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Frontispiece: Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation‐Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6
Author(s) -
Chiki Anass,
DeGuire Sean M.,
Ruggeri Francesco S.,
Sanfelice Domenico,
Ansaloni Annalisa,
Wang ZheMing,
Cendrowska Urszula,
Burai Ritwik,
Vieweg Sophie,
Pastore Annalisa,
Dietler Giovanni,
Lashuel Hilal A.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201781961
Subject(s) - huntingtin , acetylation , phosphorylation , crosstalk , semisynthesis , chemistry , mutant , lysine , microbiology and biotechnology , biochemistry , biology , gene , amino acid , physics , optics
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.