The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Geldanamycin as a Potential Anti-Cancer Agent: Its Molecular Target and Biochemical Activity
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Citations
Cites
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Weinberg, R. A. (1995) · Cell · doi:10.1016/0092-8674(95)90385-2 · Cited by 4,862
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
Self-citationRoe, 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
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
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 5×
“Interestingly, the complexes Cdk4 forms with Hsp90/p50Cdc37 are mutually exclusive to those it forms with cyclin D [54], suggesting that Hsp90 serves to fold and sequester Cdk4 in an inactive but primed conformation, which dissociates from the chaperone complex upon binding to cyclin D.”
BackgroundInfluentialMutational 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
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 · cited 1×
“Also, c-Src expressed in yeast was not destabilized or inactivated in an Hsp90-deficient mutant [18].”
BackgroundAligue, R., Akhavan‐Niak, H., & Russell, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06956.x · Cited by 261
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
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
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
17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Sang, C., Tanaka, F., Inukai, A., Doyu, M., & Sobue, G. (2005) · Nature Medicine · doi:10.1038/nm1298 · Cited by 395
Modulation of p53, ErbB1, ErbB2, and Raf-1 Expression in Lung Cancer Cells by Depsipeptide FR901228
Yu, X. (2002) · CancerSpectrum Knowledge Environment · doi:10.1093/jnci/94.7.504 · Cited by 360
Xu, W., Mimnaugh, E., Rosser, M. F. N., Nicchitta, C., Marcu, M., Yarden, Y., & Neckers, L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006864200 · Cited by 353
Self-citationHeat-shock proteins: chaperoning DNA repair
Dubrez, L., Causse, S., Borges Bonan, N., Dumétier, B., & Garrido, C. (2020) · Oncogene · doi:10.1038/s41388-019-1016-y · Cited by 224
Metadata
- Authors
- Neckers, L., Schulte, T. W., & Mimnaugh, E.
- Venue
- Investigational New Drugs
- Published
- 1999-11
- Volume
- 17
- Issue
- 4
- Pages
- 361-373
- ISSN
- 0167-6997 (ISSN-L)
- 1573-0646
- OpenAlex
- W1586440254
- Cited by
- 301
- References
- 10
- FWCI
- 4.13
- 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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- This page
- CoChat. (2026). Citation check: Geldanamycin as a Potential Anti-Cancer Agent: Its Molecular Target and Biochemical Activity. https://app.cochat.ai/papers/10.1023/a:1006382320697
- The paper
- Neckers, L., Schulte, T. W., & Mimnaugh, E. (1999). Geldanamycin as a Potential Anti-Cancer Agent: Its Molecular Target and Biochemical Activity. Investigational New Drugs. https://doi.org/10.1023/a%3A1006382320697
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.
