Literature DB >> 10934481

Ubiquitin biology: an old dog learns an old trick.

C M Pickart.   

Abstract

Regulated protein degradation in eukaryotes occurs principally through covalent tagging of substrates with ubiquitin, thereby targeting them for destruction by 26S proteasomes. Classical allostery has now been added to the repertoire of mechanisms that can modulate ubiquitin tagging, allowing feed-forward regulation to be achieved through targeted protein destruction.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 10934481     DOI: 10.1038/35019610

Source DB:  PubMed          Journal:  Nat Cell Biol        ISSN: 1465-7392            Impact factor:   28.824


  4 in total

Review 1.  The role of allostery in the ubiquitin-proteasome system.

Authors:  Jin Liu; Ruth Nussinov
Journal:  Crit Rev Biochem Mol Biol       Date:  2012-12-13       Impact factor: 8.250

2.  The MID1 E3 ligase catalyzes the polyubiquitination of Alpha4 (α4), a regulatory subunit of protein phosphatase 2A (PP2A): novel insights into MID1-mediated regulation of PP2A.

Authors:  Haijuan Du; Yongzhao Huang; Manar Zaghlula; Erica Walters; Timothy C Cox; Michael A Massiah
Journal:  J Biol Chem       Date:  2013-06-05       Impact factor: 5.157

3.  A Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation.

Authors:  Dimitrios Zattas; Jason M Berk; Stefan G Kreft; Mark Hochstrasser
Journal:  J Biol Chem       Date:  2016-04-11       Impact factor: 5.157

Review 4.  Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson's Disease and Dopa-Responsive Dystonia.

Authors:  Ichiro Kawahata; Kohji Fukunaga
Journal:  Int J Mol Sci       Date:  2020-05-27       Impact factor: 5.923

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.