Cargando…
Slow Dissociation from the PARP1–HPF1 Complex Drives Inhibitor Potency
[Image: see text] PARP1, upon binding to damaged DNA, is activated to perform poly ADP-ribosylation (PARylation) on itself and other proteins, which leads to relaxation of chromatin and recruitment of DNA repair factors. HPF1 was recently discovered as a protein cofactor of PARP1 that directs prefer...
Autores principales: | Stojanovic, Petra, Luger, Karolin, Rudolph, Johannes |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10433523/ https://www.ncbi.nlm.nih.gov/pubmed/37531469 http://dx.doi.org/10.1021/acs.biochem.3c00243 |
Ejemplares similares
-
HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase
por: Rudolph, Johannes, et al.
Publicado: (2021) -
Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1
por: Gaullier, Guillaume, et al.
Publicado: (2020) -
Dual function of HPF1 in the modulation of PARP1 and PARP2 activities
por: Kurgina, Tatyana A., et al.
Publicado: (2021) -
Inhibitors of PARP: Number crunching and structure gazing
por: Rudolph, Johannes, et al.
Publicado: (2022) -
Histone Parylation factor 1 contributes to the inhibition of PARP1 by cancer drugs
por: Rudolph, Johannes, et al.
Publicado: (2021)