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Molecular Cell, 2011 Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and thereby are essential for many aspects of cellular function. Because the proteolytic sites are sequestered in a closed barrel-shaped structure, activators are required to facilitate substrate access.
Stadtmueller, Beth M. +1 more
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Annual Review of Microbiology, 2015 Interest in bacterial proteasomes was sparked by the discovery that proteasomal degradation is required for the pathogenesis of Mycobacterium tuberculosis, one of the world's deadliest pathogens. Although bacterial proteasomes are structurally similar to their eukaryotic and archaeal homologs, there are key differences in their mechanisms of assembly,
Jordan B, Jastrab, K Heran, Darwin
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Modelling Proteasome and Proteasome Regulator Activities [PDF]
Biomolecules, 2014 Proteasomes are key proteases involved in a variety of processes ranging from the clearance of damaged proteins to the presentation of antigens to CD8+ T-lymphocytes. Which cleavage sites are used within the target proteins and how fast these proteins are degraded have a profound impact on immune system function and many cellular metabolic processes ...
Liepe, J +4 more
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The ubiquitin‐proteasome pathway and proteasome inhibitors [PDF]
Medicinal Research Reviews, 2001 AbstractThe ubiquitin‐proteasome pathway has emerged as a central player in the regulation of several diverse cellular processes. Here, we describe the important components of this complex biochemical machinery as well as several important cellular substrates targeted by this pathway and examples of human diseases resulting from defects in various ...
J, Myung, K B, Kim, C M, Crews
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Biochemical Pharmacology, 2015 Proteasome inhibitors have a 20 year history in cancer therapy. The first proteasome inhibitor, bortezomib (Velcade, PS-341), a break-through multiple myeloma treatment, moved rapidly through development from bench in 1994 to first approval in 2003. Bortezomib is a reversible boronic acid inhibitor of the chymotrypsin-like activity of the proteasome ...
Teicher, Beverly A. +1 more
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Rethinking Proteasome Evolution: Two Novel Bacterial Proteasomes [PDF]
Journal of Molecular Evolution, 2008 The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S ...
Valas, Ruben E., Bourne, Philip E.
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FEBS Letters, 2005 The 26S proteasome is responsible for regulated proteolysis of most intracellular proteins yet the focus of intense regulatory action itself. Proteasome abundance is responsive to cell needs or stress conditions, and dynamically localized to concentrations of substrates. Proteasomes are continually assembled and disassembled, and their subunits subject
Glickman, Michael H., Raveh, Dina
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Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014 Proteasomes are highly conserved multisubunit protease complexes and occur in the cyto- and nucleoplasm of eukaryotic cells. In dividing cells proteasomes exist as holoenzymes and primarily localize in the nucleus. During quiescence they dissociate into proteolytic core and regulatory complexes and are sequestered into motile cytosolic clusters ...
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Withdrawal: Human phosphatidylethanolamine-binding protein 4 promotes transactivation of estrogen receptor α (ERα) in human cancer cells by inhibiting proteasome-dependent ERα degradation via association with Src [PDF]
, 2021 Haibo Liu +4 more
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