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Recognition of the polyubiquitin proteolytic signal.
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The 26S proteasome: a molecular machine designed for controlled proteolysis.
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Trends Cell Biol. 2000 Aug;10(8):335-42
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Degradation of the E7 human papillomavirus oncoprotein by the ubiquitin-proteasome system: targeting via ubiquitination of the N-terminal residue.
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Degradation of oxidized proteins by the 20S proteasome.
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The C-terminal fragment of the Alzheimer's disease amyloid protein precursor is degraded by a proteasome-dependent mechanism distinct from gamma-secretase.
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alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome.
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The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26 S proteasome.
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A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein.
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