| Biologic impact of proteasome inhibition in multiple myeloma cells-from the aspects of preclinical studies. | |
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MedLine Citation:
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PMID: 22726545 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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The ubiquitin-proteasome pathway (UPP) is a major protein degradation system that maintains homeostasis of intracellular proteins, involved in DNA repair, cell cycle regulation, cell proliferation, and drug resistance. Since numerous proteins are processed by proteasomes, their inhibition triggers dramatic disruption of protein homeostasis. Consequently, accumulation of polyubiquitinated proteins triggers different types of cellular stress responses, followed by growth arrest and cytotoxicity. Importantly, multiple myeloma (MM) cells are considered to have lower threshold against these stresses than other cell types, which makes these cells sensitive to proteasome inhibitors. |
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Authors:
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Teru Hideshima; Kenneth C Anderson |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Seminars in hematology Volume: 49 ISSN: 1532-8686 ISO Abbreviation: Semin. Hematol. Publication Date: 2012 Jul |
Date Detail:
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Created Date: 2012-06-25 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0404514 Medline TA: Semin Hematol Country: United States |
Other Details:
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Languages: eng Pagination: 223-7 Citation Subset: IM |
Copyright Information:
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Copyright © 2012 Elsevier Inc. All rights reserved. |
Affiliation:
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Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology, Dana-Farber Cancer Institute and Harvard Medical School, Boston MA. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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