Literature DB >> 15498483

NF-kappaB signaling: flipping the switch with polyubiquitin chains.

Tommer Ravid1, Mark Hochstrasser.   

Abstract

Protein modification by ubiquitin has emerged as an important cellular regulatory mechanism. Recent studies illustrate the surprising ways in which polyubiquitin chains are manipulated in the regulation of NF-kappaB signaling.

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Year:  2004        PMID： 15498483     DOI： 10.1016/j.cub.2004.09.074

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


  4 in total

1.  Evidence that the kinase-truncated c-Src regulates NF-κB signaling by targeting NEMO.

Authors:  S Dai; W Abu-Amer; K Karuppaiah; Y Abu-Amer
Journal:  J Cell Biochem       Date:  2011-09       Impact factor: 4.429

2.  Phosphorylation of the Gal4 DNA-binding domain is essential for activator mono-ubiquitylation and efficient promoter occupancy.

Authors:  Anwarul Ferdous; Melissa O'Neal; Kip Nalley; Devanjan Sikder; Thomas Kodadek; Stephen Albert Johnston
Journal:  Mol Biosyst       Date:  2008-08-26

Review 3.  Polyubiquitin binding and disassembly by deubiquitinating enzymes.

Authors:  Francisca E Reyes-Turcu; Keith D Wilkinson
Journal:  Chem Rev       Date:  2009-04       Impact factor: 60.622

4.  Inflammatory osteolysis is regulated by site-specific ISGylation of the scaffold protein NEMO.

Authors:  Naga Suresh Adapala; Gaurav Swarnkar; Manoj Arra; Jie Shen; Gabriel Mbalaviele; Ke Ke; Yousef Abu-Amer
Journal:  Elife       Date:  2020-03-23       Impact factor: 8.140
  4 in total

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