The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
The 90-kDa Molecular Chaperone Family
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Citations
Cites
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
Heat Shock Transcription Factors: Structure and Regulation
Wu, C. (1995) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cb.11.110195.002301 · Cited by 1,231
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 4×
“. hsp90 is necessary for proper steroid action in vivo (Picard et al., 1990; Bohen and Yamamoto, 1993; Nathan and Lindquist, 1995).”
InfluentialMammalian 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 5×
“…v-Raf, c-Raf, B-Raf Stancato et al., 1993; Wartmann and Davis, 1994; Jaiswal et al., 1996 Gag-Mil Lovric et al., 1994 MEK Stancato et al., 1997 CDK4 Stepanova et al., 1996; Dai et al., 1996 eIF-2-␣ kinase Rose et al., 1987; Matts and Hurst, 1989 eEF-2-␣ kinase Nygard et al., 1991; Palmquist et…”
InfluentialGradin, K., McGuire, J., Wenger, R. H., Kvietikova, I., Whitelaw, M. L., Toftgård, R., Tora, L., Gassmann, M., & Poellinger, L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5221 · Cited by 470
Mutational 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 4×
“hsp90 is necessary for the correct folding, and thus, for the activity of many of these kinases, such as the v-Src kinase (Xu and Lindquist, 1993; Nathan and Lindquist, 1995), the Raf kinase (van der Straten et al.”
InfluentialHeat-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 2×
“hsp90 is necessary for the correct folding, and thus, for the activity of many of these kinases, such as the v-Src kinase (Xu and Lindquist, 1993; Nathan and Lindquist, 1995), the Raf kinase (van der Straten et al.”
Freeman, B. C., Toft, D. O., & Morimoto, R. I. (1996) · Science · doi:10.1126/science.274.5293.1718 · Cited by 370 · cited 1×
“…the fact that besides the " classical " chaperones hsc70 and 90-kDa Molecular Chaperones in Health and Disease 137 hsp90, almost all the other components have chaperone activities in in vitro assays when added alone (Duina et al., 1996; Bose et al., 1996; Freeman et al., 1996; Kimura et al., 1997).”
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
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693
HSP90 as a new therapeutic target for cancer therapy: the story unfolds
Maloney, A., & Workman, P. (2002) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2.1.3 · Cited by 531
Transcriptome-wide Regulation of Pre-mRNA Splicing and mRNA Localization by Muscleblind Proteins
Wang, E. T., Cody, N. A. L., Jog, S., Biancolella, M., Wang, T. T., Treacy, D. J., Luo, S., Schroth, G. P., Housman, D. E., Reddy, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.041 · Cited by 490
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
- Csermely, P., Schnaider, T., So″ti, C., Prohászka, Z., & Nardai, G.
- Venue
- Pharmacology & Therapeutics
- Publisher
- Elsevier BV
- Published
- 1998-08
- Volume
- 79
- Issue
- 2
- Pages
- 129-168
- ISSN
- 0163-7258 (ISSN-L)
- OpenAlex
- W153442697
- Cited by
- 1,028
- References
- 15
- FWCI
- 10.92
- Type
- journal article
- Language
- en
- Open access
- closed
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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 90-kDa Molecular Chaperone Family. https://app.cochat.ai/papers/10.1016/s0163-7258(98)00013-8
- The paper
- Csermely, P., Schnaider, T., So″ti, C., Prohászka, Z., & Nardai, G. (1998). The 90-kDa Molecular Chaperone Family. Pharmacology & Therapeutics. https://doi.org/10.1016/s0163-7258(98)00013-8
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.
