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Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy

Biochemical Society Transactions · 2007 · Vol. 35(1) · pp. 12–17
Alfred L. Goldberg

Abstract

This review focuses on recent insights into the mechanisms and the biological functions of the proteasome. This large ATP-dependent proteolytic complex is the main site for protein degradation in mammalian cells and catalyses the rapid degradation of ubiquitinated proteins, and is the source of most antigenic peptides used by the immune system to screen for viruses and cancer. ATP is required to unfold globular proteins to open the gated channel into the 20S proteasome and to facilitate protein translation into it. Inhibitors of its proteolytic activity are widely used as research tools and have proven effective in cancer therapy.

Ubiquitin and proteasome pathwaysAutophagy in Disease and TherapyPeptidase Inhibition and AnalysisProteasomeProtein degradationUbiquitinImmune systemProteolysisCancer therapyCancerChemistryGlobular proteinDegradation (telecommunications)

MeSH terms

Adenosine TriphosphateAnimalsAntineoplastic AgentsCatalysisHumansImmune SystemModels, BiologicalModels, ChemicalNeoplasmsUbiquitinProteasome Endopeptidase Complex
Citations
368
FWCI
13.94
field-weighted impact
References
30
Percentile
99%
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Citations per year
References
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Annual Review of Biochemistry · 1999 · 1,887 citations
THE UBIQUITIN SYSTEM
Annual Review of Biochemistry · 1998 · 8,726 citations
Intracellular Protein Degradation in Mammalian and Bacterial Cells
Annual Review of Biochemistry · 1974 · 1,774 citations
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