Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody-Reference-Cited by-同舟云学术

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Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody

Published:2004-12-14 Issue:51 Volume:101 Page:17616-17621
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Colby D. W.,Chu Y.,Cassady J. P.,Duennwald M.,Zazulak H.,Webster J. M.,Messer A.,Lindquist S.,Ingram V. M.,Wittrup K. D.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference37 articles.

1. Development of a Human Light Chain Variable Domain (VL) Intracellular Antibody Specific for the Amino Terminus of Huntingtin via Yeast Surface Display

2. Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity

3. Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease

4. A single-chain Fv intrabody provides functional protection against the effects of mutant protein in an organotypic slice culture model of Huntington's disease

5. Selection of antibodies for intracellular function using a two-hybrid in vivo system

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