Literature DB >> 17190592

Hosting neurotoxicity in polyglutamine disease.

Nan Liu1, Nancy M Bonini.   

Abstract

Polyglutamine diseases are caused by an expanded glutamine domain thought to confer a toxic activity onto the respective disease proteins. In this issue, propose that toxicity of the polyglutamine protein Ataxin-1 may not be due to abberant protein interactions mediated by the polyglutamine expansion. Instead, they suggest that toxicity is solely due to interactions of Ataxin-1 with its normal binding partners.

Entities:  

Mesh:

Substances:

Year:  2006        PMID: 17190592     DOI: 10.1016/j.cell.2006.12.012

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  1 in total

1.  Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors.

Authors:  Cesira de Chiara; Rajesh P Menon; Molly Strom; Toby J Gibson; Annalisa Pastore
Journal:  PLoS One       Date:  2009-12-23       Impact factor: 3.240

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.