Literature DB >> 12477409

Ubiquitin system: JAMMing in the name of the lid.

Christoph Berndt1, Dawadschargal Bech-Otschir, Wolfgang Dubiel, Michael Seeger.   

Abstract

The isopeptide bonds formed by ubiquitin or its relatives are cleaved by hydrolases with active site cysteines. Recent studies have revealed that similar metalloprotease motifs--JAMMs--in the Rpn11 subunit of the 26S proteasome lid and in the Csn5 subunit of the COP9 signalosome are involved in deubiquitination and deneddylation, respectively.

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Year:  2002        PMID: 12477409     DOI: 10.1016/s0960-9822(02)01317-9

Source DB:  PubMed          Journal:  Curr Biol        ISSN: 0960-9822            Impact factor:   10.834


  4 in total

1.  Characterization of the last subunit of the Arabidopsis COP9 signalosome.

Authors:  Nancy A Eckardt
Journal:  Plant Cell       Date:  2003-03       Impact factor: 11.277

Review 2.  The ubiquitin-proteasome system.

Authors:  Dipankar Nandi; Pankaj Tahiliani; Anujith Kumar; Dilip Chandu
Journal:  J Biosci       Date:  2006-03       Impact factor: 1.826

Review 3.  Protein partners of deubiquitinating enzymes.

Authors:  Karen H Ventii; Keith D Wilkinson
Journal:  Biochem J       Date:  2008-09-01       Impact factor: 3.857

4.  Computational Studies on the Inhibitor Selectivity of Human JAMM Deubiquitinylases Rpn11 and CSN5.

Authors:  Vikash Kumar; Michael Naumann; Matthias Stein
Journal:  Front Chem       Date:  2018-10-09       Impact factor: 5.221

  4 in total

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