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Due to today鈥檚 storm, 9I制作厂免费 classes are cancelled. Please note that campuses remain open, including Libraries, according to their schedules. For details, see the Alert email.


En raison de la temp锚te, les cours 脿 9I制作厂免费 sont annul茅s aujourd鈥檋ui. Veuillez noter que les campus restent ouverts, y compris les biblioth猫ques selon leurs horaires. Pour plus de d茅tails, voir le courriel d'alerte.

A new from my lab is now published online in a Nature paper Today. (Writes Parisa Ariya)

Classified as: Article
Published on: 20 Jun 2023

Human farnesyl pyrophosphate synthase (hFPPS) plays a key role in the prenylation of small GTPases, such as RAS and RAP 1A, which are intimately involved in oncogenesis. An allosteric pocket of the enzyme has been of particular interest as a therapeutic target, however, its natural biological function has been (until now) unknown. The teams of Berghuis (Biochemistry) and Tsantrizos (Chemistry) have just reported that the catalytic product of hFPPS, farnesyl pyrophosphate (FPP), bind to this pocket and locks the enzyme in a conformationally inactive state.

Classified as: Article
Category:
Published on: 21 Jan 2017
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