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1 ono- or poly-ADP-ribosylation (MARylation or PARylation).
2 gative regulation by poly(ADP-ribosyl)ation (PARylation).
3 th or without PARP-1 poly(ADP-ribosyl)ation (PARylation).
4 thway orchestrated by poly-ADP-ribosylation (PARylation).
5 tween SERBP1 and PARP1/polyADP-ribosylation (PARylation).
6  and target proteins with ADP-ribose (termed PARylation).
7 articular for protein poly-ADP-ribosylation (PARylation).
8 s, loss of HMGN1 protein reduces PARP-1 self-PARylation.
9 structural features that control binding and PARylation.
10 zation and labeling of mitochondrial protein PARylation.
11 P1 and its associated factors and influences PARylation.
12 ides an important tool for studying cellular PARylation.
13 te parameters influence TNKS interaction and PARylation.
14 rf4 attenuates virus- and DNA damage-induced parylation.
15 te by posttranslationally modulating protein PARylation.
16 hways to block histone polyADP-ribosylation (PARylation), a known effect of chemotherapy.
17 ells retain significant ADP-ribosylation and PARylation activities but accumulate markedly higher lev
18            Notably, the endogenous Parp1 and PARylation activity was enhanced by overexpression of c-
19 spectrometry and Western blotting, Parp1 and PARylation activity were intensively detected in induced
20 in to poly(ADP-ribose) and stimulates the de-PARylation activity.
21 alization of RECQL5 and WRN, suggesting that PARylation acts as a fine-tuning mechanism to coordinate
22 9 muM), as well as inhibiting PARP-modulated PARylation and cell proliferation in MDA-MB-436 cells (B
23         Preventing BER initiation suppresses PARylation and confers resistance to the synergistic eff
24  genetic inhibition of PARP-1 abrogates this PARylation and enhances extrinsic apoptosis, NF-kB signa
25 vels abrogates cGAMP-mediated suppression of PARylation and HDR.
26 rovides clear evidence of cross-talk between PARylation and histone methylation and offers new direct
27 his trapping of PARP2 is independent of auto-PARylation and is abolished by the R140A mutation in the
28  plant immunity is coordinately regulated by PARylation and K63-linked ubiquitination.
29                         Thus, both substrate PARylation and PARdU are catalysed by enzymes within the
30 umption, because cisplatin increased protein PARylation and PARP1 shRNA knock-down returned PRPP towa
31 ith a strand break, and this results in self-PARylation and PARylation of other chromatin proteins.
32 DSBs through a mechanism requiring chromatin PARylation and promotes epigenetic alterations that favo
33                 In addition, we observed AKT PARylation and prosurvival AKT-mTOR signaling in UWB+B c
34 ncy) phenotype, leading to increased histone parylation and reduced H3K9 acetylation, resulting in tr
35 atility and the functional interplay between PARylation and RNA binding.
36 amage elevates PARP1 activity, driving HMGB1 PARylation and subsequent translocation, thus impairing
37  SPINDOC in the regulation of PARP1-mediated PARylation and the DNA damage response.
38 C1 have been hindered by the requirement for PARylation and the highly heterogeneous nature of this p
39        The KO mice display reduced levels of PARylation and, like PARP1 KO mice, are hypersensitive t
40  1 (Parp1) catalyzes poly(ADP-ribosylation) (PARylation) and induces replication networks involved in
41 vented mitochondrial poly(ADP-ribosyl)ation (PARylation) and ROS formation.
42 gulate PARP1-mediated poly ADP-ribosylation (PARylation) and the choice of DSB repair pathways at sit
43  increase in protein poly(ADP-ribosyl)ation (PARylation), and was blocked by pharmacological inhibiti
44     In SPINDOC knockout cells, the levels of PARylation are reduced, in both the absence and presence
45  (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described, the enzymes i
46                                In a cellular PARylation assay, this compound inhibits PARP activity w
47 e) (PAR) polymerase 1 (PARP1) activation and PARylation at DNA damage sites, PAR-dependent recruitmen
48                   These data illustrate that PARylation at DSBs promotes NHEJ through recruitment or
49 ntrast, although Adprt1b was dispensable for PARylation at DSBs, Adprt1a and, to a lesser extent, Adp
50 er low energy laser-induced DNA damage, less PARylation at lesion sites was observed in Hmgn1(-/-) th
51 lly, CARM1 interacts with PARP1 and promotes PARylation at replication forks.
52 ylation of the DPCs in association with FEN1 PARylation at residue E285 is required for the recruitme
53 lation (PARylation) at genomic damage sites, PARylation at telomeres is mainly dependent on tankyrase
54                                              PARylation at these sites inhibits C/EBPbeta's DNA bindi
55 unlike PARP1-mediated Poly-ADP-Ribosylation (PARylation) at genomic damage sites, PARylation at telom
56 binds PARP1 and regulates the ubiquitination-PARylation balance of PARP1, which facilitates timely re
57 TOP1) in live cells, we found that sustained PARylation blocked the repair of TOP1 DNA-protein crossl
58 ence of m5C, R-loops activate PARP1-mediated PARylation both in vitro and in cells.
59 n of Parp1 and pharmacological inhibition of PARylation both reduced the efficiency of iPSC generatio
60 perties lead to enhanced labeling of protein PARylation by 3'-azido NAD(+) in the cellular contexts a
61 tic investigations indicated that inhibiting PARylation by either hyperthermia or PARPi induced letha
62                   Poly(ADP-ribose)ylation or PARylation by PAR polymerase 1 (PARP1) and dePARylation
63 alytic base Glu284 to substantially redirect PARylation by PARP1 such that the histones in nucleosome
64                     Poly(ADP-ribose)ylation (PARylation) by PAR polymerase 1 (PARP1) and PARylation r
65 ly adenosine diphosphate (ADP)-ribosylation (PARylation) by poly ADP-ribose (PAR) polymerases (PARPs)
66     Our results provide direct evidence that PARylation can control processing of mRNA precursors, an
67               Recent studies have shown that PARylation can serve as a signal for the polyubiquitinat
68 ed high activity and specificity for protein PARylation catalyzed by human poly-ADP-ribose polymerase
69                      Poly(ADP-ribosyl)ation (PARylation), catalyzed by poly(ADP-ribose) polymerases (
70                         PARP1-H862D, but not PARylation-deficient PARP1-E988K, formed stable PARP1 fo
71 s Poltheta to the vicinity of DNA damage via PARylation dependent liquid demixing, however, PARylated
72 tment induced the trapping of both PARP1 and PARylation-dependent DNA repair factors.
73                          In sum, we identify PARylation-dependent necroptosis in tumour ECs as an imp
74                                         This PARylation-dependent structural function of PARP2 at 5'p
75 146 (also known as Iduna) is responsible for PARylation-dependent ubiquitination (PARdU).
76                   We identified RNF114, as a PARylation-dependent, E3 ubiquitin ligase involved in DN
77                 The efficiency of XPC-RAD23B PARylation depends on DNA structure and increases after
78 ates both Drosophila Axin and APC2, but that PARylation does not globally regulate APC2 protein level
79 plored the model that disruption in cellular PARylation, driven by LMP1 expression, subsequently prom
80 provide a clear example of how site-specific PARylation drives biological outcomes.
81 we detail the mechanisms that drive cellular PARylation during latent EBV infection and the effects o
82                              We propose that PARylation enables HIRA to fulfill its essential role in
83                                              PARylation enhanced the impact of PARP1 depletion.
84                                         TDP1 PARylation enhances its recruitment to DNA damage sites
85                    However, the way in which PARylation facilitates these functions remains unclear,
86                            Recently, Histone PARylation Factor (HPF1) was shown to be a critical modu
87 or key regulators of PARP1 activity, histone PARylation factor 1 (HPF1) and ADP-ribosylhydrolase 3 (A
88                            Recently, histone PARylation Factor 1 (HPF1) has been shown to play an ess
89 iglio et al. (2017) demonstrate that histone PARylation factor 1 (HPF1) is required for PARP1 to atta
90       In response to DNA damage, the histone PARylation factor 1 (HPF1) regulates PARP1/2 activity, f
91 serine ADPr is strictly dependent on histone PARylation factor 1 (HPF1), a recently identified regula
92 f the paradigm-shifting discovery of histone PARylation factor 1 (HPF1), the protein that facilitates
93      We report the identification of histone PARylation factor 1 (HPF1; also known as C4orf27) as a r
94               Our data indicate that histone PARylation factor 1 arrives at sites of DNA damage indep
95                                HPF1 (Histone PARylation Factor 1), a gene crucial in the base excisio
96 f the PARP1/2 active site component, histone PARylation factor 1, on intracellular PARPi binding and
97 se polymerases 1 and 2 (PARP1/2) and histone PARylation factor 1.
98  biology, physiology, and pathophysiology of PARylation, focusing on the activity of PARP-1, the most
99 so suggests the potential regulatory role of PARylation for the repair of a broad range of DPCs.
100                                     Although PARylation has been studied extensively, few examples of
101              Protein poly(ADP-ribosyl)ation (PARylation) has a role in diverse cellular processes suc
102 efinitive biological roles for site-specific PARylation have been reported.
103                                              PARylation impacted the production of nascent mRNA and t
104                    It inhibits PARP-mediated PARylation in a whole-cell assay with an EC50 of 2.51 nM
105 for further in-depth analysis of the role of PARylation in a wide range of biological contexts.
106 ge response localized to telomeres, inhibits PARylation in cells, and has an antiproliferative effect
107                                 We find high PARylation in lamin A/C-aberrant cells, further decreasi
108     This review first introduces the role of PARylation in regulating biomolecular condensates, follo
109 elium discoideum to uncover a novel role for PARylation in regulating nonhomologous end joining (NHEJ
110 e first direct comparative role of PARP1 and PARylation in RNA stability and decay, adding a new dime
111 ings establish the involvement of PARP-1 and PARylation in the long-term actions of cocaine.
112                                              PARylation in vitro inhibits ORC2 recruitment and remode
113 le of PARP1-mediated poly(ADP-ribosyl)ation (PARylation) in regulating HMGB1 nuclear export was also
114 cover a new role for poly(ADP-ribosyl)ation (PARylation) in regulating the chromatin-assembly factor
115  and modifies PAP by poly(ADP-ribosyl)ation (PARylation) in vitro, which inhibits PAP activity.
116 ough the inhibition of polyADP-ribosylation (PARylation), in which cGAMP reduces cellular levels of N
117  the fundamental parameters of intracellular PARylation, including the sites that are conjugated, PAR
118  treatment led to persistence of detrimental PARylation, increased expression of cleaved caspase-3, a
119 AF(V600E)-induced senescence phenotypes in a PARylation-independent manner.
120 s with excellent PARP enzymatic and cellular PARylation inhibition activities.
121 venting demethylation of H3K4me3 through the PARylation, inhibition, and exclusion of the histone dem
122                       Conversely, persistent PARylation is highly toxic and has distinct physiologica
123                   These results suggest that PARylation is important for myofibroblast differentiatio
124                                 We show that PARylation is involved in the recruitment of RECQL5 and
125                      Poly(ADP-ribosyl)ation (PARylation) is a post-translational modification mediate
126                      Poly(ADP-ribosyl)ation (PARylation) is a post-translational modification of prot
127                      Poly(ADP-ribosyl)ation (PARylation) is a post-translational protein modification
128                      Poly(ADP-ribosyl)ation (PARylation) is a posttranslational modification catalyze
129                      Poly(ADP-ribosyl)ation (PARylation) is a posttranslational modification reversib
130                      Poly(ADP) ribosylation (PARylation) is important for subsequent chromatin decomp
131                      Poly(ADP-ribosyl)ation (PARylation) is mainly catalysed by poly-ADP-ribose polym
132                           Tankyrase-mediated PARylation marks protein targets for proteasomal degrada
133 se and other recent findings suggesting that PARylation may be the critical event that mediates the f
134 he decrease in PARG levels enhances the auto-PARylation-mediated inhibition of PARP, thereby avoiding
135 corresponding to a release of C/EBPbeta from PARylation-mediated inhibition.
136 ic cosolutes, we examine how acetylation and PARylation modulate histone tail electrostatic potential
137 luences PARP1 function and PARylation, while PARylation modulates SERBP1 functions and participation
138 ARP1 enzyme activity, poly-ADP-ribosylation (PARylation), nor did inhibition of SUMOylation of PARP1
139 ss of mitochondrial transmembrane potential, parylation, nuclear translocation of apoptosis-inducing
140 nhibition and the D226 mutation impair HuR's PARylation, nucleocytoplasmic shuttling and mRNA binding
141 biochemical studies that recapitulated Pol y PARylation observed in cells and showed that PARP1 regul
142                                              PARylation occurred at single-strand breaks, and two PAR
143                                              PARylation occurs at or near the sites of DNA damage and
144 RIG-I) and activates PARP-1, with consequent PARylation of components of the extrinsic apoptosis path
145              We propose that PARP1-dependent PARylation of EBNA1 and adjacently bound TRF2 induces st
146                                              PARylation of EZH2 by PARP1 then induces PRC2 complex di
147 tor of the activity of PARP1 by facilitating PARylation of histones and redirecting the target amino
148 h poly-(ADP ribose) polymerase 1 (PARP1) and PARylation of histones have been known for over 50 years
149              Mechanistically, PARP1-mediated PARylation of HMGB1 was essential for its interaction wi
150                                 Furthermore, PARylation of NSD2 inhibits its ability to bind to nucle
151 eak, and this results in self-PARylation and PARylation of other chromatin proteins.
152                               Moreover, auto-PARylation of PARP1 allowed the protein to switch its da
153                             PARG-mediated de-PARylation of Poltheta reactivates its DNA binding and e
154                                              PARylation of Poltheta-h by PARP-1 resolves these DNA br
155                     Global acetylation, auto-PARylation of poly ADP-ribose polymerase 1 (PARP1), acet
156    Purified HMGN1 was able to stimulate self-PARylation of purified PARP-1, and in experiments with c
157                                              PARylation of the DPCs in association with FEN1 PARylati
158 ating the otherwise transient and reversible PARylation of the DPCs.
159                                              PARylation of TOP1-DPC was readily revealed by inhibitin
160 ith TRF1, which subsequently facilitates the PARylation of TRF1 after damage.
161 cilitating SSBR at damaged telomeres through PARylation of TRF1, thereby protecting genome stability
162                               Significantly, PARylation of UBC13 regulates K63-linked ubiquitination
163 ity promotes these interactions and enhances PARylation of UBC13.
164 and PARP2-dependent poly-(ADP-ribosylation) (PARylation) of histones, by forming a complex with both
165 fects the self-poly(ADP-ribosyl)ation (i.e., PARylation) of poly(ADP-ribose) polymerase-1 (PARP-1), a
166 PARP1) catalyzes the poly(ADP-ribosyl)ation (PARylation) of proteins, a posttranslational modificatio
167  sensor that directs poly(ADP-ribosyl)ation (PARylation) of proteins.
168 ring latent EBV infection and the effects of PARylation on host gene expression and cellular function
169 oss of SUMOylation increased PARP1-dependent PARylation on isolated chromosomes, indicating SUMOylati
170     We tested the direct impact of PARP1 and PARylation on mRNA stability and decay.
171 ast differentiation, we examined the role of PARylation on myofibroblast differentiation.
172 DPCs, we investigated the impact of TOP1-DPC PARylation on the proteasome and found that the proteaso
173 r ability to catalyze poly-ADP-ribosylation (PARylation) or mono-ADP-ribosylation (MARylation).
174 yers in the early DNA damage response, since PARylation orchestrates the recruitment of repair protei
175 tic potential of modulating PAR conjugation (PARylation): PAR polymerase (PARP) inhibitors can modula
176       PARP1-dependent poly-ADP-ribosylation (PARylation) participates in the repair of many forms of
177                      Poly(ADP-ribosyl)ation (PARylation) plays diverse roles in many molecular and ce
178 vl1)/human antigen R (HuR), resulting in its PARylation, primarily at site D226.
179                                 In addition, PARylation recruits the deubiquitylating enzyme USP7 to
180  summary, we demonstrate that NUDT16 and its PARylation regulate CtIP stability and CtIP recruitment
181 difications, such as poly(ADP-ribosyl)ation (PARylation), regulate chromatin-modifying enzymes, ultim
182            The molecular mechanisms by which PARylation regulates innate immunity remain largely unkn
183                      Poly(ADP)-ribosylation (PARylation) regulates chromatin structure and recruits D
184 (PARylation) by PAR polymerase 1 (PARP1) and PARylation removal by poly(ADP-ribose) glycohydrolase (P
185 e) (PAR) chain removal (de-MARylation and de-PARylation, respectively) from mono- and poly(ADP)-ribos
186                  In vitro assays suggest the PARylation significantly reduces NSD2 histone methyltran
187 cal inhibition of PARP-1, or mutation of the PARylation sites on C/EBPbeta, enhances these early adip
188                                              PARylation stabilizes TDP1 together with SUMOylation of
189 r from stress-induced pathogenic increase in PARylation that can be mitigated by PARP inhibition.
190 ter ultraviolet irradiation, involving GSDME PARylation that releases autoinhibition and lipid reacti
191 d in vitro to clarify the exact pathway from PARylation to condensate formation.
192 n their formation, generate a burst of local PARylation to signal their location, and are co-targeted
193 s, a condition that fuels DNA damage-induced PARylation under oxidative stress.
194 We demonstrate that PARP1 regulates NSD2 via PARylation upon oxidative stress.
195 m and specific consequences of HPF1-mediated PARylation using nucleosomes as both activators and subs
196  and in experiments with cell extracts, self-PARylation was greater in Hmgn1(+/+) than in Hmgn1(-/-)
197 n which SERBP1 influences PARP1 function and PARylation, while PARylation modulates SERBP1 functions
198 alyze massive protein poly ADP-ribosylation (PARylation) within seconds after the induction of DNA si

 
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