ライフサイエンスコーパス: ribosylation

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

2 bit Src kinase-dependent phagocytosis by ADP-ribosylation.

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

4 ly(ADP-ribosyl) transferases (PARPs) and ADP-ribosylation.

5 enzymes capable of modifying proteins by ADP-ribosylation.

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

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

8 the many cellular processes regulated by ADP-ribosylation.

9 ntly developed stereo- and regioselective N1-ribosylation.

10 post-translational modification by mono-ADP-ribosylation.

11 DD-induced TiPARP also targets PEPCK for ADP-ribosylation.

12 ously unidentified modulatory effects on ADP-ribosylation.

13 rosstalk between ubiquitination and poly-ADP-ribosylation.

14 ial forms of PEPCK were found to undergo ADP-ribosylation.

15 easing promoter accessibility by histone ADP-ribosylation.

16 pair but also elevated levels of protein ADP-ribosylation.

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

18 fects were independent of DNA damage and ADP-ribosylation.

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

20 two major enzymes that control cellular ADP-ribosylation.

21 from PARP1-independent excessive protein ADP-ribosylations.

22 RH3) are a family of enzymes to catalyze ADP-ribosylation, a reversible and covalent post-translation

23 oves the overall localization scores for ADP-ribosylation acceptor sites but also boosts ADP-ribosyla

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

25 ETA has ADP-ribosylation activity and decisively affects the protein

26 r, and this effect was dependent on mono-ADP ribosylation activity of poly(ADP-ribose) polymerase (PA

27 Parp9 ADP-ribosylation activity therefore restrains the E3 functio

28 ning nicked DNA and which target PARP3 trans-ribosylation activity to a single-histone substrate.

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

30 s, these sirtuins exhibit robust protein ADP-ribosylation activity.

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

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

33 ADP-ribosylation (ADPr) is a posttranslational modification

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

35 xpectedly, AHR suppression also enhanced ADP-ribosylation and did so by a poly(ADP-ribose) polymerase

36 n additional methyl group that prevented ADP-ribosylation and inactivation of EF2.

37 1 functions at the crossroads of histone ADP-ribosylation and PARP-1 automodification.

38 In vitro ADP-ribosylation and protein translation assays demonstrate

39 both amino-acid starvation induced mono-ADP-ribosylation and subsequent Sec body formation and cell

40 model of type-II diabetes and ameliorate the ribosylation and the activity/transnuclear localization

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

42 ains that interpret either mono- or poly-ADP-ribosylation and the implications for cellular processes

43 an the IC50 were required to ablate both ADP-ribosylation and XRCC1 chromatin binding following H2O2

44 PJ34 reduced PARP activity, GAPDH ribosylation, and GAPDH translocation; ameliorated muscl

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

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

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

48 lts provide an example of reversible DNA ADP-ribosylation, and we anticipate potential therapeutic be

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

50 ysine deacetylation, adenosinediphospho(ADP)-ribosylation, and/or deacylation.

51 mplications of this unexpected, O-linked ADP-ribosylation are speculated on.

52 ng microsomes, suggesting a role for the ADP-ribosylation (ARF)-dependent trafficking of cathepsin B.

53 e also failed to identify a role of PI31 ADP-ribosylation as a mechanism for regulation of overall 26

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

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

56 interdomain allosteric coupling, marking ADP ribosylation as a rapid posttranslational mechanism for

57 An ADP-ribosylation assay with recombinant SpyA demonstrated th

58 Radio-ADP-ribosylation assays reveal that shedding refocuses the t

59 although disruption of this site allows ADP-ribosylation at H2BE19.

60 dvanced our knowledge of the function of ADP-ribosylation at the molecular level.

61 ists and clinicians to better understand ADP-ribosylation at the molecular level.

62 stent with this, LPS stimulation-induced ADP-ribosylation at the nucleosome-occupied promoters of il-

63 acroD1, and MacroD2 proteins can reverse ADP-ribosylation by acting on ADP-ribosylated substrates thr

64 e (IRE-1) via modulation of the level of its ribosylation by PARP-16.

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

66 Poly-ADP-ribosylation, catalyzed by PARP1, is a post-translationa

67 se enzyme families, respectively, catalyze C-ribosylation conceivably through Michael-type addition o

68 accessibility assays reveal that histone ADP-ribosylation directly destabilizes histone-DNA interacti

69 kinase (ERK) signaling, Parp1 auto-poly ADP-ribosylation enhances Sox2-Parp1 interactions, and this

70 telium to identify site-specific histone ADP-ribosylation events in vivo and define the ARTs that med

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

72 ADP ribosylation factor (Arf) 6 anchors to the plasma membra

73 The ADP ribosylation factor (Arf) and the coat protein complex I

74 tivating proteins (GAPs) that act on the ADP-ribosylation factor (ARF) family of small GTPases.

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

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

77 ADP ribosylation factor (Arf) GTPases are key regulators of

78 Here we focused on ADP ribosylation factor (Arf) GTPases, which orchestrate a v

79 Members of the ADP-ribosylation factor (ARF) small GTPase family regulate m

80 lts in the sequential recruitment of the ADP-ribosylation factor (Arf)-like protein Arl1; the Arf-spe

81 We found that silencing of the ADP-ribosylation factor (Arf)-like small GTPase Arl13b led t

82 ic screen for IpaJ substrates identified ADP-ribosylation factor (ARF)1p and ARF2p, small molecular m

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

84 TBC1D24 interacts with ADP ribosylation factor (ARF)6, a small GTPase crucial for m

85 ecific interaction with the small GTPase ADP-ribosylation factor (ARF5) in its active, GTP-bound form

86 zing, gamma-adaptin ear homology domain, ADP-ribosylation factor (GGA)-binding motif affects the endo

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

88 fically associated with the small GTPase ADP-ribosylation factor 1 (Arf1) to mediate uniform distribu

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

90 c receptor (alpha(2B)-AR) interacts with ADP-ribosylation factor 1 (ARF1), a small GTPase involved in

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

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

93 wo subcomplexes: the membrane-targeting, ADP ribosylation factor 1 (Arf1):GTP-binding betagammadeltaz

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

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

96 ositol 3 kinase (PI3K)-dependent GTPase, ADP ribosylation factor 6 (ARF-6), to stimulate MHC-I intern

97 t of signalling through the small GTPase ADP-ribosylation factor 6 (ARF6) and its activator ARF nucle

98 Here we identify the ADP-ribosylation factor 6 (Arf6) as an important regulator o

99 control the activity of the small GTPase ADP-ribosylation factor 6 (Arf6) by consecutively recruiting

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

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

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

103 The ADP-ribosylation factor 6 (Arf6) isoform and the exchange fa

104 tosis and show that adenosine 5'-diphosphate-ribosylation factor 6 (Arf6) plays a key role in fibrino

105 The small G protein ADP-ribosylation factor 6 (Arf6) plays important roles in a

106 ADP-ribosylation factor 6 (ARF6) small GTPase regulates memb

107 a guanine nucleotide exchange factor for ADP-ribosylation factor 6 (ARF6) that promotes glut4 vesicle

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

109 ADP ribosylation factor 6 (ARF6) was recently identified as

110 The small GTPase ADP-ribosylation factor 6 (Arf6) was shown to regulate the p

111 ulates the activity of adenosine diphosphate ribosylation factor 6 (ARF6), a small G protein and upst

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

113 ARF6 (ADP-ribosylation factor 6) is a small GTPase implicated in e

114 ARF6 (ADP-ribosylation factor 6) small GTP binding protein plays c

115 tive state, which is further enhanced by ADP-ribosylation factor 6, a host cofactor for CTA1.

116 einases, RNA, caveolin-1, and the GTPase ADP-ribosylation factor 6, and are biologically active towar

117 xin substrate 1, p21-activated kinase 1, ADP-ribosylation factor 6, and cell division control protein

118 to show that clathrin, dynamin, and the ADP-ribosylation factor 6, three components of the endocytic

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

120 rentially modulating PKCalpha, RhoA, and ADP-ribosylation factor 6.

121 r localization: a step that requires the ADP-ribosylation factor ARF, an ATP-dependent step that requ

122 h Golgi-localized, gamma-ear-containing, ADP-ribosylation factor binding proteins (GGAs), and ArfGAP3

123 ARL13B is a member of the ADP ribosylation factor family of regulatory GTPases, but is

124 ate these processes: members of the adenosyl-ribosylation factor family of small G-proteins (ARFs) an

125 Arl13b belongs to the ADP-ribosylation factor family within the Ras superfamily of

126 e antigen representing adenosine diphosphate-ribosylation factor GTPase activating protein 1 revealed

127 ogy protein, and MTV4, which encodes the ADP ribosylation factor GTPase-activating protein nevershed/

128 opment associated with gene mutations in ADP-ribosylation factor guanine exchange factor 2 (ARFGEF2 e

129 an mutations in the Filamin A (FLNA) and ADP-ribosylation factor guanine exchange factor 2 [ARFGEF2;

130 c and recycling pathways mediated by the ADP ribosylation factor guanine nucleotide exchange factor (

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

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

133 e Golgi membrane/cytosol partitioning of ADP-ribosylation factor proteins.

134 ore, we identified the adenosine diphosphate ribosylation factor-1 GTPase to be required for mTORC1 a

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

136 ia a distinct pathway mediated by ARF-6 (ADP-ribosylation factor-6).

137 ze to the plasma membrane, caveolae, and ADP-ribosylation factor-6+ (Arf6+) endocytic compartments.

138 -localized, gamma adaptin-ear-containing ADP ribosylation factor-binding protein 3 (GGA3) interacts d

139 ized, gamma-adaptin ear domain homology, ADP ribosylation factor-binding protein 3), a multidomain cl

140 d Golgi-localized, gamma ear-containing, ADP-ribosylation factor-binding proteins (GGAs) are both ada

141 n Golgi-localized, gamma-ear-containing, ADP-ribosylation factor-binding proteins (Ggas) bind directl

142 ized, gamma-adaptin ear domain homology, ADP ribosylation factor-binding proteins 1 and 2 (GGA1 and G

143 cking by accelerating the replacement of ADP-ribosylation factor-bound GDP with GTP.

144 ating that the responsible BFA-sensitive ADP ribosylation factor-GTP exchange factor (ARF-GEF) is GNO

145 gene encodes a class 1 adenosine diphosphate ribosylation factor-gtpase-activating protein (ARF-GAP).

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

147 he function of the brefeldin A-sensitive ADP-ribosylation factor-guanine exchange factors (ARF-GEFs).

148 UNC50 acted by recruiting GBF1, an ADP ribosylation factor-guanine nucleotide exchange factor (

149 is facilitated by another JBTS protein, ADP-ribosylation factor-like 13B (ARL13B), but not by ARL2 o

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

151 Five conserved tubulin cofactors and ADP ribosylation factor-like 2 regulate the biogenesis and d

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

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

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

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

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

157 The gene for ADP ribosylation factor-like GTPase 13B (Arl13b) encodes a s

158 BBS3 (ARL6), an ADP ribosylation factor-like small GTPase, is not part of th

159 HLB1 was found to interact with the ADP-ribosylation-factor guanine nucleotide exchange factor,

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

161 Host ADP-ribosylation factors (ARFs) act as in vitro allosteric a

162 ADP ribosylation factors (Arfs) are small GTP-binding protei

163 ADP ribosylation factors (Arfs) are the central regulators o

164 G2 activate, through their Sec7 domains, ADP ribosylation factors (Arfs) by accelerating the replacem

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

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

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

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

169 ose regulated by GTP exchange factors on ADP-ribosylation factors GNOM-LIKE1 and HOPM INTERACTOR7/BFA

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

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

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

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

174 The characterization of the prealnumycin C-ribosylation illustrates an alternative means for attach

175 dentified roles for Tiparp, MacroD1, and ADP-ribosylation in AHR-mediated steatohepatitis and lethali

176 ence of the requirement for protein mono-ADP-ribosylation in Th cell differentiation.

177 ish a novel example for the role of mono-ADP-ribosylation in the formation of stress assemblies, and

178 terized by a specific increase in serine-ADP-ribosylation in vivo under untreated conditions as well

179 rder to visualise both Poly-, and Mono-, ADP-ribosylation in vivo, we engineered specific fluorescent

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

181 Protein ADP-ribosylation is a covalent posttranslational modificatio

182 Protein adenosine diphosphate (ADP)-ribosylation is a physiologically and pathologically imp

183 PARP catalysed ADP-ribosylation is a post-translational modification involv

184 ADP-ribosylation is a post-translational modification that c

185 Poly-ADP-ribosylation is a post-translational modification that r

186 ADP-ribosylation is a post-translational modification where

187 Adenosine diphosphate (ADP)-ribosylation is a post-translational protein modificatio

188 ADP-ribosylation is a posttranslational modification that ex

189 ADP-ribosylation is a posttranslational modification that mo

190 ADP-ribosylation is a posttranslational protein modification

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

192 Poly-ADP-ribosylation is a unique post-translational modification

193 ugh redundancy between H2BE18 and H2BE19 ADP-ribosylation is also apparent following DSBs in vivo, by

194 Protein ADP-ribosylation is an ancient posttranslational modificatio

195 ADP-ribosylation is governed by ADP-ribosyltransferases and

196 ADP-ribosylation is involved in the regulation of DNA repair

197 ADP-Ribosylation is reversed by hydrolases that cleave the g

198 Though ADP-ribosylation is therapeutically important, investigation

199 ings show that proper control of protein ADP-ribosylation levels affected by ARH1 is essential for ca

200 ADP ribosylation mapped to Arg470 and Arg492 in the substrat

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

202 Mono-ADP-ribosylation (MARylation) of mammalian proteins was firs

203 pecific nanobodies blocked CDTa-mediated ADP-ribosylation of actin.

204 ADP-ribosylation of Axin enhances its interaction with the W

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

206 ngal toxin brefeldin A (BFA) induces the ADP-ribosylation of C-terminal-binding protein-1 short-form/

207 Auto-ADP-ribosylation of cholix toxin appears to have negatively

208 mes and demonstrate, for the first time, the ribosylation of chromatin at a site-specific DNA single-

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

210 the disease-causing agent that, through ADP ribosylation of diphthamide, causes irreversible inactiv

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

212 ADP-ribosylation of effector arginines likely uncouples Rab5

213 ually but, in combination, catalyzed the ADP-ribosylation of eukaryotic elongation factor 2 and inhib

214 II or PE3) inhibits protein synthesis by ADP-ribosylation of eukaryotic elongation factor 2.

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

216 oth endogenous and exogenous substrates, ADP-ribosylation of exogenous substrates occurred more effic

217 the known microbial mechanisms, such as ADP ribosylation of G protein alpha-subunits by cholera and

218 ity/intracellular localization, and poly-ADP-ribosylation of GAPDH.

219 , nicks in mononucleosomes promote the trans-ribosylation of histone H2B specifically at Glu2.

220 HPF1 promotes PARP-1-dependent in trans ADP-ribosylation of histones and limits DNA damage-induced h

221 nduces PARP-1 enzymatic activity and the ADP-ribosylation of histones at transcriptionally active and

222 If increased ADP ribosylation of P2X(7) in CD38-deficient NOD mice underl

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

224 1-induced PARP1 activation leads to self-ADP ribosylation of PARP1, consumption of nicotinamide adeni

225 TNKS-mediated ADP-ribosylation of PI31 drastically reduces its affinity fo

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

227 r-N1-cIDPR via regio- and stereoselective N1-ribosylation of protected 8-bromoinosine.

228 ous roles of PARPs and the regulation of ADP-ribosylation of protein substrates.

229 ADP-ribosylation of proteins is emerging as an important reg

230 es insight into a mechanism for how ExoS ADP-ribosylation of Rab5 inhibits Rab5 function.

231 icrobe, Vareechon et al. (2017) describe ADP-ribosylation of Ras as a strategy to inhibit assembly of

232 ism for inhibition than observed for the ADP-ribosylation of Ras by ExoS, where ADP-ribosylated Ras l

233 e immune response requires ExoS-mediated ADP-ribosylation of Ras in neutrophils.

234 get specific transcripts for regulation; ADP-ribosylation of RNA-regulatory proteins can alter their

235 ARP) activity and posttranslational poly-ADP-ribosylation of several regulatory proteins involved in

236 olase (PARG), which dynamically regulate ADP-ribosylation of Smad3 and Smad4, two central signaling p

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

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

239 ch for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subseque

240 Ribosylation of the 4,6-disubstituted 2-deoxystreptamine

241 tereoselective, featuring (1) selective beta-ribosylation of the C2-methylated amino ribose, (2) sele

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

243 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 elect

245 d shortly after viral infection via poly-ADP-ribosylation of the RNA-induced silencing complex (RISC)

246 ADP-ribosylation of the small GTPase Rab5 has previously bee

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

248 y used for Ub conjugation to substrates, ADP-ribosylation of the Ub carboxyl terminus precludes ubiqu

249 also found that tankyrase1-mediated poly-ADP-ribosylation of TRF1 is important for both the interacti

250 A, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify subst

251 terodimer mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin, exclusively in the context of

252 ADP-ribosylation of vinculin disrupted focal adhesion comple

253 -ribosylation) or polymeric chains (poly-ADP-ribosylation) of ADP-ribose are conjugated to proteins b

254 ysteine as a novel amino-acid target for ADP-ribosylation on PARPs.

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

256 ectrometry analysis to identify sites of ADP-ribosylation on vimentin.

257 al modification where single units (mono-ADP-ribosylation) or polymeric chains (poly-ADP-ribosylation

258 1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described,

259 ere, we found unlike PARP1-mediated Poly-ADP-Ribosylation (PARylation) at genomic damage sites, PARyl

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

261 es (PARPs) catalyze massive protein poly ADP-ribosylation (PARylation) within seconds after the induc

262 ent repair pathways to block histone polyADP-ribosylation (PARylation), a known effect of chemotherap

263 ose) polymerase 1 (Parp1) catalyzes poly(ADP-ribosylation) (PARylation) and induces replication netwo

264 The cumulative results reveal a unique ribosylation pathway that is highlighted by, among other

265 Here we report that mono-ADP-ribosylation plays an important role in homologous recom

266 hat viral macro domains reverse cellular ADP-ribosylation, potentially cutting the signal of a viral

267 Here, we show that ADP-ribosylation promotes 26S proteasome activity in both Dr

268 controlling Axin levels, Tnks-dependent ADP-ribosylation promotes the reprogramming of Axin followin

269 A and AlnB are responsible for the overall C-ribosylation reaction.

270 marizes the current knowledge of nuclear ADP-ribosylation reactions and their role in chromatin plast

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

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

273 ADP-ribosylation refers to the addition of one or more ADP-r

274 ADP-ribosylation refers to the transfer of the ADP-ribose gr

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

276 Our data reveal the mechanism of poly-ADP-ribosylation reversal, with ADP-ribose as the dominant p

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

278 w a fundamental step in PARP-1-dependent ADP-ribosylation signaling is regulated and suggest that HPF

279 and activation, as well as regulation of ADP-ribosylation signals by the readers and erasers of prote

280 as well as thousands of PARP-1-mediated ADP-ribosylation sites across the genome.

281 entifies DNA damage induced histone mono-ADP-ribosylation sites by specific ARTs in vivo, providing a

282 Mutations at these ADP-ribosylation sites lead to increased phosphorylation.

283 We identified 1,048 ADP-ribosylation sites on 340 proteins involved in a wide ar

284 inhibition of PARP-1 or mutation of the ADP-ribosylation sites on NELF-E promotes Pol II pausing, pr

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

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

287 ghs in proteomics techniques to identify ADP-ribosylation sites, and future developments to provide a

288 erminal-binding protein-1 short-form/BFA-ADP-ribosylation substrate (CtBP1-S/BARS), a bifunctional pr

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

290 e a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk between li

291 riggers an unprecedented display of mono-ADP-ribosylation that governs the formation of Sec body, a r

292 introduce protein modifications such as ADP-ribosylation to manipulate host cell signaling and physi

293 ern blotting and cholera toxin-dependent ADP-ribosylation to show the Gs presence in the sperm head.

294 omplemented by recent advances that link ADP-ribosylation to stress responses, metabolism, viral infe

295 hai3 are the critical in vivo targets of ADP-ribosylation underlying VAAS elicited by PTX exposure.

296 processes now known to require PARPs and ADP-ribosylation was practically unimaginable even two decad

297 ly unknown PARP downstream targets whose ADP-ribosylation was sensitive to PARP inhibitor treatment.

298 alytic fragment from our studies in auto-ADP-ribosylation, which is mediated through diffusible inter

299 Silylated 4-aminopyrimidines 2 or 5 upon ribosylation with 1 provide products 3.

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