Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher tous les synonymes
Sélectionnez vos espèces d'intérêt
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 (Montrer RAD51 Protéines). Whereas PARP2 is dispensable for tolerance of cells to single stranded breaks or homologous recombination dysfunction, it is redundant with PARP1 (Montrer PARP1 Protéines) in BER.
PARP2 specifically limits the accumulation of the resection barrier factor 53BP1 (Montrer TP53BP1 Protéines) at DNA damage sites, allowing efficient CtIP (Montrer RBBP8 Protéines)-dependent DNA end-resection
either PARP1 (Montrer PARP1 Protéines) or PARP2 are sufficient for near-normal XRCC1 (Montrer XRCC1 Protéines) 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 (Montrer MLXIP Protéines)-149 expression are involved in the pathogenesis of hepatocellular carcinomas (HCC (Montrer FAM126A Protéines)) and are poor prognosis factors in patients with HCC (Montrer FAM126A Protéines).
Data show that E7449 represents a dual Poly(ADP-ribose) Polymerase 1 (Montrer PARP1 Protéines)/2 and tankyrase 1 (Montrer TNKS Protéines)/2 inhibitor which has the advantage of targeting Wnt (Montrer WNT2 Protéines)/beta-catenin (Montrer CTNNB1 Protéines) signaling addicted tumors.
The initial affinity between the PARP1 (Montrer PARP1 Protéines), 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 (Montrer PARP1 Protéines) 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 (Montrer PARP1 Protéines), the other major DDR (Montrer DDR1 Protéines)-PARP, and highlights the specialization of the multi-domain architectures of DDR (Montrer DDR1 Protéines)-PARPs.
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 (Montrer PARP1 Protéines) or -2 is likely to play a role in muscle protein catabolism via oxidative stress, NF-kappaB (Montrer NFKB1 Protéines) signaling, and enhanced proteasomal degradation in cancer-induced cachexia.
PARP1 (Montrer PARP1 Protéines)/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 (Montrer PARP1 Protéines) and PARP2 at H2AX (Montrer H2AFX Protéines)-deficient chromatin during replicative phases of the cell cycle and uncover a unique requirement for PARP1 (Montrer PARP1 Protéines) in nonhomologous end-joining-deficient cells.
Data show reduced tumor burden through increased oxidative stress in lung adenocarcinoma cells of PARP-1 (Montrer PARP1 Protéines) and PARP-2 knockout mice.
PARP-2 has an essential role in erythropoiesis by limiting replicative stress in erythroid progenitors.
PARP-1 (Montrer PARP1 Protéines) and -2 play a role in cancer-induced cachexia, thus selective pharmacological inhibition of PARP-1 (Montrer PARP1 Protéines) and -2 may be of interest in clinical settings
the depletion of PARP-2 leads to lower HDL (Montrer HSD11B1 Protéines) 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
We found that larger deletions of >20 bp predominated after DSB repair in ku80 (Montrer XRCC5 Protéines) and ku80 (Montrer XRCC5 Protéines) parp1 parp2 mutants, corroborating with a role of KU in preventing DSB end resection. Deletion lengths did not significantly differ between ku80 (Montrer XRCC5 Protéines) and ku80 (Montrer XRCC5 Protéines) parp1 parp2 mutants, suggesting that a KU- and PARP (Montrer PARP1 Protéines)-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 (Montrer PARP1 Protéines) were localized to the nucleus they are also present in non-nuclear locations with parp1 and parp3 (Montrer PARP3 Protéines) 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 (Montrer ROS1 Protéines)).
Poly(ADP-ribose)polymerase (Montrer PARP1 Protéines) activity controls plant growth by promoting leaf cell number.
Evidence suggests a link between the glutathione pool and PARP (Montrer PARP1 Protéines) 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