A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from Bortezomib.
By D. Chauhan, L. Catley, Guilan Li, K. Podar, T. Hideshima, Mugdha Velankar, C. Mitsiades, Nicolas Mitsiades, H. Yasui, A. Letai and 8 more. Cancer Cell, 2005
685 citations recorded by the source corpus.
Subfields: Hematology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/0cfa27fb05cd0e1d37697febb9d66680b5a083c2
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Citations in the corpus
- Theoretical Basis, Experimental Design, and Computerized Simulation of Synergism and Antagonism in Drug Combination Studies (2006, methodology): “(1990), Prichard and Shipman (1990), Suhnel (1990), Chou (1991), Schinazi (1991), Jackson (1991), Lam (1991), Tallarida (1992), and Greco et al. (1995). Among them, a recent review by Berenbaum (1989) has listed 560 references and another review by Greco et al.”
- Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma. (2005, background): “Interestingly, NPI-0052 activated apoptosis predominantly through a caspase-8mediated pathway, with little dependence on caspase-9.(13) Bortezomib preferentially inhibits the ChT-L activity, as does carfilzomib, while NPI-0052 inhibits the ChT-L, as well as the PGPH and T-L proteases.”
- Developing a new resource for drug discovery: marine actinomycete bacteria (2006, background): “In addition, salinisporamide A has in vivo efficacy against human tumors in mouse models when administered orall”
- Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome. (2007, background): “(20) have reported similar results with bortezomib and have also shown that salinosporamide A, at a dose that fully inhibits proteasome chymotrypsin-like activity in blood, can also partially suppress the trypsin-like and caspase-like activities.”
- A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis (2009, background): “However, most well characterized proteasome inhibitors mediate equivalent inhibition of both proteasome chymotrypsin-like activities (β5 and LMP7”