The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Heat Shock Proteins Promote Cancer: It's a Protection Racket
Open accessAbstract
Heat Shock Proteins (HSP) are expressed at high levels in cancer and form a fostering environment essential for tumor development. We have reviewed the recent data in this area, concentrating mainly on Hsp27, Hsp70 and Hsp90. The overriding role of the HSPs in cancer is to stabilize the active functions of overexpressed and mutated cancer gene. Elevated HSPs are thus required for many of the traits that underlie the morbidity of cancer, including increased growth, survival and formation of secondary cancers. In addition, HSPs participate in the evolution of cancer treatment resistance. HSPs are also released from cancer cells and influence malignant properties by receptor- mediated signaling. Current data strongly support efforts to target HSPs in cancer treatment.
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Cites
Aging, Cellular Senescence, and Cancer
Campisi, J. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183653 · Cited by 2,954 · cited 1×
“Normal cells resist transformation by having a limited number of permitted divisions [51].”
BackgroundHsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
DNA-Repair Defects and Olaparib in Metastatic Prostate Cancer
Mateo, J., Carreira, S., Sandhu, S., Miranda, S., Mossop, H., Perez-Lopez, R., Nava Rodrigues, D., Robinson, D., Omlin, A., Tunariu, N., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1506859 · Cited by 2,185
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 1×
“It is an interesting theme that many proteins that are persistently associated with Hsp90 complexes, although stable and fully folded, are inactive[16, 17].”
BackgroundKirschke, E., Goswami, D., Southworth, D., Griffin, P. R., & Agard, D. A. (2014) · Cell · doi:10.1016/j.cell.2014.04.038 · Cited by 399
Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein
Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.003 · Cited by 151 · cited 1×
“Hsp60, Hsp70, Hsp90 and Hsp110 each utilize ATP binding and hydrolysis to mediate cycles of polypeptide binding, folding and release [5, 7, 10, 11].”
BackgroundThe co‐chaperone p23 promotes prostate cancer motility and metastasis
Querol Cano, L., Lavery, D. N., Sin, S., Spanjaard, E., Brooke, G. N., Tilman, J. D., Abroaf, A., Gaughan, L., Robson, C. N., Heer, R., et al. (2015) · Molecular Oncology · doi:10.1016/j.molonc.2014.08.014 · Cited by 33 · cited 1×
“In addition, elevated co-chaperone levels also promote (prostate) cancer; increased levels of the Hsp90 co-chaperone p23 increases metastasis in prostate cancer[70].”
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Cited by
Zhou, J., Li, M., Hou, Y., Luo, Z., Chen, Q., Cao, H., Huo, R., Xue, C., Sutrisno, L., Hao, L., et al. (2018) · ACS Nano · doi:10.1021/acsnano.8b00309 · Cited by 424
Metadata
- Authors
- Calderwood, S. K., & Gong, J.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2016-04
- Volume
- 41
- Issue
- 4
- Pages
- 311-323
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2252295447
- Cited by
- 407
- References
- 7
- FWCI
- 2.53
- Type
- journal article
- Language
- en
- Open access
- green
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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.
