Poly(ADP-ribose) polymerase-1 activation during DNA damage and repair

Autor: Dantzer, F., Amž, J., Schreiber, V., Nakamura, J., Mžnissier-de Murcia, J., de Murcia, G.

Publikováno v: Methods in Enzymology
Methods in Enzymology, Elsevier, 2006, 409, pp.493-510. ⟨10.1016/S0076-6879(05)09029-4⟩
Methods in Enzymology, Elsevier, 2006, 409, pp.493-510

Changes in chromatin structure emanating from DNA breaks are among the most initiating events in the damage response of the cell. In higher eukaryotes, poly(ADP-ribose) polymerase-1 (PARP-1) translates the occurrence of DNA breaks detected by its zin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::751efb4e9b11d63bd7149a1445955d6c
https://pubmed.ncbi.nlm.nih.gov/16793420

Control of mitotic Aurora-B kinase by poly(ADP-ribosyl)ation directs self-renewal of spermatogonial cells following DNA damage

Autor: Monaco, L., Kolthur-Seetharam, U., Loury, R., MŽnissier-De Murcia, J., Parvinen, M., De Murcia, G., Assone-Corsi, P.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2005, 102, pp.14244-14248

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______1398::9441ddcb62e4fb0728a70ebc66862209
https://hal.archives-ouvertes.fr/hal-00129936

Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2

Autor: Oliver, A W, Amé, J C, Roe, S M, Good, V, de Murcia, G, Pearl, L H

Poly(ADP-ribose) polymerase-1 (PARP-1) has become an important pharmacological target in the treatment of cancer due to its cellular role as a 'DNA-strand break sensor', which leads in part to resistance to some existing chemo- and radiological treat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::a59d4d483b839d333e149e16b66e465c
http://sro.sussex.ac.uk/id/eprint/28431/1/Nucl._Acids_Res.-2004-Oliver-456-64.pdf

Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching

Autor: de Murcia G, O'Farrell M, Rolli, Ménissier-de Murcia J

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 1997, 36 (40), pp.12147-54. ⟨10.1021/bi971055p⟩

Poly(ADP-ribose) polymerase (PARP) is a multifunctional nuclear zinc finger protein which participates in the immediate response of mammalian cells exposed to DNA damaging agents. Given the complexity of the poly(ADP-ribosylation) reaction, we develo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c197c39648c3bd625fce5f5f83e6667c
https://hal.archives-ouvertes.fr/hal-02371496

Accessibility and structural role of histone domains in chromatin. biophysical and immunochemical studies of progressive digestion with immobilized proteases

Autor: Hacques Mf, Sylviane Muller, De Murcia G, Marion C, Van Regenmortel Mh

Publikováno v: Journal of Biomolecular Structure and Dynamics
Journal of Biomolecular Structure and Dynamics, Taylor & Francis: STM, Behavioural Science and Public Health Titles, 1990, 8 (3), pp.619-41. ⟨10.1080/07391102.1990.10507832⟩

The accessibility and role of histone regions in chromatin fibres were investigated using limited proteolysis with enzymes covalently bound to collagen membranes. The changes in chromatin conformation and condensation monitored by various biophysical

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::884528312e6795cee9a535f999929521
https://pubmed.ncbi.nlm.nih.gov/2100522