Literature DB >> 11864588

Polyglutamine disease: acetyltransferases awry.

Robert E Hughes1.   

Abstract

Recent evidence indicates that inhibition of histone acetyltransferases may be a primary cause of cellular pathogenesis in polyglutamine diseases such as Huntington disease; the results raise the possibility that pharmacologic manipulation of protein acetylation levels could be of therapeutic benefit.

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Year:  2002        PMID: 11864588     DOI: 10.1016/s0960-9822(02)00709-1

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


  7 in total

Review 1.  Protein misfolding, aggregation, and degradation in disease.

Authors:  Niels Gregersen; Lars Bolund; Peter Bross
Journal:  Mol Biotechnol       Date:  2005-10       Impact factor: 2.695

Review 2.  Neurodegenerative disorders: Parkinson's disease and Huntington's disease.

Authors:  S M Hague; S Klaffke; O Bandmann
Journal:  J Neurol Neurosurg Psychiatry       Date:  2005-08       Impact factor: 10.154

Review 3.  The biological effects of simple tandem repeats: lessons from the repeat expansion diseases.

Authors:  Karen Usdin
Journal:  Genome Res       Date:  2008-07       Impact factor: 9.043

4.  Polyglutamine-expanded spinocerebellar ataxia-7 protein disrupts normal SAGA and SLIK histone acetyltransferase activity.

Authors:  Stacey J McMahon; Marilyn G Pray-Grant; David Schieltz; John R Yates; Patrick A Grant
Journal:  Proc Natl Acad Sci U S A       Date:  2005-06-02       Impact factor: 11.205

Review 5.  The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases.

Authors:  Xiang-Jiao Yang
Journal:  Nucleic Acids Res       Date:  2004-02-11       Impact factor: 16.971

6.  Safety, pharmacokinetics, pharmacogenomics and QT concentration-effect modelling of the SirT1 inhibitor selisistat in healthy volunteers.

Authors:  Goran Westerberg; Joseph A Chiesa; Claus A Andersen; Daniela Diamanti; Letizia Magnoni; Giuseppe Pollio; Borje Darpo; Meijian Zhou
Journal:  Br J Clin Pharmacol       Date:  2015-03       Impact factor: 4.335

7.  SUMO-1 modification on K166 of polyQ-expanded ataxin-3 strengthens its stability and increases its cytotoxicity.

Authors:  Ya-Fang Zhou; Shu-Sheng Liao; Ying-Ying Luo; Jian-Guang Tang; Jun-Ling Wang; Li-Fang Lei; Jing-Wei Chi; Juan Du; Hong Jiang; Kun Xia; Bei-Sha Tang; Lu Shen
Journal:  PLoS One       Date:  2013-01-31       Impact factor: 3.240

  7 in total

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