Search Results - "Goldberg, A L"
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Atrogin-1, A Muscle-Specific F-Box Protein Highly Expressed during Muscle Atrophy
Published in Proceedings of the National Academy of Sciences - PNAS (04-12-2001)“…Muscle wasting is a debilitating consequence of fasting, inactivity, cancer, and other systemic diseases that results primarily from accelerated protein…”
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What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
Published in Current opinion in clinical nutrition and metabolic care (01-05-2001)“…Studies of many different rodent models of muscle wasting have indicated that accelerated proteolysis via the ubiquitin-proteasome pathway is the principal…”
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Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
Published in The Journal of nutrition (01-01-1999)Get more information
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Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy
Published in Biochemical Society transactions (01-02-2007)“…This review focuses on recent insights into the mechanisms and the biological functions of the proteasome. This large ATP-dependent proteolytic complex is the…”
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Proteasomes play an essential role in thymocyte apoptosis
Published in The EMBO journal (01-08-1996)“…Cell death in many different organisms requires the activation of proteolytic cascades involving cytosolic proteases. Here we describe a novel requirement in…”
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Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
Published in The American journal of physiology (01-04-1993)“…Glucocorticoids are essential for the increase in protein breakdown in skeletal muscle normally seen during fasting. To determine which proteolytic pathway(s)…”
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Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy
Published in Biochemical journal (01-05-1995)“…Most of the increased protein degradation in muscle atrophy caused by starvation and denervation is due to activation of a non-lysosomal ATP-dependent…”
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Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma
Published in The American journal of physiology (01-05-1995)“…Rats implanted with Yoshida ascites hepatoma (YAH) show a rapid and selective loss of muscle protein due mainly to a marked increase (63-95%) in the rate of…”
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PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
Published in Nature cell biology (01-11-2000)“…The proteasome-activating nucleotidase (PAN) from Methanococcus jannaschii is a complex of relative molecular mass 650,000 that is homologous to the ATPases in…”
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Functions of the Proteasome: The Lysis at the End of the Tunnel
Published in Science (American Association for the Advancement of Science) (28-04-1995)“…Most proteins in eukaryotic cells are degraded by a soluble, adenosine triphosphate (ATP)-dependent pathway present in both the nucleus and cytosol. This…”
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Proteolysis, proteasomes and antigen presentation
Published in Nature (London) (04-06-1992)“…Proteins presented to the immune system must first be cleaved to small peptides by intracellular proteinases. Proteasomes are proteolytic complexes that…”
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Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
Published in The Journal of clinical investigation (01-07-1997)“…Several observations have suggested that the enhanced proteolysis and atrophy of skeletal muscle in various pathological states is due primarily to activation…”
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Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes
Published in The Journal of clinical investigation (01-05-1994)“…Metabolic acidosis often leads to loss of body protein due mainly to accelerated protein breakdown in muscle. To identify which proteolytic pathway is…”
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Protein degradation and protection against misfolded or damaged proteins
Published in Nature (London) (18-12-2003)“…The ultimate mechanism that cells use to ensure the quality of intracellular proteins is the selective destruction of misfolded or damaged polypeptides. In…”
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γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
Published in Nature (London) (16-09-1993)“…The presentation of intracellular proteins to the immune system requires their degradation to small peptides that then become associated with major…”
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The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins
Published in The Journal of biological chemistry (25-03-1990)“…Mammalian cells contain two large proteolytic complexes, the 650-kDa proteasome (or multicatalytic protease) and the 1500-kDa (26 S)…”
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Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
Published in The Journal of clinical investigation (01-11-1999)“…Insulin deficiency (e.g., in acute diabetes or fasting) is associated with enhanced protein breakdown in skeletal muscle leading to muscle wasting. Because…”
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The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes
Published in Biochimie (01-03-2001)“…26S proteasomes are composed of a 20S proteolytic core and two ATPase-containing 19S regulatory particles. To clarify the role of these ATPases in proteolysis,…”
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The N-end Rule Pathway Catalyzes a Major Fraction of the Protein Degradation in Skeletal Muscle
Published in The Journal of biological chemistry (25-09-1998)“…In skeletal muscle, overall protein degradation involves the ubiquitin-proteasome system. One property of a protein that leads to rapid ubiquitin-dependent…”
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Puromycin-sensitive aminopeptidase is the major peptidase responsible for digesting polyglutamine sequences released by proteasomes during protein degradation
Published in The EMBO journal (07-03-2007)“…Long stretches of glutamine (Q) residues are found in many cellular proteins. Expansion of these polyglutamine (polyQ) sequences is the underlying cause of…”
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