Literature DB >> 2177651

Degradation of proteins by the ubiquitin-mediated proteolytic pathway.

A Ciechanover1, H Gonen, S Elias, A Mayer.   

Abstract

Degradation of a protein by the ubiquitin system involves two distinct processes. In the first step, ubiquitin is covalently linked in an ATP-dependent mode to the protein substrate. The protein moiety of the conjugate is then degraded by a specific protease into free amino acids, resulting in the release of free and reutilizable ubiquitin. This process also requires energy. In this review we will briefly summarize our current knowledge of the role of the ubiquitin system in protein turnover and discuss in detail the mechanism involved in selection of substrates for conjugation and in degradation of ubiquitin-conjugated proteins.

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Year:  1990        PMID: 2177651

Source DB:  PubMed          Journal:  New Biol        ISSN: 1043-4674


  5 in total

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Authors:  U Isozaki; W E Mitch; B K England; S R Price
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Authors:  M Scheffner; T Takahashi; J M Huibregtse; J D Minna; P M Howley
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Authors:  M Scheffner; K Münger; J M Huibregtse; P M Howley
Journal:  EMBO J       Date:  1992-07       Impact factor: 11.598

5.  Ubiquitin-independent, Proteasome-mediated targeted degradation of KRAS in pancreatic adenocarcinoma cells using an engineered ornithine decarboxylase/antizyme system.

Authors:  Yihui Ma; Jingjing Xu; Pei Huang; Xue Bai; Hanqing Gao
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  5 in total

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