The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor.
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Citations
Cites
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
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
A 59-kilodalton protein associated with progestin, estrogen, androgen and glucocorticoid receptors
Tai, P. K. K., Maeda, Y., Nakao, K., Wakim, N. G., Duhring, J. L., & Faber, L. E. (1986) · Biochemistry · doi:10.1021/bi00366a043 · Cited by 257
Smith, D. F., Faber, L. E., & Toft, D. O. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39693-0 · Cited by 221
HSP56: a novel heat shock protein associated with untransformed steroid receptor complexes
Sanchez, E. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45667-0 · Cited by 214
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
Ning, Y. M., & Sánchez, E. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53220-8 · Cited by 136
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
Cited by
The role of the hypothalamic-pituitary-adrenal axis in neuroendocrine responses to stress
Smith, S. M., & Vale, W. W. (2006) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2006.8.4/ssmith · Cited by 1,948
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
Self-citationThe Aryl Hydrocarbon Receptor Complex
Hankinson, O. (1995) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.35.040195.001515 · Cited by 1,649
An Orphan Nuclear Receptor Activated by Pregnanes Defines a Novel Steroid Signaling Pathway
Kliewer, S. A., Moore, J. T., Wade, L., Staudinger, J. L., Watson, M. A., Jones, S. A., McKee, D. D., Oliver, B. B., Willson, T. M., Zetterström, R. H., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)80900-9 · Cited by 1,539
Glucocorticoid receptors in major depression: relevance to pathophysiology and treatment
Pariante, C. M., & Miller, A. H. (2001) · Biological Psychiatry · doi:10.1016/s0006-3223(00)01088-x · Cited by 1,147
Metadata
- Authors
- Pratt, W. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-10
- Volume
- 268
- Issue
- 29
- Pages
- 21455-21458
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1576929531
- Cited by
- 653
- References
- 8
- FWCI
- 19.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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- CoChat. (2026). Citation check: The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. https://app.cochat.ai/papers/10.1016/s0021-9258(20)80556-0
- The paper
- Pratt, W. B. (1993). The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(20)80556-0
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.
