THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATION

THE UBIQUITIN SYSTEM

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Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling

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Mapping of the Inducible IκB Phosphorylation Sites That Signal Its Ubiquitination and Degradation†

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The HECT Family of E3 Ubiquitin Ligases: Multiple Players in Cancer Development

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What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?

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Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments

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Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome

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Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.

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Identification and Characterization of XPC-Binding Domain of hHR23B

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The Ubiquitin E3 Ligase MARCH7 is Differentially Regulated by the Deubiquitylating Enzymes USP7 and USP9X

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Ubiquitin expression is up-regulated in human and rat skeletal muscles during aging

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Revealing the cellular degradome by mass spectrometry analysis of proteasome-cleaved peptides

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USP7 is a novel deubiquitinase sustaining PLK1 protein stability and regulating chromosome alignment in mitosis.

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Calorie restriction, stress and the ubiquitin-dependent pathway in mouse livers

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Autophagic activity measured in whole rat hepatocytes as the accumulation of a novel BHMT fragment (p10), generated in amphisomes by the asparaginyl proteinase, legumain

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Localization of Genes Encoding Two Human One-Domain Members of the AAA Family: PSMC5 (the Thyroid Hormone Receptor-Interacting Protein, TRIP1) and PSMC3 (the Tat-Binding Protein, TBP1)

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Untitled work

(2000) · doi:10.1002/1097-4547(20001001)62:1<9::aid-jnr2>3.0.co;2-u