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PARP2 specifically limits the accumulation of the resection barrier factor 53BP1 (show TP53BP1 Proteins) at DNA damage sites, allowing efficient CtIP (show RBBP8 Proteins)-dependent DNA end-resection
either PARP1 (show PARP1 Proteins) or PARP2 are sufficient for near-normal XRCC1 (show XRCC1 Proteins) 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 (show MLXIP Proteins)-149 expression are involved in the pathogenesis of hepatocellular carcinomas (HCC (show FAM126A Proteins)) and are poor prognosis factors in patients with HCC (show FAM126A Proteins).
Data show that E7449 represents a dual Poly(ADP-ribose) Polymerase 1 (show PARP1 Proteins)/2 and tankyrase 1 (show TNKS Proteins)/2 inhibitor which has the advantage of targeting Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling addicted tumors.
The initial affinity between the PARP1 (show PARP1 Proteins), 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 (show PARP1 Proteins) 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 (show PARP1 Proteins), the other major DDR (show DDR1 Proteins)-PARP, and highlights the specialization of the multi-domain architectures of DDR (show DDR1 Proteins)-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.
PARP2 protein deficiency protected mice from Concanavalin A -induced Liver Damage.
Activation of either PARP-1 (show PARP1 Proteins) 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.
PARP1 (show PARP1 Proteins)/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 (show PARP1 Proteins) and PARP2 at H2AX (show H2AFX Proteins)-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 (show PARP1 Proteins) in nonhomologous end-joining-deficient cells.
Data show reduced tumor burden through increased oxidative stress in lung adenocarcinoma cells of PARP-1 (show PARP1 Proteins) and PARP-2 knockout mice.
PARP-2 has an essential role in erythropoiesis by limiting replicative stress in erythroid progenitors.
PARP-1 (show PARP1 Proteins) and -2 play a role in cancer-induced cachexia, thus selective pharmacological inhibition of PARP-1 (show PARP1 Proteins) and -2 may be of interest in clinical settings
the depletion of PARP-2 leads to lower HDL (show HSD11B1 Proteins) levels which represent a risk factor to cardiovascular diseases.
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
We found that larger deletions of >20 bp predominated after DSB repair in ku80 (show XRCC5 Proteins) and ku80 (show XRCC5 Proteins) parp1 parp2 mutants, corroborating with a role of KU in preventing DSB end resection. Deletion lengths did not significantly differ between ku80 (show XRCC5 Proteins) and ku80 (show XRCC5 Proteins) parp1 parp2 mutants, suggesting that a KU- and PARP (show PARP1 Proteins)-independent b-NHEJ mechanism becomes active in these mutants.
whilst all isoforms of PARP (show PARP1 Proteins) were localized to the nucleus they are also present in non-nuclear locations with parp1 and parp3 (show PARP3 Proteins) 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 (show ROS1 Proteins)).
PARP (show PARP1 Proteins) isoforms play a minor role in telomere length maintenance in Arabidopsis.
Evidence suggests a link between the glutathione pool and PARP (show PARP1 Proteins) expression and activity that is perhaps related to the distribution of intracellular glutathione between the cytoplasm and the nucleus. [PARP1]
in PARP2-deficient Arabidopsis plants, the observed abiotic stress resistance can also be explained by alterations in abscisic acid levels that facilitate the induction of a wide set of defense-related genes
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.
poly (ADP-ribose) polymerase family, member 2
, ADP-ribosyltransferase (NAD+; poly(ADP-ribose) polymerase)-like 2
, ADP-ribosyltransferase (NAD+, poly(ADP-ribose) polymerase)-like 2
, poly [ADP-ribose] polymerase 2
, poly (ADP-ribose) polymerase 2
, poly [ADP-ribose] polymerase 2-like
, ADP-ribosyltransferase diphtheria toxin-like 2
, NAD(+) ADP-ribosyltransferase 2
, poly (ADP-ribosyl) transferase-like 2
, poly(ADP-ribose) synthetase
, poly[ADP-ribose] synthase 2
, poly[ADP-ribose] synthetase 2
, ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase) 2