The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
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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
Self-citationMutational 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
Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370
Smith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300
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
Reconstitution of Progesterone Receptor with Heat Shock Proteins
Smith, D. F., Schowalter, D. B., Kost, S. L., & Toft, D. O. (1990) · Molecular Endocrinology · doi:10.1210/mend-4-11-1704 · Cited by 144
ATP induces a conformational change of the 90-kDa heat shock protein (hsp90).
Csermely, P., Kajtár, J., Hollósi, M., Jalsovszky, G., Holly, S., Kahn, C. R., Gergely, P., Söti, C., Mihály, K., & Somogyi, J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53939-9 · Cited by 133
Bohen, S. P. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3330 · Cited by 106
Weikl, T., Abelmann, K., & Buchner, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3172 · Cited by 97
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
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
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-citationZhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., et al. (2005) · Cell · doi:10.1016/j.cell.2004.12.024 · Cited by 819
Metadata
- Authors
- Young, J. C.
- Venue
- The EMBO Journal
- Published
- 2000-11-01
- Volume
- 19
- Issue
- 21
- Pages
- 5930-5940
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W1989074864
- Cited by
- 232
- References
- 9
- FWCI
- 5.07
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. https://app.cochat.ai/papers/10.1093/emboj/19.21.5930
- The paper
- Young, J. C. (2000). Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. The EMBO Journal. https://doi.org/10.1093/emboj/19.21.5930
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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.
