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Dog (Canine) Polyclonal PARP2 Primary Antibody for ELISA, WB - ABIN547604
Kofler, Otsuka, Zhang, Noppens, Grafe, Koh, Dawson, de Murcia, Hurn, Traystman: Differential effect of PARP-2 deletion on brain injury after focal and global cerebral ischemia. in Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2005
Human Polyclonal PARP2 Primary Antibody for ChIP, IP - ABIN2668807
Hanzlikova, Gittens, Krejcikova, Zeng, Caldecott: Overlapping roles for PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin. in Nucleic acids research 2016
Human Polyclonal PARP2 Primary Antibody for WB - ABIN151360
Ovadje, Ammar, Guerrero, Arnason, Pandey: Dandelion root extract affects colorectal cancer proliferation and survival through the activation of multiple death signalling pathways. in Oncotarget 2016
analysis of how ARTD2/PARP2 functions in DNA break recognition
PARP2 is preferentially activated by poly(ADP-ribose) (PAR) and subsequently catalyzes branched PAR chain synthesis.
data further suggest that ARTD2 would function in double strand break repair as a dimeric module, while in single strand break repair it would function as a monomer.
Report a requirement for PARP2 in stabilizing replication forks that encounter base excision repair (BER) intermediates through Fbh1-dependent regulation of Rad51. Whereas PARP2 is dispensable for tolerance of cells to single stranded breaks or homologous recombination dysfunction, it is redundant with PARP1 in BER.
PARP2 specifically limits the accumulation of the resection barrier factor 53BP1 at DNA damage sites, allowing efficient CtIP-dependent DNA end-resection
either PARP1 or PARP2 are sufficient for near-normal XRCC1 recruitment at oxidative single-strand breaks
Studies indicate that poly(ADP-ribose) polymerase 2 (PARP2) is involved in the differentiation of several cell types, including erythrocytes, T cells and adipocytes.
Findings indicate that Increased poly(ADP-ribose) polymerase-2 (PARP-2) expression and loss of micrRNA miR-149 expression are involved in the pathogenesis of hepatocellular carcinomas (HCC) and are poor prognosis factors in patients with HCC.
Data show that E7449 represents a dual Poly(ADP-ribose) Polymerase 1/2 and tankyrase 1/2 inhibitor which has the advantage of targeting Wnt/beta-catenin signaling addicted tumors.
The initial affinity between the PARP1, PARP2 and the DNA damaged site appears to influence both the size of the Poly(ADP-Ribose) synthesized and the time of residence of PARylated PARP1 and PARP2 on DNA damages.
Our data suggest for the first time that a SNP in PARP2, rs878156, may together with other genetic variants modulate cancer specific survival in breast cancer patients depending on chemotherapy
Our study differentiates the functions of PARP-2 domains from those of PARP-1, the other major DDR-PARP, and highlights the specialization of the multi-domain architectures of DDR-PARPs.
Interaction of PARP-2 with AP site containing DNA
Identification of ADP-ribosylation sites in PARP2 and the determination of the extent ofpoly(ADP-ribosyl)ated residues in this protein was performed.
Nuclear Smad function is negatively regulated by PARP-1 that is assisted by PARP-2 and positively regulated by PARG during the course of TGFB signaling.
the depletion of PARP-2 leads to lower HDL levels which represent a risk factor to cardiovascular diseases.
these findings propose a novel mechanism of PARP-2 in transcriptional regulation involving specific protein-protein interactions and highlight the importance of PARP-2 in the regulation of cell cycle progression.
PARP-1 (but not PARP-2) poly(ADP) ribosylates Snail1, both in vivo and in vitro, and interacts with Snail1, an association that is sensitive to PARP inhibitors.
In complex with its inhibitor, the crystal structure of PARP2 alpha-helix 5 that contains glutamate residue Glu335 is closer to the active site than in both PARP1 and PARP3 and suggests a mechanism for a weak bias toward PARP2.
The PARP-2 gene might be associated with azoospermia by meiotic arrest
PARP2 can PARylate and mono(ADP-ribosyl)ate (MARylate), respectively, 5'- and 3'-terminal phosphate residues at double- and single-strand break termini of a DNA molecule containing multiple strand breaks.
Results provide evidence for a new role for PARP2 as a lipid-modulated regulator of lipid metabolism.
Peripheral T-cell number was not affected in single PARP-2-deficient mice. Double-deficiency in PARP-1/PARP-2 in T-cells led to highly aggressive T-cell lymphomas.
PARP2 protein deficiency protected mice from Concanavalin A -induced Liver Damage.
Activation of either PARP-1 or -2 is likely to play a role in muscle protein catabolism via oxidative stress, NF-kappaB signaling, and enhanced proteasomal degradation in cancer-induced cachexia.
PARP1/2 inhibitor simmiparib causes growth inhibition in cancer cell- or tissue-derived xenografts in nude mice.
The findings highlight specific non-overlapping functions of PARP1 and PARP2 at H2AX-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 in nonhomologous end-joining-deficient cells.
Data show reduced tumor burden through increased oxidative stress in lung adenocarcinoma cells of PARP-1 and PARP-2 knockout mice.
PARP-2 has an essential role in erythropoiesis by limiting replicative stress in erythroid progenitors.
PARP-1 and -2 play a role in cancer-induced cachexia, thus selective pharmacological inhibition of PARP-1 and -2 may be of interest in clinical settings
This study represents the first description of a significant role for PARP-2 in neuroinflammation and neurological dysfunction in Experimental autoimmune encephalomyelitis
our data show that PARP-2 can directly regulate base excision repair proteins
Our results show that Parp-2 plays essential roles in the surveillance of genome integrity of stem cell hematopoiesis by orchestrating DNA repair and restraining p53-induced and Puma-mediated apoptosis.
PARP2 activity mobilizes intracellular TRPM2 channels in a Parp1-/- background.
Identify PARP-2 as a mediator of doxorubicin toxicity by regulating vascular SIRT1 activity and mitochondrial biogenesis.
Inhibition of PARP1 and PARP2 (by genetic or pharmacological means) leads to increased TOP2B activity in elongating spermatids.
PARP-2 deletion in mice increases SIRT1 levels, promotes energy expenditure, and increases mitochondrial content.
role of PARP-2 activity in the maintenance of telomere integrity; PARP-2 physically binds to TRF2 with high affinity
We found that larger deletions of >20 bp predominated after DSB repair in ku80 and ku80 parp1 parp2 mutants, corroborating with a role of KU in preventing DSB end resection. Deletion lengths did not significantly differ between ku80 and ku80 parp1 parp2 mutants, suggesting that a KU- and PARP-independent b-NHEJ mechanism becomes active in these mutants.
we have found that although plant PARPs and PARGs have partially overlapping functions Arabidopsis PARP2 and PARG1 play the predominant roles in plant poly(ADP-ribosyl)ation during DNA damage and immune responses.
whilst all isoforms of PARP were localized to the nucleus they are also present in non-nuclear locations with parp1 and parp3 also localised in the cytosol, and parp2 also present in the mitochondria
Studies indicate that a massive and rapid accumulation of a massive and rapid accumulation poly(ADP-ribose) polymerases AtPARP1 and AtPARP2 transcripts was observed upon treatment with ionizing radiation and reactive oxigen species (ROS).
Poly(ADP-ribose)polymerase activity controls plant growth by promoting leaf cell number.
Evidence suggests a link between the glutathione pool and PARP expression and activity that is perhaps related to the distribution of intracellular glutathione between the cytoplasm and the nucleus. [PARP2]
This gene encodes poly(ADP-ribosyl)transferase-like 2 protein, which contains a catalytic domain and is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. The basic residues within the N-terminal region of this protein may bear potential DNA-binding properties, and may be involved in the nuclear and/or nucleolar targeting of the protein. Two alternatively spliced transcript variants encoding distinct isoforms have been found.
ADP-ribosyltransferase (NAD+; poly(ADP-ribose) polymerase)-like 2
, ADP-ribosyltransferase diphtheria toxin-like 2
, NAD(+) ADP-ribosyltransferase 2
, poly (ADP-ribose) polymerase family, member 2
, poly (ADP-ribosyl) transferase-like 2
, poly [ADP-ribose] polymerase 2
, poly(ADP-ribose) synthetase
, poly[ADP-ribose] synthase 2
, poly[ADP-ribose] synthetase 2
, ADP-ribosyltransferase (NAD+, poly(ADP-ribose) polymerase)-like 2
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase) 2
, poly (ADP-ribose) polymerase 2
, poly [ADP-ribose] polymerase 2-like
, Poly[ADP-ribose] synthase 2