ライフサイエンスコーパス: ADP-ribosyltransferase

1 osyltransferase designated SpyA (S. pyogenes ADP-ribosyltransferase).

2 the C-terminus (residues 232-453) encodes an ADP-ribosyltransferase.

3 ibose antibodies, suggesting that Sir2 is an ADP-ribosyltransferase.

4 ivation of phospholipase D and cholera toxin ADP-ribosyltransferase.

5 in blocking ARF stimulation of cholera toxin ADP-ribosyltransferase.

6 he potential for ExoS to function as an ecto-ADP-ribosyltransferase.

7 was characterized as a diphthamide dependent ADP-ribosyltransferase.

8 he ability of 14-3-3 to activate exoenzyme S ADP-ribosyltransferase.

9 express on their surfaces arginine-specific ADP ribosyltransferases.

10 h the enzymatic activity of deacetylases and ADP ribosyltransferases.

11 oiety into hydrophobic subpockets in various ADP-ribosyltransferases.

12 y link between bacterial and vertebrate mono-ADP-ribosyltransferases.

13 nzylguanidine, inhibitors of endogenous mono-ADP-ribosyltransferases.

14 o-ADP-ribosyltransferases than the bacterial ADP-ribosyltransferases.

15 t have been attributed to several vertebrate ADP-ribosyltransferases.

16 catalyzed by a family of amino acid-specific ADP-ribosyltransferases.

17 mechanism of NAD binding and catalysis among ADP-ribosyltransferases.

18 omology (DNA or amino acid) with other known ADP-ribosyltransferases.

19 of ADP-ribose are conjugated to proteins by ADP-ribosyltransferases.

20 r tested against a panel of homologous human ADP-ribosyltransferases.

21 ng loops, L1 and L4, not found in other mono-ADP-ribosyltransferases.

22 We found that an arginine-specific ADP ribosyltransferase-1 present on airway epithelial ce

23 Full length cDNA encoding ADP-ribosyltransferase-1 (ART1) was generated from human

24 First, IENK cells express high levels of ADP-ribosyltransferase 2 (a marker of regulatory T cells

25 uitously expressed CD38 and T cell-expressed ADP-ribosyltransferase 2 (ART2) are ectoenzymes competin

26 We found that in the absence of CD38, ADP-ribosyltransferase 2 preferentially activates apopto

27 itive to NAD-induced cell death activated by ADP ribosyltransferase-2 (ART2)-mediated ADP ribosylatio

28 selective inhibitor of diphtheria toxin-like ADP-ribosyltransferase 3 (ARTD3).

29 ADP-ribosyltransferase 5 (ART5), a murine transferase or

30 Among these were genes encoding additional ADP-ribosyltransferases, a homolog of SrfC (a candidate

31 hat have two amino acid substitutions in the ADP-ribosyltransferase active center (E112K) and COOH-te

32 eins possesses NAD-dependent deacetylase and ADP ribosyltransferase activities.

33 ut also carrying out ADP-ribosyl cyclase and ADP-ribosyltransferase activities, making SPN the only b

34 esses both Rho GTPase-activating protein and ADP-ribosyltransferase activities.

35 e fragment, which possesses both the GAP and ADP-ribosyltransferase activities.

36 otide (NAD) glycohydrolase (NADase) and auto-ADP-ribosyltransferase activities.

37 bbit muscle increased NAD glycohydrolase and ADP-ribosyltransferase activities.

38 nd lacked detectable ADP-ribosyl cyclase and ADP-ribosyltransferase activities.

39 A subunit (S61F), which resulted in loss of ADP ribosyltransferase activity and toxicity.

40 solated B-oligomer subunit of PTX that lacks ADP ribosyltransferase activity nor the related cholera

41 tudy, we have used LFnDTA and its associated ADP-ribosyltransferase activity (DTA) to determine the r

42 e effector proteins include two enzymes with ADP-ribosyltransferase activity (ExoS and ExoT) and an a

43 of mutagenesis were quantified by measuring ADP-ribosyltransferase activity (i.e., auto-ADP-ribosyla

44 Using the translocation of C-domain ADP-ribosyltransferase activity across the endosomal mem

45 protein toxin that has diphthamide-specific ADP-ribosyltransferase activity against eukaryotic elong

46 , inhibition of ARF-stimulated cholera toxin ADP-ribosyltransferase activity and effects of ARF on mu

47 Thus, redirection of TT is dependent on ADP-ribosyltransferase activity and GM1 binding and is a

48 minal domain of ExoS possesses FAS-dependent ADP-ribosyltransferase activity and is cytotoxic to euka

49 by their ability to stimulate cholera toxin ADP-ribosyltransferase activity and later recognized as

50 by their ability to stimulate cholera toxin ADP-ribosyltransferase activity and now recognized as cr

51 ed that V. fischeri hvn null still possessed ADP-ribosyltransferase activity and that this activity i

52 duction of ExoS was monitored by a sensitive ADP-ribosyltransferase activity assay, and specific acti

53 eltaN222 so it could express FAS-independent ADP-ribosyltransferase activity at a linear rate.

54 id homology, Exo53 has been shown to express ADP-ribosyltransferase activity at about 0.2% of the spe

55 ExoT also affects PI3K signaling via its ADP-ribosyltransferase activity but does not act directl

56 hat a E379D mutation inhibited expression of ADP-ribosyltransferase activity but had little effect on

57 These data demonstrate ecto-ADP-ribosyltransferase activity by ExoS.

58 ase activity, and in J744-Eclone cells, ExoS ADP-ribosyltransferase activity caused a more severe inh

59 protein (GAP) activity, or ExoS defective in ADP-ribosyltransferase activity demonstrated that the vi

60 Recently, ExoS ADP-ribosyltransferase activity has been detected in the

61 e protein stimulated cholera-toxin-catalyzed ADP-ribosyltransferase activity in a reaction that was d

62 investigate the structural requirements for ADP-ribosyltransferase activity in human PARP13 and two

63 lytic residues that is required for the mono-ADP-ribosyltransferase activity involved in ubiquitin ac

64 We suggest that the reported histone/protein ADP-ribosyltransferase activity is a low-efficiency side

65 The latent ADP-ribosyltransferase activity of cholera toxin (CT) th

66 The ARF proteins stimulate the in vitro ADP-ribosyltransferase activity of cholera toxin and app

67 and purified by their ability to enhance the ADP-ribosyltransferase activity of cholera toxin and mor

68 identified by their ability to stimulate the ADP-ribosyltransferase activity of cholera toxin in vitr

69 ditions, the initial rate of FAS-independent ADP-ribosyltransferase activity of DeltaN222 was not lin

70 ither NaCH3COOH, NaCl, or KCl stabilized the ADP-ribosyltransferase activity of DeltaN222.

71 Antibodies to this epitope blocked the ADP-ribosyltransferase activity of ETA and appeared to i

72 The mechanism for the lower ADP-ribosyltransferase activity of Exo53 relative to Exo

73 Here, two aspects of the activation of the ADP-ribosyltransferase activity of ExoS by 14-3-3 protei

74 We investigated whether the ADP-ribosyltransferase activity of ExoS influences its G

75 Although the ADP-ribosyltransferase activity of ExoS is dependent upo

76 xoS-GAP was identified as a substrate of the ADP-ribosyltransferase activity of ExoS.

77 The ADP-ribosyltransferase activity of ExoT stimulated depol

78 used NAD analogues and 32P-NAD to study the ADP-ribosyltransferase activity of several different sir

79 other sirtuins, we propose that the reported ADP-ribosyltransferase activity of sirtuins is likely so

80 These findings suggest that Sir2 contains an ADP-ribosyltransferase activity that is essential for it

81 cal studies have localized the FAS-dependent ADP-ribosyltransferase activity to the carboxyl-terminus

82 genesis and analyzed both NAD(+) binding and ADP-ribosyltransferase activity using a fluorescence-bas

83 Thus, ADP-ribosyltransferase activity was essential for antige

84 The ADP-ribosyltransferase activity was released from transf

85 genetically engineered PTX mutant (devoid of ADP-ribosyltransferase activity) altered TER.

86 oxin (LT), and LTK63 (an LT mutant devoid of ADP-ribosyltransferase activity) to elicit murine CD8(+)

87 Inactivation of Rab5 was dependent on ExoS ADP-ribosyltransferase activity, and in J744-Eclone cell

88 in after PTX and were dependent on intrinsic ADP-ribosyltransferase activity, as neither the cell bin

89 s not inhibited by mutant LT with attenuated ADP-ribosyltransferase activity, CT B or LT B subunit, w

90 their ability to activate cholera toxin (CT) ADP-ribosyltransferase activity, have a critical role in

91 ExoS(E381D), a mutant deficient in ADP-ribosyltransferase activity, isolated from cultured

92 ither mutant CT nor mutant LTh-1, which lack ADP-ribosyltransferase activity, redirected TT antigen i

93 lase activity, have been reported to possess ADP-ribosyltransferase activity, too.

94 are a number of reports that suggest protein ADP-ribosyltransferase activity.

95 rulence of ExoS was largely dependent on its ADP-ribosyltransferase activity.

96 ) encodes a factor-activating ExoS-dependent ADP-ribosyltransferase activity.

97 ity, while the C-terminal domain comprises a ADP-ribosyltransferase activity.

98 d chemiluminescence responses and had potent ADP-ribosyltransferase activity.

99 m cells transfected with deltaN222 expressed ADP-ribosyltransferase activity.

100 activating exoenzyme S (FAS) for expressing ADP-ribosyltransferase activity.

101 antigen processing correlated with A subunit ADP-ribosyltransferase activity.

102 yme S (FAS) activation for the expression of ADP-ribosyltransferase activity.

103 PARP13 lacks the structural requirements for ADP-ribosyltransferase activity.

104 Most members have mono-ADP-ribosyltransferase activity.

105 ponding positions in PARP15 abolished PARP15 ADP-ribosyltransferase activity.

106 ed the chemical binder space of enzymes with ADP-ribosyltransferase activity.

107 pendent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity.

108 ion, although some sirtuins exhibit a weaker ADP-ribosyltransferase activity.

109 is concluded that ecto-NAD, as substrate of ADP ribosyltransferase, acts on naive, but not on activa

110 ity domain mutants of exoS revealed that the ADP-ribosyltransferase (ADP-r) activity of ExoS, but not

111 w that the type III effector HopU1 is a mono-ADP-ribosyltransferase (ADP-RT).

112 Point mutations in the ADP ribosyltransferase (ADPR) regions of ExoS or ExoT al

113 ed that the pBC210 LF homologue contained an ADP-ribosyltransferase (ADPr) domain.

114 towards Rho family GTPases and a C-terminal ADP ribosyltransferase (ADPRT) domain with minimal activ

115 se Cbl-b and Crk, the substrate for the ExoT ADP ribosyltransferase (ADPRT) domain.

116 oS includes both GTPase-activating (GAP) and ADP-ribosyltransferase (ADPRT) activities, and P. aerugi

117 or protein, with GTPase-activating (GAP) and ADP-ribosyltransferase (ADPRT) activities.

118 ting (GAP) activity and the carboxy-terminal ADP-ribosyltransferase (ADPRT) activity of ExoS have bee

119 We assessed the ADP-ribosyltransferase (ADPRT) activity of various domai

120 ow-molecular-weight G (LMWG) proteins and an ADP-ribosyltransferase (ADPRT) activity that targets LMW

121 Significantly higher levels of ExoS ADP-ribosyltransferase (ADPRT) activity were detected in

122 ae is a 591-amino-acid virulence factor with ADP-ribosyltransferase (ADPRT) and vacuolating activitie

123 vating protein (GAP) domain and a C-terminal ADP-ribosyltransferase (ADPRT) domain.

124 tein having both GTPase-activating (GAP) and ADP-ribosyltransferase (ADPRT) functional domains.

125 The ADP-ribosyltransferase (ADPRT) gene encodes a zinc-finge

126 ADP-ribosyltransferase (ADPRT) is a glycosylphosphatidyl

127 Preferred substrates of the ADP-ribosyltransferase (ADPRT) portion of ExoS include l

128 ently described a cell surface protein, mono-ADP-ribosyltransferase (ADPRT), on cytotoxic T cells and

129 tation as found in the A chain of CRM197, an ADP-ribosyltransferase (ADPrT)-deficient form of DTx, we

130 odrin, calmodulin-dependent protein kinases, ADP-ribosyltransferase (ADPRT/PARP) and tau.

131 , that exhibits sequence similarity to known ADP-ribosyltransferases (ADPRTs) such as Bordetella pert

132 This post-translational modification and the ADP-ribosyltransferases (also known as PARPs) responsibl

133 activities from a single Sde polypeptide: an ADP-ribosyltransferase and a nucleotidase/phosphohydrola

134 a bioinformatic strategy as a putative mono-ADP-ribosyltransferase and a possible virulence factor f

135 ble poly(ADP-ribose) polymerase (Tiparp), an ADP-ribosyltransferase and AHR repressor, increases sens

136 Both ADP-ribosyltransferase and deacetylase activities of SIR

137 e dra operon encodes dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase-activ

138 One ADP-ribosyltransferase and the SrfC homolog were tested

139 ADP-ribosylation is governed by ADP-ribosyltransferases and a subclass of sirtuins (writ

140 e modification of proteins with NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolas

141 NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolas

142 ic cross talk exists between bacterial toxin ADP-ribosyltransferases and host ADP-ribosylation cycles

143 The bacterial ADP-ribosyltransferases are a family of protein toxins t

144 We conclude that endogenous mono-ADP-ribosyltransferases are present in smooth muscle fro

145 is pathologic process, PARP-1 and other poly(ADP-ribosyltransferases) are also localized within mitoc

146 y epithelial cells express arginine-specific ADP ribosyltransferase (ART)-1, a GPI-anchored ART that

147 e used to detect ecto-adenosine diphosphate (ADP)-ribosyltransferase (ART) activity.

148 Several proteins with NAD+:arginine ADP-ribosyltransferase (ART) activity are expressed in T

149 N372 encodes a 68-kDa protein that possesses ADP-ribosyltransferase (ART) activity.

150 ation is catalyzed by ART2.2, a GPI-anchored ADP-ribosyltransferase (ART) that is constitutively expr

151 presence of NAD-metabolizing enzymes (e.g., ADP-ribosyltransferase (ART)2) on the surface of immune

152 NAD but not ADPR provides the substrate for ADP-ribosyltransferase (ART-2)-mediated attachment of AD

153 Arginine-specific ADP-ribosyltransferases (ART) on the surface of these ce

154 ding human skeletal muscle arginine-specific ADP-ribosyltransferase (ART1).

155 Five mammalian ADP-ribosyltransferases (ART1--ART5) have been cloned an

156 Mono-ADP-ribosyltransferases (ART1-7) transfer ADP-ribose fro

157 and HvnB were presumptively designated mono-ADP-ribosyltransferases (ARTases), and it was hypothesiz

158 The diphtheria toxin-like ADP-ribosyltransferases (ARTDs) are an enzyme family tha

159 ADP-ribosyltransferases (ARTs) catalyze transfer of ADP-

160 ADP-ribosyltransferases (ARTs) modify proteins with sing

161 rgely mediated by a family of mammalian ecto-ADP-ribosyltransferases (ARTs) that covalently modify ta

162 All mutants were inactive in the ADP-ribosyltransferase assay; however, auto-ADP-ribosyla

163 are similarly ADP-ribosylated by endogenous ADP-ribosyltransferase, but only one arginine is modifie

164 characterized for this enzyme from the mono-ADP-ribosyltransferase C3 toxin subgroup.

165 by microinjection of a Clostridium botulinum ADP-ribosyltransferase (C3) and treatment with a ROCK sp

166 Thus, mRt6.1 is an NAD:arginine ADP-ribosyltransferase capable of catalyzing a multiple

167 Protein ADP-ribosyltransferases catalyze the transfer of adenosi

168 mary adenocarcinoma) cells with NAD:arginine ADP-ribosyltransferase cDNAs from Yac-1 murine lymphoma

169 veral polysaccharide capsules, and the novel ADP-ribosyltransferase, Certhrax.

170 This protein modification is often added by ADP-ribosyltransferases, commonly known as PARPs, but it

171 P gamma ADP-ribosylation, indicates that rod ADP-ribosyltransferase contains two isozymes, and that t

172 Thus, airway mono-ADP-ribosyltransferases could have an important regulato

173 se findings reveal links between a mammalian ADP ribosyltransferase, cytokine-regulated metabolic act

174 The ADP-ribosyltransferase-deficient CT-2* protein, which wa

175 Streptococcus pyogenes produces a C3 family ADP-ribosyltransferase designated SpyA (S. pyogenes ADP-

176 ed by the DRAT-DRAG (dinitrogenase reductase ADP-ribosyltransferase-dinitrogenase reductase-activatin

177 , independent of the dinitrogenase reductase ADP-ribosyltransferase/dinitrogenase reductase activatin

178 Mice deficient for ADP-ribosyltransferase diphteria toxin-like 1 (ARTD1) ar

179 Furthermore, comparing with a bacterial ADP-ribosyltransferase diphtheria toxin, the observed ra

180 nas aeruginosa, which comprises a C-terminal ADP ribosyltransferase domain and an N-terminal Rho GTPa

181 oenzyme S, which represent the FAS-dependent ADP-ribosyltransferase domain (termed deltaN222), and a

182 t form of ExoS rounded cells, indicating the ADP-ribosyltransferase domain alone is sufficient to eli

183 of this study was to define the role of the ADP-ribosyltransferase domain in the modulation of eukar

184 , these data indicate that expression of the ADP-ribosyltransferase domain of exoenzyme S is cytotoxi

185 A single amino acid mutation in the putative ADP-ribosyltransferase domain of SIRT1 inhibits the inte

186 The RhoGAP-, but not the ADP-ribosyltransferase domain of the related effector pr

187 rminus (residues 233-453) is a FAS-dependent ADP-ribosyltransferase domain that targets Ras and Ras-l

188 onal mapping has localized the FAS-dependent ADP-ribosyltransferase domain to the carboxyl-terminus o

189 This putative bacterial ADP-ribosyltransferase domain was denoted CerADPr.

190 esidues 234-453 include the 14-3-3-dependent ADP-ribosyltransferase domain.

191 idues 233 to 453 comprise a 14-3-3-dependent ADP-ribosyltransferase domain.

192 ues 23 to 157) replaces the cholera toxin A1 ADP-ribosyltransferase domain.

193 sidues 234-453 comprise the 14-3-3-dependent ADP-ribosyltransferase domain.

194 an N-terminal RhoGAP domain and a C-terminal ADP-ribosyltransferase domain.

195 ctivity, whereas the C terminus comprises an ADP-ribosyltransferase domain.

196 sidues 233-453 comprise the 14-3-3-dependent ADP-ribosyltransferase domain.

197 amino-terminal RhoGAP and a carboxy-terminal ADP-ribosyltransferase domain.

198 e-activating protein (RhoGAP) and C-terminal ADP-ribosyltransferase domains.

199 e-regulating enzymes dinitrogenase reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductas

200 form a complex with dinitrogenase reductase ADP-ribosyltransferase (DRAT) from Rhodospirillum rubrum

201 genase reductase and dinitrogenase reductase ADP-ribosyltransferase (DRAT) from Rhodospirillum rubrum

202 sibly inactivated by dinitrogenase reductase ADP-ribosyltransferase (DraT) in response to an increase

203 ionally regulated by dinitrogenase reductase ADP-ribosyltransferase (DRAT) via ADP-ribosylation of th

204 ogenase reductase by dinitrogenase reductase ADP-ribosyltransferase (DRAT).

205 is a member of the adenosine 5'-diphosphate (ADP)-ribosyltransferase ectoenzyme gene family.

206 Depending on the family member, ADP-ribosyltransferases either conjugate a single ADP-ri

207 the first structure of a DNA-targeting mono-ADP-ribosyltransferase enzyme; the structures of the apo

208 This unusual finding, of two ADP-ribosyltransferase enzymes produced by a microorgani

209 with a nonphosphorylated protein ligand, the ADP-ribosyltransferase Exoenzyme S (ExoS) from Pseudomon

210 structural genes, exoS, encoding the 49-kDa ADP-ribosyltransferase (ExoS), and exoT, encoding the 53

211 Pseudomonas aeruginosa produces two ADP-ribosyltransferases, exotoxin A and exoenzyme S (Exo

212 ARTC2.2 is a toxin-related, GPI-anchored ADP-ribosyltransferase expressed by murine T cells.

213 wed that CerADPr possessed several conserved ADP-ribosyltransferase features, including an alpha-3 he

214 Cholix toxin is an ADP-ribosyltransferase found in non-O1/non-O139 strains

215 other target protein, exoenzyme S (ExoS), an ADP-ribosyltransferase from Pseudomonas aeruginosa.

216 , and initial characterization of a secreted ADP-ribosyltransferase, halovibrin (gene designation hvn

217 HopPtoG, HopPtoH, HopPtoI, and HopPtoS1 (an ADP-ribosyltransferase homolog).

218 re recognized by specific antibodies against ADP-ribosyltransferase in the coronary arterial homogena

219 and cysteine on proteins and is mediated by ADP-ribosyltransferases, including a subset commonly kno

220 ences, we have discovered >20 novel putative ADP-ribosyltransferases, including several new potential

221 ) hydrolysis assay, and 6.8 in the enzymatic ADP-ribosyltransferase inhibitor dose-response assay.

222 tion of P gamma arginine mutants, effects of ADP-ribosyltransferase inhibitors on the P gamma ADP-rib

223 conserved NAD(+)-dependent deacetylases and ADP-ribosyltransferases involved in the regulation of ce

224 ART-1, a cell surface ADP-ribosyltransferase, is imbedded in the membrane by a

225 3, which is ADP-ribosylated by an endogenous ADP-ribosyltransferase, is required for the phosphorylat

226 seudomonas aeruginosa exoenzyme S (ExoS), an ADP-ribosyltransferase, is translocated into eukaryotic

227 zation of a novel gene, ADPRTL1, encoding an ADP-ribosyltransferase-like protein.

228 ses a 591-aa virulence factor with both mono-ADP ribosyltransferase (mART) and vacuolating activities

229 The mono-ADP-ribosyltransferase (mART) toxins are contributing fa

230 structure suggested that the toxin is a mono-ADP-ribosyltransferase (mART).

231 is a substrate for two enzyme families, mono-ADP-ribosyltransferases (mARTs) and poly(ADP-ribose) pol

232 A putative mono-ADP-ribosyltransferase motif critical for the ubiquitina

233 a recently discovered arginine-specific mono-ADP-ribosyltransferase on cytotoxic T cells (CTL).

234 ylase activity but functions as an efficient ADP-ribosyltransferase on histones and bovine serum albu

235 ART2 is an ADP-ribosyltransferase on naive CD4+ and CD8+ T cells.

236 CerADPr(E431D) did not possess ADP-ribosyltransferase or NAD glycohydrolase activities

237 Here we find that the ADP-ribosyltransferases Parp1 and Parp7 play a critical

238 Here, we identify the mono-ADP-ribosyltransferase PARP10/ARTD10 as a novel PCNA bin

239 We show that the mono-ADP-ribosyltransferase PARP14 interacts with the DNA rep

240 We reported that ART1, a mammalian ADP-ribosyltransferase, present in epithelial cells lini

241 ermeable pores through which iota a (Ia), an ADP-ribosyltransferase, presumably enters the cytosol.

242 Exoenzyme S (ExoS) is an ADP-ribosyltransferase produced and directly translocate

243 ADP-ribosyltransferases promote repair of DNA single str

244 f conserved NAD(+)-dependent deacetylases or ADP-ribosyltransferases, promote longevity in diverse or

245 e catalytic domains of the nuclear-localized ADP-ribosyltransferase proteins (Adprt), two recently id

246 analyses of Tse6 show that it resembles mono-ADP-ribosyltransferase proteins, such as diphtheria toxi

247 ide donor S-nitrosoglutathione and enzymatic ADP-ribosyltransferase PtxS1-subunit of pertussis toxin,

248 Here we characterize Parp9, a mono-ADP-ribosyltransferase reported to be enzymatically inac

249 e type III-secreted effector HopU1 is a mono-ADP-ribosyltransferase required for full virulence on Ar

250 f membrane proteins on mouse T cells by ecto-ADP-ribosyltransferase(s) (ARTs) can down-regulate proli

251 Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophil

252 Exoenzyme S (ExoS) is a mono-ADP-ribosyltransferase secreted by the opportunistic pat

253 owever, inhibition of adenosine diphosphate (ADP) ribosyltransferase significantly decreased the resp

254 Mammalian cells contain ADP-ribosyltransferases similar to CT and an ADP-ribosyl

255 Rod ADP-ribosyltransferase solubilized from membranes by pho

256 cient in the production of the streptococcal ADP-ribosyltransferase SpyA generates lesions of reduced

257 bonded heterohexamers in which the catalytic ADP-ribosyltransferase subunit is activated when exposed

258 eversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicot

259 These data suggest that proteolysis of ADP-ribosyltransferase synthesized in transformed NMU ce

260 We identify the ADP-ribosyltransferase tankyrase (TNKS) and the 19S asse

261 The ADP-ribosyltransferase TccC3 from the insect bacterial p

262 amino acid homology with the vertebrate mono-ADP-ribosyltransferases than the bacterial ADP-ribosyltr

263 amily of macrodomain-containing PARPs--is an ADP ribosyltransferase that interacts with Stat6, enhanc

264 acetylases (HDACs), are protein deacetylases/ADP ribosyltransferases that target a wide range of cell

265 tify EspJ as a unique adenosine diphosphate (ADP) ribosyltransferase that directly inhibits Src kinas

266 An adenosine diphosphate (ADP)-ribosyltransferase that causes actin cytoskeletal d

267 experiments identify CerADPr as a cytotoxic ADP-ribosyltransferase that disrupts the host cytoskelet

268 subgenomic recombinant Sindbis virus C3), an ADP-ribosyltransferase that inactivates Rho, or dominant

269 s syringae type III effector HopU1 is a mono-ADP-ribosyltransferase that is injected into plant cells

270 a binary toxin consisting of iota a (Ia), an ADP-ribosyltransferase that modifies actin, and iota b (

271 udomonas aeruginosa exoenzyme S (ExoS) is an ADP-ribosyltransferase that modifies low-molecular-weigh

272 PT is an ADP-ribosyltransferase that modifies several mammalian h

273 SIRT3-5, are NAD(+)-dependent deacylases and ADP-ribosyltransferases that are critical for stress res

274 Mammalian cells contain mono-ADP-ribosyltransferases that catalyze the formation of A

275 Tankyrases are ADP-ribosyltransferases that play key roles in various c

276 ily of protein deacetylases, deacylases, and ADP-ribosyltransferases that regulate life span, control

277 er reduced liver injury, and animals lacking ADP-ribosyltransferase, the enzyme that uses NAD to atta

278 HIF-1 promotes the transcription of an ADP ribosyltransferase, TiPARP, which serves to deactiva

279 uctures of the Pierisin subgroup of the mono-ADP-ribosyltransferase toxin family.

280 xigenic Escherichia coli (ETEC) produces the ADP-ribosyltransferase toxin known as heat-labile entero

281 Each bacterial ADP-ribosyltransferase toxin modifies a specific host pr

282 ce identity with the Pierisin family of mono-ADP-ribosyltransferase toxins.

283 de a protein, SpyA, with homology to C3-like ADP-ribosyltransferase toxins.

284 n of these toxins requires their activity as ADP-ribosyltransferases, transferring the ADP-ribose moi

285 ase features, including an alpha-3 helix, an ADP-ribosyltransferase turn-turn loop, and a "Gln-XXX-Gl

286 tive insecticidal protein 2 (VIP2), an actin ADP-ribosyltransferase, unexpectedly implicates two adja

287 ADP-ribosylation is a PTM, in which ADP-ribosyltransferases use nicotinamide adenine dinucle

288 Mouse ART2, which is an NAD:arginine ADP-ribosyltransferase, was able to modify HNP-1, but to

289 24 mum PJ34, a well known inhibitor of poly-ADP-ribosyltransferases, was shown to be the most potent

290 unusual target for modification by bacterial ADP-ribosyltransferases, we quantitatively compared the

291 rase (PDE), is ADP-ribosylated by endogenous ADP-ribosyltransferase when P gamma is free or complexed

292 hese data identify ExoS as a biglutamic acid ADP-ribosyltransferase, where E381 is the catalytic resi

293 7) are NAD(+)-dependent protein deacetylases/ADP ribosyltransferases, which play decisive roles in ch

294 The latter is an ADP-ribosyltransferase, which activates the alpha-subuni

295 Exoenzyme S of Pseudomonas aeruginosa is an ADP-ribosyltransferase, which is secreted via a type III

296 e T cells expressing the cell surface enzyme ADP ribosyltransferase with nicotinamide adenine dinucle

297 PARP14 is an ADP-ribosyltransferase with multiple roles in transcript

298 Sirtuins are a family of deacylases and ADP-ribosyltransferases with clear links to regulation o

299 DP-ribose) polymerase (PARP) family includes ADP-ribosyltransferases with diphtheria toxin homology (

300 was generated in NMU cells by proteolysis of ADP-ribosyltransferase, with release of a carboxyl-termi