The Infona portal uses cookies, i.e. strings of text saved by a browser on the user's device. The portal can access those files and use them to remember the user's data, such as their chosen settings (screen view, interface language, etc.), or their login data. By using the Infona portal the user accepts automatic saving and using this information for portal operation purposes. More information on the subject can be found in the Privacy Policy and Terms of Service. By closing this window the user confirms that they have read the information on cookie usage, and they accept the privacy policy and the way cookies are used by the portal. You can change the cookie settings in your browser.
Herein, we used protein semisynthesis to investigate, for the first time, the effect of lysine acetylation and phosphorylation, as well as the crosstalk between these modifications on the structure and aggregation of mutant huntingtin exon1 (Httex1). Our results demonstrate that phosphorylation at T3 stabilizes the α‐helical conformation of the N‐terminal 17 amino acids (Nt17) and significantly inhibits...
Huntington‐Krankheit In der Zuschrift auf S. 5286 ff. nutzen H. A. Lashuel et al. die Proteinsemisynthese, um die Auswirkungen der Acetylierung und Phosphorylierung von Lysin auf die Aggregation eines mutierten Huntingtin‐Proteins zu untersuchen. Während Phosphorylierung die Aggregation hemmt, hat Acetylierung keinen Effekt.
Set the date range to filter the displayed results. You can set a starting date, ending date or both. You can enter the dates manually or choose them from the calendar.