Slow Dissociation from the PARP1–HPF1 Complex Drives Inhibitor Potency
Author:
Affiliation:
1. Department of Biochemistry, University of Colorado Boulder, Boulder, Colorado 80309, United States
2. Howard Hughes Medical Institute, University of Colorado Boulder, Boulder, Colorado 80309, United States
Funder
Howard Hughes Medical Institute
National Cancer Institute
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.3c00243
Reference35 articles.
1. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
2. Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance
3. PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification
4. Progress and outlook in studying the substrate specificities of PARPs and related enzymes
5. HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
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