Cargando…
Poly(ADP‐ribose)‐mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function
Poly(ADP‐ribose) (PAR) is a complex and reversible post‐translational modification that controls protein function and localization through covalent modification of, or noncovalent binding to target proteins. Previously, we and others characterized the noncovalent, high‐affinity binding of the key nu...
Autores principales: | Fischer, Jan M. F., Popp, Oliver, Gebhard, Daniel, Veith, Sebastian, Fischbach, Arthur, Beneke, Sascha, Leitenstorfer, Alfred, Bergemann, Jörg, Scheffner, Martin, Ferrando‐May, Elisa, Mangerich, Aswin, Bürkle, Alexander |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4160017/ https://www.ncbi.nlm.nih.gov/pubmed/24953096 http://dx.doi.org/10.1111/febs.12885 |
Ejemplares similares
-
Interactions of p53 with poly(ADP-ribose) and DNA induce distinct changes in protein structure as revealed by ATR-FTIR spectroscopy
por: Krüger, Annika, et al.
Publicado: (2019) -
The C-terminal domain of p53 orchestrates the interplay between non-covalent and covalent poly(ADP-ribosyl)ation of p53 by PARP1
por: Fischbach, Arthur, et al.
Publicado: (2018) -
Influence of chain length and branching on poly(ADP-ribose)–protein interactions
por: Löffler, Tobias, et al.
Publicado: (2023) -
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
por: Aberle, Lisa, et al.
Publicado: (2020) -
Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose)
por: Reber, Julia M, et al.
Publicado: (2021)