Frontispiece: Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation‐Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6

Huntington's Disease In their Communication on page 5202 ff. H. A. Lashuel et al. use protein semisynthesis to investigate the effect of lysine acetylation and phosphorylation on the aggregation of mutant huntingtin exon1. While phosphorylation significantly inhibits the aggregation, acetylatio...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2017-05, Vol.56 (19), p.n/a
Main Authors: Chiki, Anass, DeGuire, Sean M., Ruggeri, Francesco S., Sanfelice, Domenico, Ansaloni, Annalisa, Wang, Zhe‐Ming, Cendrowska, Urszula, Burai, Ritwik, Vieweg, Sophie, Pastore, Annalisa, Dietler, Giovanni, Lashuel, Hilal A.
Format: Article
Language:English
Subjects:
acetylation
fibrils
Huntington's disease
Phosphorylation
semisynthesis
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Summary:Huntington's Disease In their Communication on page 5202 ff. H. A. Lashuel et al. use protein semisynthesis to investigate the effect of lysine acetylation and phosphorylation on the aggregation of mutant huntingtin exon1. While phosphorylation significantly inhibits the aggregation, acetylation has no effect.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201781961