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Human PARP1 Protein expressed in Baculovirus - ABIN1741729
Lamarre, Talbot, de Murcia, Laplante, Leduc, Mazen, Poirier: Structural and functional analysis of poly(ADP ribose) polymerase: an immunological study. in Biochimica et biophysica acta 1988
Show all 9 Pubmed References
Human PARP1 Protein expressed in Baculovirus - ABIN1741730
Woodhouse, Dianov: Poly ADP-ribose polymerase-1: an international molecule of mystery. in DNA repair 2008
Show all 11 Pubmed References
This study is the first to investigate the combination of PARP inhibitors with cytotoxic chemotherapy in acute leukemias in the clinical setting
Our data suggest that in both BRCA1-mutant and BRCA1-wild-type TNBCs, CSCs are relatively resistant to PARP inhibition. This resistance is mediated by RAD51 (show RAD51 Proteins), suggesting that strategies aimed at targeting RAD51 (show RAD51 Proteins) may increase the therapeutic efficacy of PARPi
SLFN11 is a relevant predictive biomarker of sensitivity to PARP inhibitor monotherapy in SCLC and we identify combinatorial therapy with TMZ as a particularly promising therapeutic strategy that warrants further clinical investigation
Data show that the combination of targeting RAD51 (show RAD51 Proteins) and p38 (show CRK Proteins) inhibits cell proliferation both in vitro and in vivo, which was further enhanced by targeting of PARP1.
Describe a novel series of 2,4-difluorophenyl- linker analogs derived from olaparib for use as PARP1 inhibitors BRCA-deficient tumors.
Co-localization of AP endonuclease (APE1 (show APEX1 Proteins)) with poly(ADP-ribose) polymerase 1 (PARP1) on DNA was found capable of inducing 1D diffusion of otherwise nonmotile PARP1, while excess APE1 (show APEX1 Proteins) also facilitated the dissociation of DNA-bound PARP1.
review of systematized and analyzed data on changes in PARP activity during development and aging of an organism, as well as data on differences in the dynamics of this activity in the presence/absence of additional stimulation and on cellular processes that are associated with activation of these enzymes.
High PARP1 expression is associated with hepatocellular carcinoma.
Up-regulation of PARP1 in the host nucleus is associated with Salmonella infection.
The mitochondrial localization of PARP1 and its intra-mitochondrial functions, with focus on cellular bioenergetics, mitochondrial DNA repair and mitochondrial dysfunction are reviewed.
A stimulation induced PARP1 binding to phosphorylated Erk2 (show MAPK1 Proteins) in the chromatin of cerebral neurons caused Erk (show EPHB2 Proteins)-induced PARP1 activation, rendering transcription factors and promoters of immediate early (show JUN Proteins) genes (IEG) accessible to PARP1-bound phosphorylated Erk2 (show MAPK1 Proteins).
The present work identifies several microglial responses to the endogenous alarmin S100B (show S100B Proteins), including release of the cytotoxic protease MMP9 (show MMP9 Proteins) and shows that these effects are modulated by PARP-1.
flavonoids of Rosa roxburghii Tratt enhanced radioprotection at least partially by regulating PARP-1/AIF (show AIFM1 Proteins) to reduce apoptosis.
These data demonstrate the presence of an FAF1 (show FAF1 Proteins)-PARP1 axis that is involved in oxidative stress-induced (show SQSTM1 Proteins) necrosis and in the pathology of Parkinson's disease.
Data indicate that poly(ADP-ribose)polymerase 1 (PARP1) D993A/D993A mice and cells are viable and show no obvious abnormalities.
Telomere-internal double-strand breaks (DSBs) are also repaired by a PARP1- and Ligase3-dependent reaction, suggesting alternative non-homologous end-joining (alt-NHEJ), which relies on microhomology at DSBs.
post-translational modification facilitates the mobilization of SIRT6 (show SIRT6 Proteins) to DNA damage sites and is required for efficient recruitment of poly (ADP-ribose) polymerase 1 (PARP1) to DNA break sites and for efficient repair of double-strand break.
Data show that Tp53 (show TP53 Proteins)- and Atm (show ATM Proteins)-defective Chronic lymphocytic leukemia (CLL) mimicking the high-risk form of human disease and that Atm (show ATM Proteins)-deficient CLL is sensitive to PARP1 inhibition.
The results suggest that ATRX (show ATRX Proteins) is required to limit replication stress during cellular proliferation, whereas upregulation of PARP-1 activity functions as a compensatory mechanism to protect stalled forks, limiting genomic damage, and facilitating late-born neuron production.
No increase of axonal regeneration was observed in Parp1(-/-) mice after optic nerve crush injury or dorsal hemisection of the thoracic spinal cord, and there was no improvement in motor function recovery. Comprehensive in vivo analysis reveals no indication that clinical PARP inhibitors will on their own provide benefit for recovery from central nervous system trauma.
The results demonstrate that PARylation process in Drosophila is tightly regulated in the context of strands-breaks repair; PARP is essential during the maintenance of DNA integrity, but dispensable in the DNA repair process.
A mutation of Parp also increases NAD+ levels; although, this was only observed in parkin (show PARK2 Proteins) mutant flies and not in the heterozygous Parp mutants, possibly owing to an increased PARP activity in the parkin (show PARK2 Proteins) mutants.
chromatin loosening and associated initiation of gene expression is activated by phosphorylation of H2Av (show H2AFV Proteins) in a nucleosome positioned in promoter regions of PARP-1-dependent genes
Based on these findings, we propose a model that explains how PARP1 activity impacts nucleolar functions and, consequently, ribosomal biogenesis
PARP is associated with the 5' end of Hsp70, and its enzymatic activity is rapidly induced by heat shock leading to nucleosome loss.
Activation of PARP-1 overexpression in the imago results in extension of the lifespan in females and males. The lifespan increase in females with PARP-1 conditional overexpression was accompanied by decrease of fertility.
PARP1 is targeted to chromatin by association with the histone H2A variant (H2Av).
demonstrate that this alteration specifically excludes PARP1 protein from heterochromatin and makes PARP1 unable to maintain repression of retrotransposable elements.
PARP-e autoregulates Parp transcription
propose that chromosomal PARP molecules become activated by developmental or environmental cues and strip nearby chromatin proteins off DNA to generate a puff
no difference was found in the level of SBDP145 between muscles, while SBDP120 and PARP-1 cleavage products were not detected
ADPRT Val762Ala and APE1 (show APEX1 Proteins) Asp148Glu polymorphisms are not associated with increased breast cancer risk
analysis of poly(ADP-ribose) polymerase 1 interaction with apurinic/apyrimidinic sites
FGF2 (show FGF2 Proteins) stimulates poly(ADP-ribose) polymerase activity by a DNA strand breaks-independent manner which involves a mitogen-activated protein kinases (MAPK (show MAPK1 Proteins))-dependent pathway
The transcript levels of autophagy-related genes and poly(ADP-ribose) polymerase 1 (PARP1), were transiently up-regulated by fertilization, decreased at the late 1-cell stage, and maintained until the blastocyst stage.
The PARP1 signaling pathway is involved in oocyte nest breakdown and primordial follicle formation in fetal and neonatal porcine ovaries, but is different from follicular atresia in adult porcine ovaries that involves cellular apoptosis.
Cleavage of PARP-1 by activated (cleaved) caspase-3 (show CASP3 Proteins) may serve a key role in controlling follicular atresia through granulosa cell degeneration.
This gene encodes a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes.
ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase)
, ADP-ribosyltransferase NAD(+)
, ADP-ribosyltransferase diphtheria toxin-like 1
, NAD(+) ADP-ribosyltransferase 1
, poly (ADP-ribose) polymerase family, member 1
, poly [ADP-ribose] polymerase 1
, poly(ADP-ribose) polymerase
, poly(ADP-ribose) synthetase
, poly[ADP-ribose] synthase 1
, ADP-ribosyltransferase (NAD+
, ADP-ribosyltransferase 1
, ADPRT 1
, poly (ADP-ribose) polymerase)
, poly(ADP-ribose) polymerase PARP-1
, poly[ADP-ribose] synthetase 1
, ADP-ribosyltransferase (NAD+, poly (ADP-ribose) polymerase) 1
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase) 1
, Poly(ADP ribose) polymerase 1
, Poly(ADP)-Ribose polymerase
, Poly(ADP-)Ribose polymerase
, Poly(ADP-ribose) polymerase
, Poly(ADP-ribose) polymerase 1
, ADP-ribosyltransferase (NAD+) poly (ADP-ribose) polymerase)
, Poly[ADP-ribose] synthase 1
, LOW QUALITY PROTEIN: poly [ADP-ribose] polymerase 1