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1 trations required to maximally activate auto-poly(ADP-ribosylation).
2 CTCF participate in DNA damage response via poly(ADP-ribosylation).
3 ng to the lesions where it catalyses protein poly(ADP-ribosylation).
4 e stress in IDH-mutant cells is dependent on poly-(ADP-ribosylation).
5 tes the crosstalk between ubiquitination and poly-ADP-ribosylation.
6 e role in the cell or is just a byproduct of poly-ADP-ribosylation.
7 This modification can occur as mono- or poly-ADP-ribosylation.
8 ver, histone phosphorylation is modulated by poly(ADP-)ribosylation.
10 P-ribose may not be unique to PARPs and that poly(ADP-ribosylation), an established nuclear activity,
11 erent domains that interpret either mono- or poly-ADP-ribosylation and the implications for cellular
13 NAD(+) is a substrate for PARP-enzymes (mono/poly-ADP-ribosylation) and sirtuins (deacetylation).
14 increase in GAPDH activity, decreased GAPDH poly-ADP-ribosylation, and nuclear translocation of GAPD
15 These data implicate intra-mitochondrial poly(ADP-ribosylation) as an important therapeutic targe
17 tion, HPF1-deficient cells maintained robust poly-ADP-ribosylation at SSB sites, possibly reflecting
18 ar concentrations of ATP inhibit PARP-1 auto(poly-ADP-ribosylation) but less so the transfer of oligo
25 regulated kinase (ERK) signaling, Parp1 auto-poly ADP-ribosylation enhances Sox2-Parp1 interactions,
27 nction of the DLK regeneration pathway, that poly-(ADP ribosylation) inhibits axon regeneration acros
30 While the overall impact of PARP1-dependent poly-ADP-ribosylation is heavily investigated, very litt
32 n) was at least 100-fold lower than in trans-poly(ADP-ribosylation) (K(a) = 1400 versus 3-15, respect
35 catalyze post-translational modification by poly-ADP-ribosylation of a plethora of target proteins.
37 ed for the regulation of mtDNA integrity via poly-ADP-ribosylation of mtLIG3, the rate-limiting enzym
38 function, stimulating NAD(+)-dependent auto-poly-ADP-ribosylation of poly(ADP-ribose) polymerase 1 (
40 merase (PARP) activity and posttranslational poly-ADP-ribosylation of several regulatory proteins inv
42 is reduced shortly after viral infection via poly-ADP-ribosylation of the RNA-induced silencing compl
46 ed SSB level, gamma-H2AX foci formation, and poly(ADP-ribosylation) of PARP-1, which were associated
47 (mono-ADP-ribosylation) or polymeric chains (poly-ADP-ribosylation) of ADP-ribose are conjugated to p
48 ansfer to histone H(1) is 1% of that of auto(poly-ADP-ribosylation) of PARP-1, and this trans(ADP-rib
49 und that MDM2-deficient cells have increased poly-ADP-ribosylation on chromatin which supports the po
50 ose from NAD to histone H1 (defined as trans-poly(ADP-ribosylation)) or to PARP I (defined as auto-po
51 ns of oxidative stress and energy depletion, poly(ADP-ribosylation) paradoxically contributes to mito
54 ys a crucial role to regulate PARP1-mediated poly ADP-ribosylation (PARylation) and the choice of DSB
55 polymerases (PARPs) catalyze massive protein poly ADP-ribosylation (PARylation) within seconds after
58 RTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well d
60 ed on the basis of their ability to catalyze poly-ADP-ribosylation (PARylation) or mono-ADP-ribosylat
62 id not alter in vitro PARP1 enzyme activity, poly-ADP-ribosylation (PARylation), nor did inhibition o
65 y(ADP-ribose) polymerase 1 (Parp1) catalyzes poly(ADP-ribosylation) (PARylation) and induces replicat
66 ntial role in the PARP1- and PARP2-dependent poly-(ADP-ribosylation) (PARylation) of histones, by for
67 abase chromatin domains surrounding DSBs via poly-ADP-ribosylation, phosphorylation, acetylation, and
70 ribosylation)] or to PARP-1 [defined as auto(poly-ADP-ribosylation)] requires binding of coenzymic DN
72 for PARP I and catalyze preferentially trans-poly(ADP- ribosylation), thereby opening the possibility
75 of PARP I toward dcDNA or dsDNA in the auto-poly(ADP-ribosylation) was at least 100-fold lower than
76 ribosylation)) or to PARP I (defined as auto-poly(ADP-ribosylation)) was studied with respect to the
78 cts of H2O2 can be overcome by inhibitors of poly(ADP)-ribosylation, which also preserve cellular ATP