The DOI matches its Crossref record; 111 of the 111 references it cites were found in a registry or an index.
Proteasome Inhibitors in Cancer Therapy: Lessons from the First Decade
Abstract
The ubiquitin-proteasome pathway is involved in intracellular protein turnover, and its function is crucial to cellular homeostasis. First synthesized as probes of proteolytic processes, proteasome inhibitors began to be thought of as potential drug candidates when they were found to induce programmed cell death preferentially in transformed cells. They made their first leap into the clinic to be tested as therapeutic agents 10 years ago, and since then, great strides have been made in defining their mechanisms of action, their clinical efficacy and toxicity, and some of their limitations in the form of resistance pathways. Validation of the ubiquitin-proteasome pathway as a target for cancer therapy has come in the form of approvals of the first such inhibitor, bortezomib, for relapsed/refractory multiple myeloma and mantle cell lymphoma, for which this agent has become a standard of care. Lessons learned from this first-in-class agent are now being applied to the development of a new generation of proteasome inhibitors that hold the promise of efficacy in bortezomib-resistant disease and possibly in a broader spectrum of diseases. This saga provides a salient example of the promise of translational medicine and a paradigm by which other agents may be successfully brought from the bench to the bedside.
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Cites
A Phase 2 Study of Bortezomib in Relapsed, Refractory Myeloma
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Bortezomib or High-Dose Dexamethasone for Relapsed Multiple Myeloma
Richardson, P. G., Sonneveld, P., Schuster, M. W., Irwin, D., Stadtmauer, E. A., Facon, T., Harousseau, J.-L., Ben-Yehuda, D., Lonial, S., Goldschmidt, H., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa043445 · Cited by 2,491
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Proteasome inhibitors: a novel class of potent and effective antitumor agents.
Adams, J., Palombella, V. J., Sausville, E. A., Johnson, J. I., Destree, A. T., Lazarus, D. D., Maas, J., Pien, C. S., Prakash, S., & Elliott, P. J. (1999) · PubMed · Cited by 1,477
Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
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Promiscuous Mutations Activate the Noncanonical NF-κB Pathway in Multiple Myeloma
Keats, J. J., Fonseca, R., Chesi, M., Schop, R., Baker, A., Chng, W.-J., Van Wier, S., Tiedemann, R., Shi, C.-X., Sebag, M., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.07.003 · Cited by 983
Cited by
Nasir, O. (2013) · Kidney and Blood Pressure Research · doi:10.1159/000350152 · Cited by 2,331
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764
Mitochondrial metabolism promotes adaptation to proteotoxic stress
Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645
Ubiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets
Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., & Brownell, J. E. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3321 · Cited by 563
“Such an approach offers a new 26S proteasome target that is independent of inhibiting proteasomal catalytic activities, for which there is already evidence of drug resistance 73 .”
BackgroundRadhakrishnan, S. K., Lee, C. S., Young, P., Beskow, A., Chan, J. Y., & Deshaies, R. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.029 · Cited by 526
Metadata
- Authors
- Orlowski, R. Z., & Kuhn, D. J.
- Venue
- Clinical Cancer Research
- Published
- 2008-03-15
- Volume
- 14
- Issue
- 6
- Pages
- 1649-1657
- ISSN
- 1078-0432 (ISSN-L)
- 1557-3265
- OpenAlex
- W2166761147
- Cited by
- 578
- References
- 111
- FWCI
- 25.44
- Type
- journal article
- Language
- en
- Open access
- closed
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