ライフサイエンスコーパス: ribosylation

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

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

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

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

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

6 two major enzymes that control cellular ADP-ribosylation.

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

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

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

10 enzymes capable of modifying proteins by ADP-ribosylation.

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

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

13 the many cellular processes regulated by ADP-ribosylation.

14 ntly developed stereo- and regioselective N1-ribosylation.

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

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

17 ously unidentified modulatory effects on ADP-ribosylation.

18 rosstalk between ubiquitination and poly-ADP-ribosylation.

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

20 unction and the mechanism of RNA phospho-ADP-ribosylation.

21 that inhibits bacterial clearance by its ADP-ribosylation.

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

23 from PARP1-independent excessive protein ADP-ribosylations.

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

25 phate-ribose polymerases (PARPs) promote ADP-ribosylation, a highly conserved, fundamental posttransl

26 PARPs-a family of enzymes that catalyze ADP-ribosylation, a posttranslational modification of protei

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

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

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

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

31 nction mutants to reveal that SIRT6 mono-ADP-ribosylation activity is required for transcriptional ac

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

33 Parp9 ADP-ribosylation activity therefore restrains the E3 functio

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

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

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

37 ediated polyglutamylation suppresses the ADP-ribosylation activity.

38 ADP-ribosylation (ADPr) is a posttranslational modification

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

40 ADP-ribosylation (ADPRylation) is a posttranslational modifi

41 ein, leading to inhibition of PARP1 auto-ADP-ribosylation and defective repair of oxidative lesions,

42 a functional interplay between H2B-Glu35 ADP-ribosylation and H2B-Ser36 phosphorylation that controls

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

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

45 In vitro ADP-ribosylation and protein translation assays demonstrate

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

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

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

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

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

51 signaling effects of NAD(+) mediated by ADP-ribosylation, and epigenetic effects of intracellular ad

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

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

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

55 s insights into the functions of protein ADP-ribosylation, and suggests activating TiPARP as an antic

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

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

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

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

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

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

62 hes 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 with

64 type immunotoxin in an adenosine diphosphate-ribosylation assay.

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

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

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

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

69 s as a negative regulator and suppresses ADP-ribosylation both in vitro and in vivo.

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

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

72 lar ATP concentrations or NAD-mediated P2RX7 ribosylation by the enzyme ARTC2.2 can induce P2RX7 pore

73 While ADP-ribosylation can be reversed by ADP-ribosylhydrolases, t

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

75 es performed with wild-type H2AX and the ADP-ribosylation-deficient E141A mutant suggest that H2AX AD

76 NADP(+) impairs ADP-ribosylation-dependent DNA damage repair and sensitizes

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

78 Moreover, loss of this ADP-ribosylation enhances serine-139 phosphorylation of H2AX

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

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

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

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

83 ucleotide exchange factors (GEFs) on the ADP-ribosylation factor (ARF) family of small GTPases initia

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

85 nal membrane trafficking is regulated by ADP-ribosylation factor (ARF) GTPases and the development th

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

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

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

89 ADP-ribosylation factor (Arf)-like 4A (Arl4A), an Arf small

90 ADP-ribosylation factor (Arf)-like 4D (Arl4D), one of the Ar

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

92 main GTPase-activating protein (GAP) for ADP-ribosylation factor (ARF)-type GTPases.

93 ecture; facilitates secretion; activates ADP-ribosylation factor (ARF)1, 3, 4, and 5; and recruits AR

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

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

96 e causes dissociation of the Sig-1R from ADP-ribosylation factor (ARF6), a G-protein regulating EV tr

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

98 ss of the small guanosine triphosphatase ADP-ribosylation factor 1 (Arf1) or its effector, phosphatid

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

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

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

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

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

104 Pase-independent mechanism that requires ADP-ribosylation factor 1 (Arf1).

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

106 s to identify and validate two key nodes-ADP-ribosylation factor 4 (ARF4) and valosin-containing prot

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

108 fically examine the expression levels of ADP-ribosylation factor 6 (ARF6) and EPS8-like 2 (EPS8L2) in

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

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

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

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

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

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

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

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

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

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

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

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

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

122 ecycling and degradation is regulated by ADP-ribosylation factor 6 (ARF6).

123 f endosomal trafficking, including Arf6 (ADP ribosylation factor 6) GTPase activating proteins and cl

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

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

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

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

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

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

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

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

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

133 GNOM and its suppressor, ADENOSINE PHOSPHATE RIBOSYLATION FACTOR GTPase ACTIVATION PROTEIN DOMAIN3, a

134 ed that ALA3 functions together with the ADP ribosylation factor GTPase exchange factors GNOM and BIG

135 he developing neuron, the protein ADAP1 (ADP-ribosylation factor GTPase-activating protein [ArfGAP] w

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

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

138 es the activation of members of the ARF (ADP-ribosylation factor) family of small GTPases.

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

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

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

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

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

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

145 ized, gamma-adaptin ear domain homology, ADP ribosylation factor-binding proteins (GGAs) mediate the

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

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

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

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

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

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

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

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

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

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

156 otein complex, AP-4, and small G protein ADP-ribosylation factor-like GTPase 5b (Arl5b) are required

157 on impeded the interaction of PROM1 with ADP-ribosylation factor-like protein 13B, a key regulator of

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

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

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

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

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

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

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

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

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

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

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

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

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

174 Protein ADP-ribosylation is a covalent posttranslational modificatio

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

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

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

178 ADP-ribosylation is a post-translational modification that o

179 ADP-ribosylation is a post-translational modification where

180 ADP-ribosylation is a posttranslational modification that ex

181 ADP-ribosylation is a posttranslational protein modification

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

183 ADP-ribosylation is a reversible chemical modification catal

184 ADP-ribosylation is a unique posttranslational modification

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

186 Protein ADP-ribosylation is an ancient posttranslational modificatio

187 ADP-ribosylation is an intricate and versatile posttranslati

188 ADP-ribosylation is governed by ADP-ribosyltransferases and

189 ADP-ribosylation is integral to a diverse range of cellular

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

191 Though ADP-ribosylation is therapeutically important, investigation

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

193 arget proteins, leading to mono- or poly-ADP-ribosylation (MARylation or PARylation).

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

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

196 Our data suggest that RNA ADP-ribosylation may represent a widespread and physiologica

197 together, these results reveal that H2AX ADP-ribosylation not only facilitates BER repair, but also s

198 T16 has hydrolase activities that remove ADP-ribosylation of 53BP1 to regulate 53BP1 stability and 53

199 tor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamid

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

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

202 We demonstrate that SIRT6 mono-ADP-ribosylation of BAF170, a subunit of BAF chromatin remod

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

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

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

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

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

208 ADP-ribosylation of effector arginines likely uncouples Rab5

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

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

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

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

213 TP-loading and pertussis toxin-catalyzed ADP-ribosylation of G(i)alpha, for which we synthesized a no

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

215 ADP-ribosylation of Glu35 and the subsequent reduction of H2

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

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

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

219 Although ADP-ribosylation of histones by PARP-1 has been linked to ge

220 l DNA damage response is associated with ADP-ribosylation of histones.

221 ncluding long-chain deacylation and mono-ADP-ribosylation of other proteins, have also been reported,

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

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

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

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

226 s, enzymes that remove posttranslational ADP-ribosylation of proteins, and viral multifunctional papa

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

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

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

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

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

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

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

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

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

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

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

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

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

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

241 sponse to CT is due to adenosine diphosphate ribosylation of the small G protein alpha-subunit activa

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

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

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

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

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

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

248 ADP-ribosylation of vinculin disrupted focal adhesion comple

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

250 Mechanistically, ADP-ribosylation on E141 mediates the recruitment of Neil3 g

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

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

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

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

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

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

257 Poly(ADP) ribosylation (PARylation) is important for subsequent ch

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

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

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

261 ification in particular for protein poly-ADP-ribosylation (PARylation).

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

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

264 ADP-ribosylation plays an important role in several biologic

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

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

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

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

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

270 h cysteine modifying S-nitrosylation and ADP-ribosylation reactions using a chemical nitric oxide don

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

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

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

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

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

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

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

278 siologically relevant form of reversible ADP-ribosylation signalling.

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

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

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

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 sttranslational modification of 53BP1 by ADP-ribosylation that is targeted by a PAR-binding E3 ubiqui

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

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

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

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