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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
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
depletion of NOX1 (show NOX1 Proteins) and NOX4 (show NOX4 Proteins) partially rescued the growth inhibition of PARP1-deficient tumor xenografts. Our findings suggest that in addition to compromising the repair of DNA damage, PARP inhibition or depletion may exert extra antitumor effect by elevating oxidative stress in ovarian cancer cells
CDK4/6 (show CDK4 Proteins) inhibitors also lead to accumulation of DNA damage by repressing PARP1 in oxidatively stressed cells. Thus, CDK4/6 (show CDK4 Proteins) inhibitors sensitize G1-arrested cells to anticancer drugs, since these cells require PARP1-OGG1 (show OGG1 Proteins) functional interaction for cell survival
Low PARP expression is associated with mouth Cancer.
The dysfunction of PARP1 in esophageal epithelial cells increases the levels of ROS (show ROS1 Proteins) and oxidative DNA damage in Barrett's esophagus.
results suggest that PARP-1 overexpression may define an important risk factor in non-M3 AML (show RUNX1 Proteins) patients and PARP-1 is a potential therapeutic target for AML (show RUNX1 Proteins) treatment
polymorphism of PARP-1 gene is more likely responsible for development of GD in Chinese individuals
In response to DNA damage, activated and auto-poly-ADP-ribosylated PARP1 dissociates from HSF1 (show HSF1 Proteins)-PARP13 (show ZC3HAV1 Proteins), and redistributes to DNA lesions and DNA damage-inducible gene loci.
Results show that Rpp29 (show POP4 Proteins) and Rpp21 (show RPP21 Proteins) bind poly ADP-ribose moieties and are recruited to DNA damage sites in a PARP1-dependent manner.
PARP1 inhibitor also suppressed the aldosterone secretion in response to the angiotensin II. Together, these results suggest PARP1 is a prime coregulator for Nurr1 (show NR4A2 Proteins).
Here, we show that PARP1 and host insulator protein CTCF (show CTCF Proteins) colocalize at specific sites throughout the EBV genome and provide evidence to suggest that PARP1 acts to stabilize CTCF (show CTCF Proteins) binding and maintain the open chromatin landscape at the active Cp promoter during type III latency. Further, PARP1 activity is important in maintaining latency type-specific viral gene expression.
Peripheral T-cell number was not affected in single PARP1-deficient mice. Double-deficiency in PARP-1/PARP-2 (show PARP2 Proteins) in T-cells led to highly aggressive T-cell lymphomas.
pharmacological inhibition of PARP-1 reversed both particulate matter-induced Abeta (show APP Proteins) increase and glial activation.
The functional consequence of Parp1 heterozygosity on BRCA2 (show BRCA2 Proteins) loss is demonstrated by a significant increase in tumorigenesis in Brca2 (show BRCA2 Proteins) knockout mice.
findings reveal PARP-1 as a double-edged sword in colorectal carcinogenesis, which suppresses tumor initiation following DNA alkylation in a MGMT (show MGMT Proteins)-dependent manner, but promotes inflammation-driven tumor progression.
an immunoprecipitation assay indicated that hypoxia triggered activation of the binding activity of Sp1 (show SP1 Proteins) to the promoters of PARP-1 and caspase-3 (show CASP3 Proteins), which is abrogated by miR (show MLXIP Proteins)-7a/b. In summary, these findings identified miR (show MLXIP Proteins)-7a/b as protectors of cardiac remodeling and hypoxia-induced injury in H9c2 cardiomyoblasts involving Sp1 (show SP1 Proteins) and PARP-1.
PARP-1 mediated microgial responses can directly reduce blood brain barrier integrity by increasing endothelial cell permeability.
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.
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