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1 CTCF participate in DNA damage response via poly(ADP-ribosylation).
2 trations required to maximally activate auto-poly(ADP-ribosylation).
3 tes the crosstalk between ubiquitination and poly-ADP-ribosylation.
4 This modification can occur as mono- or poly-ADP-ribosylation.
5 ver, histone phosphorylation is modulated by poly(ADP-)ribosylation.
7 P-ribose may not be unique to PARPs and that poly(ADP-ribosylation), an established nuclear activity,
8 erent domains that interpret either mono- or poly-ADP-ribosylation and the implications for cellular
10 increase in GAPDH activity, decreased GAPDH poly-ADP-ribosylation, and nuclear translocation of GAPD
11 These data implicate intra-mitochondrial poly(ADP-ribosylation) as an important therapeutic targe
12 ar concentrations of ATP inhibit PARP-1 auto(poly-ADP-ribosylation) but less so the transfer of oligo
18 regulated kinase (ERK) signaling, Parp1 auto-poly ADP-ribosylation enhances Sox2-Parp1 interactions,
19 nction of the DLK regeneration pathway, that poly-(ADP ribosylation) inhibits axon regeneration acros
22 n) was at least 100-fold lower than in trans-poly(ADP-ribosylation) (K(a) = 1400 versus 3-15, respect
25 function, stimulating NAD(+)-dependent auto-poly-ADP-ribosylation of poly(ADP-ribose) polymerase 1 (
26 merase (PARP) activity and posttranslational poly-ADP-ribosylation of several regulatory proteins inv
28 is reduced shortly after viral infection via poly-ADP-ribosylation of the RNA-induced silencing compl
31 ed SSB level, gamma-H2AX foci formation, and poly(ADP-ribosylation) of PARP-1, which were associated
32 (mono-ADP-ribosylation) or polymeric chains (poly-ADP-ribosylation) of ADP-ribose are conjugated to p
33 ansfer to histone H(1) is 1% of that of auto(poly-ADP-ribosylation) of PARP-1, and this trans(ADP-rib
34 ose from NAD to histone H1 (defined as trans-poly(ADP-ribosylation)) or to PARP I (defined as auto-po
35 ns of oxidative stress and energy depletion, poly(ADP-ribosylation) paradoxically contributes to mito
37 polymerases (PARPs) catalyze massive protein poly ADP-ribosylation (PARylation) within seconds after
38 RTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well d
41 id not alter in vitro PARP1 enzyme activity, poly-ADP-ribosylation (PARylation), nor did inhibition o
42 y(ADP-ribose) polymerase 1 (Parp1) catalyzes poly(ADP-ribosylation) (PARylation) and induces replicat
43 abase chromatin domains surrounding DSBs via poly-ADP-ribosylation, phosphorylation, acetylation, and
46 ribosylation)] or to PARP-1 [defined as auto(poly-ADP-ribosylation)] requires binding of coenzymic DN
48 for PARP I and catalyze preferentially trans-poly(ADP- ribosylation), thereby opening the possibility
51 of PARP I toward dcDNA or dsDNA in the auto-poly(ADP-ribosylation) was at least 100-fold lower than
52 ribosylation)) or to PARP I (defined as auto-poly(ADP-ribosylation)) was studied with respect to the
54 cts of H2O2 can be overcome by inhibitors of poly(ADP)-ribosylation, which also preserve cellular ATP
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