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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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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container_issue 19
container_start_page
container_title Angewandte Chemie International Edition
container_volume 56
creator 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.
description 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.
doi_str_mv 10.1002/anie.201781961
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subjects acetylation
fibrils
Huntington's disease
Phosphorylation
semisynthesis
title Frontispiece: Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation‐Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6
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