ライフサイエンスコーパス: ADP-ribosylation

1 participate in DNA damage response via poly(ADP-ribosylation).

2 k repair but also elevated levels of protein ADP-ribosylation.

3 This modification can occur as mono- or poly-ADP-ribosylation.

4 h effects were independent of DNA damage and ADP-ribosylation.

5 ability to hydrolyze PARP-dependent protein ADP-ribosylation.

6 the two major enzymes that control cellular ADP-ribosylation.

7 inhibit Src kinase-dependent phagocytosis by ADP-ribosylation.

8 ner by a nucleotide-type modification called ADP-ribosylation.

9 f poly(ADP-ribosyl) transferases (PARPs) and ADP-ribosylation.

10 of enzymes capable of modifying proteins by ADP-ribosylation.

11 NA repair, but much less is known about mono-ADP-ribosylation.

12 ish a crosstalk between lipoylation and mono-ADP-ribosylation.

13 of the many cellular processes regulated by ADP-ribosylation.

14 d on post-translational modification by mono-ADP-ribosylation.

15 t TCDD-induced TiPARP also targets PEPCK for ADP-ribosylation.

16 reviously unidentified modulatory effects on ADP-ribosylation.

17 he crosstalk between ubiquitination and poly-ADP-ribosylation.

18 ondrial forms of PEPCK were found to undergo ADP-ribosylation.

19 acetylation, ubiquitination, AMPylation, and ADP-ribosylation.

20 ce junction and the mechanism of RNA phospho-ADP-ribosylation.

21 opF that inhibits bacterial clearance by its ADP-ribosylation.

22 ify RNA as a novel target of reversible mono-ADP-ribosylation.

23 lts from PARP1-independent excessive protein ADP-ribosylations.

24 hydrolase activity was required for 53BP1 de-ADP-ribosylation, 53BP1 protein stability, and its funct

25 phosphate-ribose polymerases (PARPs) promote ADP-ribosylation, a highly conserved, fundamental posttr

26 k on PARPs-a family of enzymes that catalyze ADP-ribosylation, a posttranslational modification of pr

27 nd ARH3) are a family of enzymes to catalyze ADP-ribosylation, a reversible and covalent post-transla

28 improves the overall localization scores for ADP-ribosylation acceptor sites but also boosts ADP-ribo

29 To appreciate the diverse roles of ADP-ribosylation across the proteome, we have created AD

30 ETA has ADP-ribosylation activity and decisively affects the pro

31 f function mutants to reveal that SIRT6 mono-ADP-ribosylation activity is required for transcriptiona

32 The ADP-ribosylation activity of AvrRpm1 is required for sub

33 Parp9 ADP-ribosylation activity therefore restrains the E3 fun

34 anner, but independently of PARP-1 catalytic ADP-ribosylation activity.

35 asses, these sirtuins exhibit robust protein ADP-ribosylation activity.

36 dJ-mediated polyglutamylation suppresses the ADP-ribosylation activity.

37 ADP-ribosylation (ADPr) is a posttranslational modificat

38 ADP-ribosylation (ADPr) regulates important patho-physio

39 ADP-ribosylation (ADPRylation) is a posttranslational mo

40 protein, leading to inhibition of PARP1 auto-ADP-ribosylation and defective repair of oxidative lesio

41 ate a functional interplay between H2B-Glu35 ADP-ribosylation and H2B-Ser36 phosphorylation that cont

42 th an additional methyl group that prevented ADP-ribosylation and inactivation of EF2.

43 HPF1 functions at the crossroads of histone ADP-ribosylation and PARP-1 automodification.

44 They combine mono-ADP-ribosylation and phosphodiesterase activities to att

45 In vitro ADP-ribosylation and protein translation assays demonstr

46 for both amino-acid starvation induced mono-ADP-ribosylation and subsequent Sec body formation and c

47 ies of the different enzymes associated with ADP-ribosylation and the consequences of this PTM on sub

48 domains that interpret either mono- or poly-ADP-ribosylation and the implications for cellular proce

49 r than the IC50 were required to ablate both ADP-ribosylation and XRCC1 chromatin binding following H

50 ) is a substrate for PARP-enzymes (mono/poly-ADP-ribosylation) and sirtuins (deacetylation).

51 in lysine deacetylation, adenosinediphospho(ADP)-ribosylation, and/or deacylation.

52 ular signaling effects of NAD(+) mediated by ADP-ribosylation, and epigenetic effects of intracellula

53 ding a clear functional link between PARP-1, ADP-ribosylation, and NELF.

54 ease in GAPDH activity, decreased GAPDH poly-ADP-ribosylation, and nuclear translocation of GAPDH.

55 inding to poly (ADP-ribose) at low levels of ADP-ribosylation, and promotes interaction with cellular

56 vides insights into the functions of protein ADP-ribosylation, and suggests activating TiPARP as an a

57 results provide an example of reversible DNA ADP-ribosylation, and we anticipate potential therapeuti

58 nd implications of this unexpected, O-linked ADP-ribosylation are speculated on.

59 We also failed to identify a role of PI31 ADP-ribosylation as a mechanism for regulation of overal

60 Here we report ADP-ribosylation as a new post-translational modificatio

61 This report 1) identifies ADP-ribosylation as a new posttranslational modification

62 roaches as well as a deeper understanding of ADP-ribosylation as a whole.

63 We also developed a drug-dependent ADP-ribosylation assay in primary cells that correlated

64 Radio-ADP-ribosylation assays reveal that shedding refocuses t

65 tro, although disruption of this site allows ADP-ribosylation at H2BE19.

66 ly advanced our knowledge of the function of ADP-ribosylation at the molecular level.

67 ientists and clinicians to better understand ADP-ribosylation at the molecular level.

68 acts as a negative regulator and suppresses ADP-ribosylation both in vitro and in vivo.

69 0, MacroD1, and MacroD2 proteins can reverse ADP-ribosylation by acting on ADP-ribosylated substrates

70 While ADP-ribosylation can be reversed by ADP-ribosylhydrolase

71 Poly-ADP-ribosylation, catalyzed by PARP1, is a post-translat

72 tudies performed with wild-type H2AX and the ADP-ribosylation-deficient E141A mutant suggest that H2A

73 nuclear condensates or nuclear bodies in an ADP ribosylation-dependent manner.

74 NADP(+) impairs ADP-ribosylation-dependent DNA damage repair and sensiti

75 Moreover, loss of this ADP-ribosylation enhances serine-139 phosphorylation of

76 tyostelium to identify site-specific histone ADP-ribosylation events in vivo and define the ARTs that

77 tone genes that can be manipulated to assess ADP-ribosylation events in vivo.

78 ADP ribosylation factor (Arf) 6 anchors to the plasma me

79 The ADP ribosylation factor (Arf) and the coat protein compl

80 ADP ribosylation factor (Arf) GTPases are key regulators

81 Here we focused on ADP ribosylation factor (Arf) GTPases, which orchestrate

82 TBC1D24 interacts with ADP ribosylation factor (ARF)6, a small GTPase crucial f

83 ily GTPase Arf79F, the Drosophila homolog of ADP ribosylation factor 1 (ARF1), essential for clathrin

84 of two subcomplexes: the membrane-targeting, ADP ribosylation factor 1 (Arf1):GTP-binding betagammade

85 erminal tail of PC1 functions as a CTS in an ADP ribosylation factor 4 (Arf4)/ArfGAP with SH3 domain,

86 ADP ribosylation factor 6 (Arf6) is a small GTPase known

87 rs of endosomal trafficking, including Arf6 (ADP ribosylation factor 6) GTPase activating proteins an

88 ARL13B is a member of the ADP ribosylation factor family of regulatory GTPases, bu

89 vealed that ALA3 functions together with the ADP ribosylation factor GTPase exchange factors GNOM and

90 omology protein, and MTV4, which encodes the ADP ribosylation factor GTPase-activating protein nevers

91 cytic and recycling pathways mediated by the ADP ribosylation factor guanine nucleotide exchange fact

92 Here, we show that Drosophila ADP ribosylation factor like-2 (Arl2) and Msps, a known

93 osomes back to the surface in a small GTPase ADP ribosylation factor-6 (Arf6)-dependent manner.

94 olgi-localized, gamma adaptin-ear-containing ADP ribosylation factor-binding protein 3 (GGA3) interac

95 ocalized, gamma-adaptin ear domain homology, ADP ribosylation factor-binding protein 3), a multidomai

96 ocalized, gamma-adaptin ear domain homology, ADP ribosylation factor-binding proteins (GGAs) mediate

97 ocalized, gamma-adaptin ear domain homology, ADP ribosylation factor-binding proteins 1 and 2 (GGA1 a

98 UNC50 acted by recruiting GBF1, an ADP ribosylation factor-guanine nucleotide exchange fact

99 Five conserved tubulin cofactors and ADP ribosylation factor-like 2 regulate the biogenesis a

100 The gene for ADP ribosylation factor-like GTPase 13B (Arl13b) encodes

101 ne nucleotide exchange factors (GEFs) on the ADP-ribosylation factor (ARF) family of small GTPases in

102 was dependent on both its RING E3 ligase and ADP-ribosylation factor (ARF) GTPase activity.

103 At least six ADP-ribosylation factor (Arf) GTPase-activating proteins

104 ctional membrane trafficking is regulated by ADP-ribosylation factor (ARF) GTPases and the developmen

105 Members of the ADP-ribosylation factor (ARF) small GTPase family regula

106 ADP-ribosylation factor (Arf)-like 4A (Arl4A), an Arf sm

107 ADP-ribosylation factor (Arf)-like 4D (Arl4D), one of th

108 results in the sequential recruitment of the ADP-ribosylation factor (Arf)-like protein Arl1; the Arf

109 tidomain GTPase-activating protein (GAP) for ADP-ribosylation factor (ARF)-type GTPases.

110 chitecture; facilitates secretion; activates ADP-ribosylation factor (ARF)1, 3, 4, and 5; and recruit

111 a specific interaction with the small GTPase ADP-ribosylation factor (ARF5) in its active, GTP-bound

112 caine causes dissociation of the Sig-1R from ADP-ribosylation factor (ARF6), a G-protein regulating E

113 Although we have showed that the GTPase ADP-ribosylation factor 1 (ARF1) is overexpressed in hig

114 e loss of the small guanosine triphosphatase ADP-ribosylation factor 1 (Arf1) or its effector, phosph

115 pecifically associated with the small GTPase ADP-ribosylation factor 1 (Arf1) to mediate uniform dist

116 the finiteness of the cyclical activation of ADP-ribosylation factor 1 (Arf1), a fundamental step in

117 We show that ADP-ribosylation factor 1 (ARF1), bridging integrator 1

118 and cell biological evidence for the role of ADP-ribosylation factor 1 (ARF1)-GTPase and its effector

119 g GTPase-independent mechanism that requires ADP-ribosylation factor 1 (Arf1).

120 In this study, we report that ADP-ribosylation factor 3p (Arf3p) acts as a regulator o

121 ssays to identify and validate two key nodes-ADP-ribosylation factor 4 (ARF4) and valosin-containing

122 pecifically examine the expression levels of ADP-ribosylation factor 6 (ARF6) and EPS8-like 2 (EPS8L2

123 ARs control the activity of the small GTPase ADP-ribosylation factor 6 (Arf6) by consecutively recrui

124 The ADP-ribosylation factor 6 (Arf6) is a small GTPase that

125 The ADP-ribosylation factor 6 (Arf6) isoform and the exchang

126 They modify ADP-ribosylation factor 6 (ARF6) on lysine 3 allowing it

127 The small G protein ADP-ribosylation factor 6 (Arf6) plays important roles i

128 ADP-ribosylation factor 6 (ARF6) small GTPase regulates

129 By using ADP-ribosylation factor 6 (ARF6) small interfering RNA,

130 ogic or genetic blockade of the small GTPase ADP-ribosylation factor 6 (arf6) that regulates integrin

131 The small GTPase ADP-ribosylation factor 6 (Arf6) was shown to regulate t

132 host plasma membrane and interacts with host ADP-ribosylation factor 6 (Arf6).

133 A1 recycling and degradation is regulated by ADP-ribosylation factor 6 (ARF6).

134 ARF6 (ADP-ribosylation factor 6) is a small GTPase implicated

135 n active state, which is further enhanced by ADP-ribosylation factor 6, a host cofactor for CTA1.

136 m toxin substrate 1, p21-activated kinase 1, ADP-ribosylation factor 6, and cell division control pro

137 copy to show that clathrin, dynamin, and the ADP-ribosylation factor 6, three components of the endoc

138 rane vesicles requires the activation of the ADP-ribosylation factor ARF GTPase by the SEC7 domain of

139 aptor localization: a step that requires the ADP-ribosylation factor ARF, an ATP-dependent step that

140 Arl13b belongs to the ADP-ribosylation factor family within the Ras superfamil

141 in the developing neuron, the protein ADAP1 (ADP-ribosylation factor GTPase-activating protein [ArfGA

142 g the Golgi membrane/cytosol partitioning of ADP-ribosylation factor proteins.

143 itates the activation of members of the ARF (ADP-ribosylation factor) family of small GTPases.

144 es via a distinct pathway mediated by ARF-6 (ADP-ribosylation factor-6).

145 calize to the plasma membrane, caveolae, and ADP-ribosylation factor-6+ (Arf6+) endocytic compartment

146 Human Golgi-localized, gamma-ear-containing, ADP-ribosylation factor-binding proteins (Ggas) bind dir

147 Cat-1) is a signaling scaffold as well as an ADP-ribosylation factor-GTPase-activating protein.

148 or the function of the brefeldin A-sensitive ADP-ribosylation factor-guanine exchange factors (ARF-GE

149 The small GTPase, ADP-ribosylation factor-like 3 (ARL3), has been proposed

150 The ADP-ribosylation factor-like 4C (Arl4C) small GTPase act

151 report the crucial role of the small GTPase ADP-ribosylation factor-like 8b (Arl8b) in MHC II presen

152 re, we identify a small GTP-binding protein, ADP-ribosylation factor-like 8b (Arl8b), as a critical f

153 Herein, we investigated the protein ADP-ribosylation factor-like GTPase 13b (ARL13b) as a mo

154 r protein complex, AP-4, and small G protein ADP-ribosylation factor-like GTPase 5b (Arl5b) are requi

155 tation impeded the interaction of PROM1 with ADP-ribosylation factor-like protein 13B, a key regulato

156 emerged from PtdIns(4)P-rich regions, where ADP-ribosylation factor-like protein 8B (ARL8B) and SifA

157 HLB1 was found to interact with the ADP-ribosylation-factor guanine nucleotide exchange fact

158 Small G-proteins of the ADP-ribosylation-factor-like (Arl) subfamily have been s

159 d BIG2 activate, through their Sec7 domains, ADP ribosylation factors (Arfs) by accelerating the repl

160 Host ADP-ribosylation factors (ARFs) act as in vitro alloster

161 factors 1 and 2 (BIG1 or BIG2) that activate ADP-ribosylation factors (Arfs) by accelerating the repl

162 ADP-ribosylation factors (ARFs) have been reported to fu

163 nucleotide exchange factors (GEFs) activate ADP-ribosylation factors (ARFs) to facilitate coating of

164 s as a guanine nucleotide exchange factor of ADP-ribosylation factors (Arfs), is critical for Rickett

165 his approach, we mapped hundreds of sites of ADP-ribosylation for PARPs 1, 2, and 3 across the proteo

166 Furthermore, dysregulation of ADP-ribosylation has been linked to diseases including c

167 ignals by the readers and erasers of protein ADP-ribosylation, has been significantly advanced by the

168 unidentified roles for Tiparp, MacroD1, and ADP-ribosylation in AHR-mediated steatohepatitis and let

169 evidence of the requirement for protein mono-ADP-ribosylation in Th cell differentiation.

170 tablish a novel example for the role of mono-ADP-ribosylation in the formation of stress assemblies,

171 aracterized by a specific increase in serine-ADP-ribosylation in vivo under untreated conditions as w

172 In order to visualise both Poly-, and Mono-, ADP-ribosylation in vivo, we engineered specific fluores

173 of the DLK regeneration pathway, that poly-(ADP ribosylation) inhibits axon regeneration across spec

174 Protein adenosine diphosphate (ADP)-ribosylation is a physiologically and pathologicall

175 Adenosine diphosphate (ADP)-ribosylation is a post-translational protein modifi

176 Protein ADP-ribosylation is a covalent posttranslational modific

177 PARP catalysed ADP-ribosylation is a post-translational modification in

178 ADP-ribosylation is a post-translational modification th

179 ADP-ribosylation is a post-translational modification th

180 ADP-ribosylation is a post-translational modification wh

181 ADP-ribosylation is a posttranslational modification tha

182 ADP-ribosylation is a posttranslational modification tha

183 ADP-ribosylation is a posttranslational protein modifica

184 ADP-ribosylation is a PTM, in which ADP-ribosyltransfera

185 ADP-ribosylation is a reversible chemical modification c

186 ADP-ribosylation is a unique posttranslational modificat

187 lthough redundancy between H2BE18 and H2BE19 ADP-ribosylation is also apparent following DSBs in vivo

188 Protein ADP-ribosylation is an ancient posttranslational modific

189 ADP-ribosylation is an intricate and versatile posttrans

190 ADP-ribosylation is governed by ADP-ribosyltransferases

191 ADP-ribosylation is integral to a diverse range of cellu

192 ADP-Ribosylation is reversed by hydrolases that cleave t

193 Though ADP-ribosylation is therapeutically important, investiga

194 rase, DarT(Mtb) ), to mediate reversible DNA ADP-ribosylation (Jankevicius et al., 2016).

195 of target proteins, leading to mono- or poly-ADP-ribosylation (MARylation or PARylation).

196 well described, the enzymes involved in mono-ADP-ribosylation (MARylation) have been less well invest

197 Mono-ADP-ribosylation (MARylation) of mammalian proteins was

198 Our data suggest that RNA ADP-ribosylation may represent a widespread and physiolo

199 ken together, these results reveal that H2AX ADP-ribosylation not only facilitates BER repair, but al

200 xin, the disease-causing agent that, through ADP ribosylation of diphthamide, causes irreversible ina

201 Loss of diphthamide prevented ADP ribosylation of eEF2, rendered cells resistant to PE

202 its Src kinase by simultaneous amidation and ADP ribosylation of the conserved kinase-domain residue,

203 n factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, dipht

204 NUDT16 has hydrolase activities that remove ADP-ribosylation of 53BP1 to regulate 53BP1 stability an

205 Ta-specific nanobodies blocked CDTa-mediated ADP-ribosylation of actin.

206 ADP-ribosylation of Axin enhances its interaction with t

207 We demonstrate that SIRT6 mono-ADP-ribosylation of BAF170, a subunit of BAF chromatin r

208 e fungal toxin brefeldin A (BFA) induces the ADP-ribosylation of C-terminal-binding protein-1 short-f

209 Auto-ADP-ribosylation of cholix toxin appears to have negativ

210 Here, we report that ADP-ribosylation of CtBP1-S/BARS by BFA occurs via a non

211 ADP-ribosylation of effector arginines likely uncouples

212 ividually but, in combination, catalyzed the ADP-ribosylation of eukaryotic elongation factor 2 and i

213 in III or PE3) inhibits protein synthesis by ADP-ribosylation of eukaryotic elongation factor 2.

214 ears to have negatively regulatory effect on ADP-ribosylation of exogenous substrate.

215 of both endogenous and exogenous substrates, ADP-ribosylation of exogenous substrates occurred more e

216 ha GTP-loading and pertussis toxin-catalyzed ADP-ribosylation of G(i)alpha, for which we synthesized

217 ctivity/intracellular localization, and poly-ADP-ribosylation of GAPDH.

218 ADP-ribosylation of Glu35 and the subsequent reduction o

219 We found that NAD(+)-dependent ADP-ribosylation of histone H2B-Glu35 by small nucleolar

220 lly, HPF1 promotes PARP-1-dependent in trans ADP-ribosylation of histones and limits DNA damage-induc

221 Although ADP-ribosylation of histones by PARP-1 has been linked t

222 timal DNA damage response is associated with ADP-ribosylation of histones.

223 6, including long-chain deacylation and mono-ADP-ribosylation of other proteins, have also been repor

224 TNKS-mediated ADP-ribosylation of PI31 drastically reduces its affinit

225 tion, stimulating NAD(+)-dependent auto-poly-ADP-ribosylation of poly(ADP-ribose) polymerase 1 (PARP1

226 various roles of PARPs and the regulation of ADP-ribosylation of protein substrates.

227 ADP-ribosylation of proteins is emerging as an important

228 mains, enzymes that remove posttranslational ADP-ribosylation of proteins, and viral multifunctional

229 ovides insight into a mechanism for how ExoS ADP-ribosylation of Rab5 inhibits Rab5 function.

230 & Microbe, Vareechon et al. (2017) describe ADP-ribosylation of Ras as a strategy to inhibit assembl

231 chanism for inhibition than observed for the ADP-ribosylation of Ras by ExoS, where ADP-ribosylated R

232 nnate immune response requires ExoS-mediated ADP-ribosylation of Ras in neutrophils.

233 Here, we show that AvrRpm1 induces ADP-ribosylation of RIN4 proteins from both Arabidopsis

234 We further reveal that ADP-ribosylation of RNA mediated by PARP10 and TRPT1 can

235 target specific transcripts for regulation; ADP-ribosylation of RNA-regulatory proteins can alter th

236 hydrolase (PARG), which dynamically regulate ADP-ribosylation of Smad3 and Smad4, two central signali

237 PARP14 induces ADP-ribosylation of STAT1, which is suppressed by PARP9.

238 proach for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subs

239 bit protein synthesis of mammalian cells via ADP-ribosylation of the eukaryotic elongation factor-2.

240 ADP-ribosylation of the small GTPase Rab5 has previously

241 PE kills by ADP-ribosylation of the translation elongation factor 2,

242 mally used for Ub conjugation to substrates, ADP-ribosylation of the Ub carboxyl terminus precludes u

243 We also found that tankyrase1-mediated poly-ADP-ribosylation of TRF1 is important for both the inter

244 SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify s

245 9 heterodimer mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin, exclusively in the contex

246 ADP-ribosylation of vinculin disrupted focal adhesion co

247 -ADP-ribosylation) or polymeric chains (poly-ADP-ribosylation) of ADP-ribose are conjugated to protei

248 Mechanistically, ADP-ribosylation on E141 mediates the recruitment of Nei

249 fy cysteine as a novel amino-acid target for ADP-ribosylation on PARPs.

250 the functional consequences of site-specific ADP-ribosylation on those substrates.

251 tional modification where single units (mono-ADP-ribosylation) or polymeric chains (poly-ADP-ribosyla

252 Here we report that both BRCA1 poly-ADP ribosylation (PARsylation) and the presence of BRCA1

253 Poly(ADP) ribosylation (PARylation) is important for subseque

254 PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well descri

255 Here, we found unlike PARP1-mediated Poly-ADP-Ribosylation (PARylation) at genomic damage sites, P

256 PARP1-dependent poly-ADP-ribosylation (PARylation) participates in the repair

257 erases (PARPs) catalyze massive protein poly ADP-ribosylation (PARylation) within seconds after the i

258 modification in particular for protein poly-ADP-ribosylation (PARylation).

259 -ribose) polymerase 1 (Parp1) catalyzes poly(ADP-ribosylation) (PARylation) and induces replication n

260 ion-deficient E141A mutant suggest that H2AX ADP-ribosylation plays a critical role in base excision

261 Here we report that mono-ADP-ribosylation plays an important role in homologous r

262 ADP-ribosylation plays an important role in several biol

263 mide adenine dinucleotide (NAD(+))-dependent ADP-ribosylation plays important roles in physiology and

264 ow that viral macro domains reverse cellular ADP-ribosylation, potentially cutting the signal of a vi

265 Here, we show that ADP-ribosylation promotes 26S proteasome activity in bot

266 n to controlling Axin levels, Tnks-dependent ADP-ribosylation promotes the reprogramming of Axin foll

267 summarizes the current knowledge of nuclear ADP-ribosylation reactions and their role in chromatin p

268 polymerase (PARP) family of enzymes and the ADP-ribosylation reactions that they catalyze.

269 with cysteine modifying S-nitrosylation and ADP-ribosylation reactions using a chemical nitric oxide

270 ADP-ribosylation refers to the addition of one or more A

271 ADP-ribosylation refers to the addition of one or more A

272 ADP-ribosylation refers to the transfer of the ADP-ribos

273 ding a unique platform to assess how histone ADP-ribosylation regulates DNA repair.

274 ular mechanism of DNA damage-induced histone ADP-ribosylation remains elusive.

275 F1; also known as C4orf27) as a regulator of ADP-ribosylation signaling in the DNA damage response.

276 e how a fundamental step in PARP-1-dependent ADP-ribosylation signaling is regulated and suggest that

277 physiologically relevant form of reversible ADP-ribosylation signalling.

278 ism and activation, as well as regulation of ADP-ribosylation signals by the readers and erasers of p

279 ome, as well as thousands of PARP-1-mediated ADP-ribosylation sites across the genome.

280 s identifies DNA damage induced histone mono-ADP-ribosylation sites by specific ARTs in vivo, providi

281 Mutations at these ADP-ribosylation sites lead to increased phosphorylation

282 We identified 1,048 ADP-ribosylation sites on 340 proteins involved in a wid

283 n or inhibition of PARP-1 or mutation of the ADP-ribosylation sites on NELF-E promotes Pol II pausing

284 We demonstrate their utility in identifying ADP-ribosylation sites on Poly(ADP-ribose) Polymerase 1

285 Treatment with PARPi or mutation of the ADP-ribosylation sites reduces DDX21 nucleolar localizat

286 Mutations of potential tankyrase1 ADP-ribosylation sites within the RGCADG motif of TRF1 s

287 hroughs in proteomics techniques to identify ADP-ribosylation sites, and future developments to provi

288 C-terminal-binding protein-1 short-form/BFA-ADP-ribosylation substrate (CtBP1-S/BARS), a bifunctiona

289 results demonstrate that very low levels of ADP-ribosylation, synthesized by either PARP1 or PARP2,

290 cribe a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk betwee

291 on triggers an unprecedented display of mono-ADP-ribosylation that governs the formation of Sec body,

292 l posttranslational modification of 53BP1 by ADP-ribosylation that is targeted by a PAR-binding E3 ub

293 xins introduce protein modifications such as ADP-ribosylation to manipulate host cell signaling and p

294 en complemented by recent advances that link ADP-ribosylation to stress responses, metabolism, viral

295 Galphai3 are the critical in vivo targets of ADP-ribosylation underlying VAAS elicited by PTX exposur

296 histone modifications and found that histone ADP-ribosylation was associated with histone removal at

297 cal processes now known to require PARPs and ADP-ribosylation was practically unimaginable even two d

298 iously unknown PARP downstream targets whose ADP-ribosylation was sensitive to PARP inhibitor treatme

299 catalytic fragment from our studies in auto-ADP-ribosylation, which is mediated through diffusible i

300 in particular, are known to utilize protein ADP-ribosylation, yet very little is known about their e