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 inhibit Src kinase-dependent phagocytosis by ADP-ribosylation.

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

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

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

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

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

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

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

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

11 reviously unidentified modulatory effects on ADP-ribosylation.

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

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

14 increasing promoter accessibility by histone ADP-ribosylation.

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

16 l for deconvoluting the biochemical roles of ADP-ribosylation.

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

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

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

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

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

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

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

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

25 epair, and this effect was dependent on mono-ADP ribosylation activity of poly(ADP-ribose) polymerase

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

27 Parp9 ADP-ribosylation activity therefore restrains the E3 fun

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

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

30 ARTD15 displays auto-mono(ADP-ribosylation) activity and is affected by canonical

31 ADP-ribosylation actor 6 (ARF6) regulates the endocytosi

32 ADP-ribosylation (ADP(R)) of eEF2 by bacterial toxins on

33 ADP-ribosylation (ADPr) is a posttranslational modificat

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

35 itors modestly increased the levels of PARP1 ADP ribosylation and molecular or small-molecule inhibit

36 Unexpectedly, AHR suppression also enhanced ADP-ribosylation and did so by a poly(ADP-ribose) polyme

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

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

39 In vitro ADP-ribosylation and protein translation assays demonstr

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

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

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

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

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

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

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

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

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

49 ole in the turnover and recycling of protein ADP-ribosylation, and we have implicated the importance

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

51 aining microsomes, suggesting a role for the ADP-ribosylation (ARF)-dependent trafficking of cathepsi

52 ith interdomain allosteric coupling, marking ADP ribosylation as a rapid posttranslational mechanism

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

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

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

56 An ADP-ribosylation assay with recombinant SpyA demonstrate

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

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

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

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

61 onsistent with this, LPS stimulation-induced ADP-ribosylation at the nucleosome-occupied promoters of

62 0, MacroD1, and MacroD2 proteins can reverse ADP-ribosylation by acting on ADP-ribosylated substrates

63 Axin turnover is controlled by its poly-ADP-ribosylation catalyzed by tankyrase (TNKS), which re

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

65 ase accessibility assays reveal that histone ADP-ribosylation directly destabilizes histone-DNA inter

66 ated kinase (ERK) signaling, Parp1 auto-poly ADP-ribosylation enhances Sox2-Parp1 interactions, and t

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

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

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

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

71 ADP ribosylation factor (Arf) GTPases are key regulators

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

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

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

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

76 We report a novel role for the small GTPase ADP ribosylation factor 4 (Arf4) in controlling pattern

77 ylinositol 3 kinase (PI3K)-dependent GTPase, ADP ribosylation factor 6 (ARF-6), to stimulate MHC-I in

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

79 ADP ribosylation factor 6 (ARF6) was recently identified

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

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

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

83 Pst) DC3000 infection of Arabidopsis, a host ADP ribosylation factor guanine nucleotide exchange fact

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

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

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

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

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

89 ndicating that the responsible BFA-sensitive ADP ribosylation factor-GTP exchange factor (ARF-GEF) is

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

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

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

93 BBS3 (ARL6), an ADP ribosylation factor-like small GTPase, is not part o

94 e-activating proteins (GAPs) that act on the ADP-ribosylation factor (ARF) family of small GTPases.

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

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

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

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

99 We found that silencing of the ADP-ribosylation factor (Arf)-like small GTPase Arl13b l

100 enetic screen for IpaJ substrates identified ADP-ribosylation factor (ARF)1p and ARF2p, small molecul

101 Previous studies indicated that ADP-ribosylation factor (ARF)6 and its GTP-exchange fact

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

103 calizing, gamma-adaptin ear homology domain, ADP-ribosylation factor (GGA)-binding motif affects the

104 is a 64-kDa protein containing a functional ADP-ribosylation factor (GTP hydrolase, GTPase), GTPase-

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

106 tudies defined the STAU1-binding site within ADP-ribosylation factor 1 (ARF1) mRNA as a 19-base-pair

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

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

109 ergic receptor (alpha(2B)-AR) interacts with ADP-ribosylation factor 1 (ARF1), a small GTPase involve

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

111 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1).

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

113 esult of signalling through the small GTPase ADP-ribosylation factor 6 (ARF6) and its activator ARF n

114 Here we identify the ADP-ribosylation factor 6 (Arf6) as an important regulat

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

116 Here, we report a novel role for the ADP-ribosylation factor 6 (ARF6) GTPase in the post-mito

117 ADP-ribosylation factor 6 (ARF6) is a member of the Ras

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

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

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

121 as a guanine nucleotide exchange factor for ADP-ribosylation factor 6 (ARF6) that promotes glut4 ves

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

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

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

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

126 ARF6 (ADP-ribosylation factor 6) small GTP binding protein pla

127 equires the activation of small GTPase Arf6 (ADP-ribosylation factor 6), which regulates intracellula

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

129 proteinases, RNA, caveolin-1, and the GTPase ADP-ribosylation factor 6, and are biologically active t

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

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

132 Another PLD1 activator, ADP-ribosylation factor 6, was involved in VWF secretion

133 ifferentially modulating PKCalpha, RhoA, and ADP-ribosylation factor 6.

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

135 with Golgi-localized, gamma-ear-containing, ADP-ribosylation factor binding proteins (GGAs), and Arf

136 ADP-ribosylation factor domain protein 1 (ARD1) is a 64-

137 Arl13b, a ciliary protein within the ADP-ribosylation factor family and Ras superfamily of GT

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

139 evelopment associated with gene mutations in ADP-ribosylation factor guanine exchange factor 2 (ARFGE

140 Human mutations in the Filamin A (FLNA) and ADP-ribosylation factor guanine exchange factor 2 [ARFGE

141 nucleotide exchange factors (GEFs), such as ADP-ribosylation factor nucleotide binding site opener (

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

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

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

145 ) and Golgi-localized, gamma ear-containing, ADP-ribosylation factor-binding proteins (GGAs) are both

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

147 afficking by accelerating the replacement of ADP-ribosylation factor-bound GDP with GTP.

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

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

150 PP5E is facilitated by another JBTS protein, ADP-ribosylation factor-like 13B (ARL13B), but not by AR

151 gulation of GliA and GliR: the cilia protein ADP-ribosylation factor-like 13b (Arl13b).

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

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

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

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

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

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 ADP ribosylation factors (Arfs) are small GTP-binding pr

160 ADP ribosylation factors (Arfs) are the central regulato

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

162 e-exchange protein (BIG) 1 activates class I ADP ribosylation factors (ARFs) by accelerating the repl

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

164 ADP-ribosylation factors (ARFs) and their activating gua

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

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

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

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

169 e those regulated by GTP exchange factors on ADP-ribosylation factors GNOM-LIKE1 and HOPM INTERACTOR7

170 nucleotide-exchange protein (BIG)2 activates ADP-ribosylation factors, approximately 20-kDa GTPase pr

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

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

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

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

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

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

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

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

179 Despite these roles, the functions of ADP-ribosylation, in particular mono-ADP-ribosylation, r

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

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

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

183 Protein ADP-ribosylation is a covalent posttranslational modific

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

185 Poly-ADP-ribosylation is a post-translational modification th

186 ADP-ribosylation is a post-translational modification th

187 ADP-ribosylation is a post-translational modification wh

188 ADP-ribosylation is a posttranslational modification tha

189 ADP-ribosylation is a posttranslational modification tha

190 ADP-ribosylation is a posttranslational protein modifica

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

192 Protein ADP-ribosylation is a reversible posttranslational modif

193 Poly-ADP-ribosylation is a unique post-translational modifica

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

195 Protein ADP-ribosylation is an ancient posttranslational modific

196 ADP-ribosylation is an important post-translational modi

197 ADP-ribosylation is governed by ADP-ribosyltransferases

198 ADP-ribosylation is involved in the regulation of DNA re

199 ADP-Ribosylation is reversed by hydrolases that cleave t

200 Though ADP-ribosylation is therapeutically important, investiga

201 findings show that proper control of protein ADP-ribosylation levels affected by ARH1 is essential fo

202 ADP ribosylation mapped to Arg470 and Arg492 in the subs

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

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

205 In this issue, Chambers et al. report that ADP ribosylation of BiP provides a reversible switch tha

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

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

208 d to the known microbial mechanisms, such as ADP ribosylation of G protein alpha-subunits by cholera

209 If increased ADP ribosylation of P2X(7) in CD38-deficient NOD mice un

210 by ADP ribosyltransferase-2 (ART2)-mediated ADP ribosylation of P2X(7) receptors.

211 HES1-induced PARP1 activation leads to self-ADP ribosylation of PARP1, consumption of nicotinamide a

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

213 his manuscript, the transition state for the ADP-ribosylation of acetyllysine is solved for an Archae

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

215 ATP-like conformation of the W-loop, whereas ADP-ribosylation of Arg-177 forces the W-loop into a con

216 ADP-ribosylation of Axin enhances its interaction with t

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

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

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

220 ences in killing were due to steps after the ADP-ribosylation of EF2.

221 ADP-ribosylation of effector arginines likely uncouples

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

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

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

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

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

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

228 on induces PARP-1 enzymatic activity and the ADP-ribosylation of histones at transcriptionally active

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

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

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

232 ADP-ribosylation of proteins is emerging as an important

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

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

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

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

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

238 e (PARP) activity and posttranslational poly-ADP-ribosylation of several regulatory proteins involved

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

240 Thus, our study suggests that ADP-ribosylation of SpyB may be an important function of

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

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

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

244 Our results showed that ADP-ribosylation of the Fe protein does not affect the e

245 er with an IL-4 signal, this is aided by the ADP-ribosylation of the HDACs by PARP-14.

246 duced shortly after viral infection via poly-ADP-ribosylation of the RNA-induced silencing complex (R

247 ADP-ribosylation of the small GTPase Rab5 has previously

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

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

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

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

252 9 heterodimer mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin, exclusively in the contex

253 ADP-ribosylation of vinculin disrupted focal adhesion co

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

255 B level, gamma-H2AX foci formation, and poly(ADP-ribosylation) of PARP-1, which were associated with

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

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

258 s spectrometry analysis to identify sites of ADP-ribosylation on vimentin.

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

260 Poly adenosine diphosphate (ADP)-ribosylation (PARylation) by poly ADP-ribose (PAR)

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

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

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

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

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

266 chromatin domains surrounding DSBs via poly-ADP-ribosylation, phosphorylation, acetylation, and prot

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

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

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

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

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

272 A family of proteins that catalyse ADP-ribosylation reactions are the poly(ADP-ribose) (PAR

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

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

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

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

277 ions of ADP-ribosylation, in particular mono-ADP-ribosylation, remain poorly understood.

278 Our data reveal the mechanism of poly-ADP-ribosylation reversal, with ADP-ribose as the domina

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

295 Western blotting and cholera toxin-dependent ADP-ribosylation to show the Gs presence in the sperm he

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

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

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

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

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

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