Literature DB >> 23148019

Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity.

Zhe-Ming Wang1, Hilal A Lashuel.   

Abstract

Aggravating aggregation: an N-terminal domain that is in close proximity to the polyQ domain in the huntingtin protein, htt105-138, is shown to be highly aggregation prone. Potential cross-talk between this domain and the polyQ region may play a central role in regulating the aggregation and toxicity of Htt-N-terminal fragments.
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2012        PMID: 23148019     DOI: 10.1002/anie.201206561

Source DB:  PubMed          Journal:  Angew Chem Int Ed Engl        ISSN: 1433-7851            Impact factor:   15.336


  3 in total

1.  Structure and topology of the huntingtin 1-17 membrane anchor by a combined solution and solid-state NMR approach.

Authors:  Matthias Michalek; Evgeniy S Salnikov; Burkhard Bechinger
Journal:  Biophys J       Date:  2013-08-06       Impact factor: 4.033

2.  A huntingtin-mediated fast stress response halting endosomal trafficking is defective in Huntington's disease.

Authors:  Siddharth Nath; Lise N Munsie; Ray Truant
Journal:  Hum Mol Genet       Date:  2014-09-08       Impact factor: 6.150

3.  Protein-protein interactions as a strategy towards protein-specific drug design: the example of ataxin-1.

Authors:  Cesira de Chiara; Rajesh P Menon; Geoff Kelly; Annalisa Pastore
Journal:  PLoS One       Date:  2013-10-14       Impact factor: 3.240

  3 in total

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