Results 261 to 270 of about 39,389 (304)

Poly(ADP-ribose) polymerase: Structure-function relationship

Biochimie, 1995
Dissection of the human poly(ADP-ribose) polymerase (PARP) molecule in terms of its structure-function relationship has proved to be an essential step towards understanding the biological role of poly(ADP-ribosylation) as a cellular response to DNA damage in eukaryotes.
M. Masson, V. Rolli, F. Dantzer, C. Trucco, V. Schreiber, S. Fribourg, M. Molinete, A. Ruf, E. Alves Miranda, C. Niedergang, D. Hunting, B. Gowans, G.E. Schulz, J.Ménissier de Murcia, G. de Murcia   +14 more
openaire   +2 more sources

Poly(ADP-ribose)polymerase Inhibition - Where Now?

Current Medicinal Chemistry, 2005
The poly(ADP-ribose)polymerases (PARPs) catalyse the transfer of ADP-ribose units from the substrate NAD+ to acceptor proteins, biosynthesising polyanionic poly(ADP-ribose) polymers. A major isoform, PARP-1, has been the target for design of inhibitors for over twenty-five years.
Esther C Y, Woon, Michael D, Threadgill
openaire   +2 more sources

Regulatory mechanisms of poly(ADP-ribose) polymerase

Molecular and Cellular Biochemistry, 1999
Here, we describe the latest developments on the mechanistic characterization of poly(ADP-ribose) polymerase (PARP) [EC 2.4.2.30], a DNA-dependent enzyme that catalyzes the synthesis of protein-bound ADP-ribose polymers in eucaryotic chromatin. A detailed kinetic analysis of the automodification reaction of PARP in the presence of nicked dsDNA ...
R, Alvarez-Gonzalez, T A, Watkins, P K, Gill, J L, Reed, H, Mendoza-Alvarez   +4 more
openaire   +2 more sources

Poly(ADP-Ribose) Polymerase Inhibitor Combination Therapy

The Cancer Journal, 2021
Abstract The introduction of poly(ADP-ribose) polymerase (PARP) inhibitors has led to significant improvements in outcome for several cancer types, most notably high-grade serous ovarian cancer. However, in general, benefit is restricted to tumors characterized by either BRCA1/2 mutation or homologous recombination deficiency.
openaire   +2 more sources

Cytological detection of poly (ADP-ribose) polymerase

Experimental Cell Research, 1976
Abstract An attempt was made to demonstrate poly (ADP-ribose) polymerase cytologically. In vitro incorporation from the nucleotide, [ 3 H]NAD was detected in frozen sections of onion embryo and meristematic tissue by autoradiography. In meristematic tissue, there was a correlation between the number of cells displaying intensein vitro incorporation ...
J F, Payne, A K, Bal
openaire   +2 more sources

Interaction of poly(ADP-ribose)polymerase with DNA polymerase ?

Molecular and Cellular Biochemistry, 1994
Homogeneously purified poly(ADP-ribose) polymerase (PARP) specifically stimulated the activity of immunoaffinity-purified calf or human DNA polymerase alpha by about 6 to 60-fold. Apparently, poly(ADP-ribosyl)ation of DNA polymerase alpha was not necessary for the stimulation.
S, Yoshida, C M, Simbulan
openaire   +2 more sources

Activity Assays for Poly-ADP Ribose Polymerase

2004
Poly(ADP-ribose) polymerase (PARP-1) is a nuclear enzyme that has traditionally been thought to require discontinuous or "damaged" DNA (dcDNA) as a coenzyme, a preconception that has limited research mainly to its role in cell pathology, i.e., DNA repair and apoptosis.
Eva, Kirsten, Ernest, Kun, Jerome, Mendeleyev, Charles P, Ordahl   +3 more
openaire   +2 more sources

Detection of poly(ADP-ribose) polymerase and its reaction product poly(ADP-ribose) by immunocytochemistry

The Histochemical Journal, 1996
Poly(ADP-ribose) polymerase catalyses the formation of ADP-ribose polymers covalently attached to various nuclear proteins, using NAD+ as substrate. The activity of this enzyme is strongly stimulated upon binding to DNA single or double strand breaks. Poly(ADP-ribosyl)ation is an immediate cellular response to DNA damage and is thought to be involved ...
J H, Küpper, L, van Gool, M, Müller, A, Bürkle   +3 more
openaire   +2 more sources

Poly(ADP-ribose) polymerase and aging

2001
Publisher Summary Poly(ADP-ribose) polymerase (PARP) is a major nuclear protein associated with chromatin that contains zinc fingers and binds to either double- or single-strand DNA breaks. Upon binding to DNA, PARP is activated and forms covalent homopolymers of poly(ADP-ribose) (PAR) attached to a number of nuclear proteins, including itself and ...
Dean S. Rosenthal, Cynthia M. Simbulan-Rosenthal, Wen Fang Liu, Mark E. Smulson   +3 more
openaire   +1 more source

Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1, PARP2 and PARP3.

Experimental Cell Research, 2014
Carole Beck, I. Robert, B. Reina-San-Martin, V. Schreiber, F. Dantzer   +4 more
semanticscholar   +1 more source