou, C. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00047-0 · Cited by 317
Binding of p23 and hsp90 during assembly with the progesterone receptor.
Johnson, J. L., & Toft, D. O. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.6.8592513 · Cited by 233
Morishima, Y., Murphy, P. J. M., Li, D.-P., Sanchez, E. R., & Pratt, W. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000434200 · Cited by 166 · cited 3×
“It is thought that the client protein ®rst interacts with Hsp70, possibly through an initial interaction with Hsp40.(19) Hop, which binds simultaneously to Hsp70 and Hsp90 through its N and C-terminal TPR domains, then brings the client protein into contact with Hsp90.”
BackgroundInfluentialCrystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperone
Weaver, A. J., Sullivan, W. P., Felts, S. J., Owen, B. A. L., & Toft, D. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003410200 · Cited by 136
Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
Structure and mechanism of the Hsp90 molecular chaperone machinery
Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103
Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
Metadata
- Authors
- McLaughlin, S. H., Smith, H. W., & Jackson, S. E.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2002-01
- Volume
- 315
- Issue
- 4
- Pages
- 787-798
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2160114316
- Cited by
- 242
- References
- 8
- Type
- book review
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne. https://app.cochat.ai/papers/10.1006/jmbi.2001.5245
- The paper
- McLaughlin, S. H., Smith, H. W., & Jackson, S. E. (2002). Stimulation of the weak ATPase activity of human Hsp90 by a client protein 1 1Edited by G. von Heijne. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.2001.5245
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
