Transition State of ADP-Ribosylation of Acetyllysine Catalyzed by Archaeoglobus fulgidus Sir2 Determined by Kinetic Isotope Effects and Computational Approaches
Author:
Affiliation:
1. Department of Pharmacology, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10065
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja910342d
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2. The Sir2 Family of Protein Deacetylases
3. Plasmodium falciparum Sir2 is an NAD+-Dependent Deacetylase and an Acetyllysine-Dependent and Acetyllysine-Independent NAD+ Glycohydrolase
4. Plasmodium falciparum Sir2: an Unusual Sirtuin with Dual Histone Deacetylase and ADP-Ribosyltransferase Activity
5. Investigating the ADP-ribosyltransferase Activity of Sirtuins with NAD Analogues and 32P-NAD
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