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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
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
This study reports the novel findings that HER2 (show ERBB2 Proteins) increases PARP1 protein via suppression of the let-7a miRNA, which regulates the PARP1 3'-UTR. Moreover, HER2 (show ERBB2 Proteins) status correlates with high PARP1 and low let-7a in breast cancer clinical specimens.
Results show that PARP1 mediates 14-3-3s regulation of non-homologous end joining repair.
Identification of PARP-1 as a unique regulator of Il12b (show IL12B Proteins) transcription in response to inflammatory insults in an allele-differentiating manner
discuss the roles of PARP1 in mediating various aspects of DNA metabolism, such as single-strand break repair, nucleotide excision repair, double-strand break repair and the stabilization of replication forks, and in modulating chromatin structure. [Review]
The NF90 regulates PARP1 mRNA stability in hepatocellular carcinoma cells, and NF90 is a potential target to inhibit PARP1 activity.
In response to UV irradiation, DICER (show DICER1 Proteins) is recruited to chromatin in a ZRF1 (show DNAJC2 Proteins)-mediated manner. The H2A-ubiquitin binding protein ZRF1 (show DNAJC2 Proteins) and DICER (show DICER1 Proteins) together impact on the chromatin conformation via PARP1.
This paper summarises the most significant current literature on the involvement of PARP-1 in gastrointestinal cancer, focusing in particular on its role in the development and occurrence of tumours, providing information about clinical trials and exploring therapeutic possibilities. [review]
PARP-1 stabilizes Sox2 (show SOX2 Proteins) binding to nucleosomes at suboptimal sites through cooperative interactions on DNA to regulate Sox2 (show SOX2 Proteins) pioneer activity at intractable genomic loci.
PARP1 can modulate the tumor-suppressing function of HIPK2 (show HIPK2 Proteins) by regulating the protein stability of HIPK2 (show HIPK2 Proteins).
HBx increased signs of DNA damage such as accumulation of 8-hydroxy-2'-deoxyguanosine and comet formation, which were reversed by overexpression of PARP1 and/or Sirt6 (show SIRT6 Proteins)..physical interaction of HBx and PARP1 accelerates DNA damage by inhibiting recruitment of the DNA repair complex to the damaged DNA sites, which may lead to the onset of hepatocarcinogenesis
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
MEIS2 (show MEIS2 Proteins) associates with chromatin-bound PBX1 (show PBX1 Proteins), recruits PARP1/ARTD1, and initiates PARP1-mediated eviction of H1 from the chromatin fiber.
Activation of either PARP-1 or -2 is likely to play a role in muscle protein catabolism via oxidative stress, NF-kappaB (show NFKB1 Proteins) signaling, and enhanced proteasomal degradation in cancer-induced cachexia.
PARP-1 attenuates adipogenesis by PARylating C/EBPb (show CEBPB Proteins), a pro-adipogenic transcription factor, on three residues in its regulatory domain.
The findings suggest that PARP1 inhibition protects against long-term ethanol-induced liver injury, as indicated by limited hepatocytes steatosis, apoptosis, inflammation levels, and neutrophil infiltration, mainly by limiting KC activation during the initiation of ALD.
PARP-1 knockout resulted in lowered arginase II (show ARG2 Proteins) expression in macrophages and aortic endothelial cells.
Delayed healing in ischemic and diabetic wounds is caused by PARP hyperactivity, and PARP inhibition significantly enhanced ischemic and diabetic wound healing by promoting angiogenesis.
The findings highlight specific non-overlapping functions of PARP1 and PARP2 (show PARP2 Proteins) at H2AX (show H2AFX Proteins)-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 in nonhomologous end-joining-deficient cells.
data establish the importance of XRCC1 (show XRCC1 Proteins) protein complexes for normal neurological function and identify PARP1 as a therapeutic target in DNA strand break repair-defective disease
this study shows that PARP-1 inhibition plays role in puerarin-mediated protection from liver fibrosis
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.
, 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)
, 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)
, ADP-ribosyltransferase (NAD+, poly (ADP-ribose) polymerase) 1
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase) 1
, Poly[ADP-ribose] synthase 1