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Title:
The ubiquitin-proteasome system | Journal of Biosciences
Description:
The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic proteins targeted for degradation by this pathway are first ‘tagged’ by multimers of a protein known as ubiquitin and are later proteolyzed by a giant enzyme known as the proteasome. This article recounts the key observations that led to the discovery of ubiquitin-proteasome system (UPS). In addition, different aspects of proteasome biology are highlighted. Finally, some key roles of the UPS in different areas of biology and the use of inhibitors of this pathway as possible drug targets are discussed.
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Keywords {🔍}
pubmed, google, scholar, article, cas, proteasome, biol, central, cell, protein, chem, system, degradation, proteasomes, goldberg, sci, kloetzel, subunit, ciechanover, ubiquitin, activator, baumeister, usa, biochem, tanaka, mammalian, natl, acad, rechsteiner, ubiquitinproteasome, nandi, proteins, london, proteolysis, particle, monaco, mol, atpdependent, hershko, function, inhibitor, rev, demartino, proteolytic, structure, huber, site, ubiquitination, cellular, eukaryotic,
Topics {✒️}
anujith kumar & dilip chandu month download article/chapter implications forproteasome-pan/pa700 interactions nucleotide-sensitive proteasome-interacting proteins 1997 ube3a/e6-ap mutations atp-dependent proteolysis factor nuclear envelope-er network delta-aminolevulinic acid dehydratase heat-stable polypeptide component n-end rule pathway atp-dependent proteases lon ubiquitin-conjugating enzyme results atp-dependent proteolytic system aproteasome-11s activator complex arginine-rich peptides constitute ubiquitin/atp-dependent proteases ubiquitin-protein ligase system ubiquitin-proteasome pathway-mediated protein-unfolding molecular chaperone active site nucleophile atp-dependent protein breakdown full article pdf atp-dependent proteolysis van den broek active site function 2004 n-terminal ubiquitination privacy choices/manage cookies eukaryotic proteins targeted deficient cell proliferation scf ubiquitin ligase proteasome subunit lmp-7 cellular proteolysis n-terminal acetylation peptide products generated small-molecule antagonists atp-dependent protease central area multiubiquitin chain assembly subunit precursor processing proteasome ofmycobacterium tuberculosis precursor beta subunits proteasome-activating nucleotidase unusual macromolecular complex ubiquitin-proteasome system ubiquitin–proteasome system ubiquitin proteasome system core particle maturation author correspondence protein-unfolding machines molecular bassifor selectivity
Questions {❓}
- Kisselev A F, Songyang Z and Goldberg A L 2000 Why does threonine, and not serine, function as the active site nucleophile in proteasomes?
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headline:The ubiquitin-proteasome system
description:The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic proteins targeted for degradation by this pathway are first ‘tagged’ by multimers of a protein known as ubiquitin and are later proteolyzed by a giant enzyme known as the proteasome. This article recounts the key observations that led to the discovery of ubiquitin-proteasome system (UPS). In addition, different aspects of proteasome biology are highlighted. Finally, some key roles of the UPS in different areas of biology and the use of inhibitors of this pathway as possible drug targets are discussed.
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proteasomes
protein degradation
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Microbiology
Cell Biology
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