Abstract
It should be clear from the foregoing accounts that our understanding of MCP and 26S regulation is still rudimentary. Moreover, we have only recently identified about a dozen natural substrates of these two proteases. Those outside the field may view the situation with some dismay. Those who study the MCP and 26S enzymes are provided with rich opportunities to address fundamental questions of protein catabolism and metabolic regulation.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Animals
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Archaea / enzymology
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Cysteine Endopeptidases / chemistry
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Cysteine Endopeptidases / genetics
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Cysteine Endopeptidases / physiology*
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Eukaryotic Cells / enzymology
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Gene Expression Regulation, Enzymologic
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Humans
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Models, Molecular
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Molecular Sequence Data
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Multienzyme Complexes / chemistry
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Multienzyme Complexes / genetics
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Multienzyme Complexes / physiology*
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Neoplasm Proteins / physiology
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Peptide Hydrolases / chemistry
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Peptide Hydrolases / genetics
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Peptide Hydrolases / physiology*
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Proteasome Endopeptidase Complex
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Protein Conformation
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Protein Processing, Post-Translational
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Proteins / physiology
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Rats
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Stress, Physiological / enzymology
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Subcellular Fractions / enzymology
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Substrate Specificity
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Tumor Cells, Cultured
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Ubiquitins / metabolism
Substances
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Multienzyme Complexes
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Neoplasm Proteins
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Proteins
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Ubiquitins
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multicatalytic protease activator
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Adenosine Triphosphate
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Peptide Hydrolases
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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ATP dependent 26S protease