ライフサイエンスコーパス: deiminase

1 second reservoir, containing the enzyme CRE deiminase.

2 ated by esophagus-enriched peptidyl arginine deiminases.

3 itretin partly restored the peptidylarginine deiminase 1 defect caused by IL-22.

4 d to suppress expression of peptidylarginine deiminase 1 in epidermal keratinocytes.

5 ulates expression of PADI1 (Protein Arginine Deiminase 1) and PADI3 in multiple cancer cell types mod

6 , we show reduced levels of peptidylarginine deiminase 1, an enzyme that converts peptidylarginine in

7 of semaphorin 4D (SEMA4D), peptidylarginine deiminase 2 (PAD2) and matrix metalloproteinase-8 (MMP-8

8 el) interacting partners of protein arginine deiminase 2 (PAD2) and pyruvate dehydrogenase kinase 1 (

9 Protein arginine deiminase 2 (PAD2) plays a key role in the onset and pro

10 rate that the expression of peptidylarginine deiminase 2 (PAD2), an enzyme that catalyzes protein cit

11 Peptidyl arginine deiminase 2 (PAD2), an enzyme that converts protein argi

12 of Cit-Vim in an Akt1- and peptidylarginine deiminase 2 (PAD2)-dependent manner.

13 Peptidylarginine deiminase 2 (PAD2/PADI2) has been implicated in various

14 onversion to citrulline by peptidyl arginine deiminase 2 (PADI2), an enzyme that has been associated

15 nced gene expression of the peptidylarginine deiminase 2 gene, itself a chromatin-modifying protein.

16 expression and activity of peptidylarginine deiminase 2, one of the five enzymes responsible for cit

17 neutrophils or recombinant protein arginine deiminases 2 or 4 at 37 degrees C resulted in its rapid

18 of semaphorin-4D (SEMA-4D), peptidylarginine deiminase-2 (PAD-2), and matrix metalloproteinase-8 (MMP

19 Peptidyl arginine deiminase-2 and cyclic nucleotide phosphodiesterase are

20 ain of LRP1 is a target of peptidyl arginine deiminase-2-mediated deimination in vitro.

21 dotoxic mice with YW3-56, a peptidylarginine deiminase-2/4 inhibitor, significantly diminished levels

22 ly 1 gene (PADI3, encoding peptidyl arginine deiminase 3) has been thus far associated with CCCA.

23 d in the three genes PADI3 (peptidylarginine deiminase 3), TGM3 (transglutaminase 3), and TCHH (trich

24 ied citrullination sites in protein arginine deiminase 4 (12 sites) and in fibrinogen (25 sites, two

25 ulline with recombinant polypeptide arginine deiminase 4 (PAD4) abolished ADAMDEC1-catalyzed pro-EGF1

26 n NET formation, including peptidyl arginine deiminase 4 (PAD4) activity, neutrophil nuclear histone

27 ination of core histones by peptidylarginine deiminase 4 (PAD4) and that patients with autoimmune dis

28 (GCF) levels of galectin-3, peptidylarginine deiminase 4 (PAD4) and tumor necrosis factor-alpha (TNF-

29 (GCF) levels of galectin-3, peptidylarginine deiminase 4 (PAD4) and tumor necrosis factor-alpha (TNF-

30 Unlocking the potential of protein arginine deiminase 4 (PAD4) as a drug target for rheumatoid arthr

31 Peptidylarginine deiminase 4 (PAD4) citrullinates histones and is require

32 citrullination catalyzed by peptidylarginine deiminase 4 (PAD4) correlates with chromatin decondensat

33 Protein arginine deiminase 4 (PAD4) facilitates the post-translational ci

34 critical role of neutrophil peptidylarginine deiminase 4 (PAD4) in neutrophil migration in cancer.

35 ional experiments implicate protein arginine deiminase 4 (PAD4) in the pathogenesis of rheumatoid art

36 sumed role of an overactive protein arginine deiminase 4 (PAD4) in the pathophysiology of rheumatoid

37 phages in the presence of a peptidylarginine deiminase 4 (PAD4) inhibitor reduced TNF-alpha and IL-6

38 mmunotherapeutic synergy of protein arginine deiminase 4 (PAD4) inhibitors, which curtail NETosis wit

39 Protein arginine deiminase 4 (PAD4) is a Ca(2+)-dependent enzyme that cat

40 Peptidylarginine deiminase 4 (PAD4) is a Ca(2+)-dependent enzyme that con

41 Protein arginine deiminase 4 (PAD4) is a transcriptional coregulator that

42 Peptidylarginine deiminase 4 (PAD4) is an enzyme that citrullinates histo

43 Peptidylarginine deiminase 4 (PAD4) is associated with NETosis by increas

44 rullination of histones by peptidyl arginine deiminase 4 (PAD4) is central for NET formation in vivo.

45 t targeting of NETs via the peptidylarginine deiminase 4 (PAD4) mechanism was insufficient to reduce

46 trullination and NETosis by peptidylarginine deiminase 4 (PAD4) on MI/R.

47 , we demonstrate that human peptidylarginine deiminase 4 (PAD4) regulates histone Arg methylation by

48 t of specific inhibitors of protein-arginine deiminase 4 (PAD4), an enzyme required for NET formation

49 phil-specific deficiency of peptidylarginine deiminase 4 (PAD4), an enzyme that is essential for NET

50 tiation factor 88 (MYD88), peptidyl arginine deiminase 4 (PAD4), and gasdermin D (GSDMD) for NET form

51 [NETosis]), orchestrated by peptidylarginine deiminase 4 (PAD4), damages organs in acute inflammatory

52 histones, generated by the peptidylarginine deiminase 4 (PAD4), is synonymous with NETosis and is co

53 dy investigated the role of peptidylarginine deiminase 4 (PAD4), neutrophil extracellular traps (NETs

54 Peptidyl arginine deiminase 4 (PAD4), which binds proteins and citrullinat

55 hils express high levels of peptidylarginine deiminase 4 (PAD4), which catalyzes histone citrullinati

56 analyzed venous thrombi in peptidylarginine deiminase 4 (PAD4)-deficient mice that cannot citrullina

57 ates the regulatory role of peptidylarginine deiminase 4 (PAD4)-mediated citrullination on the tumor

58 he calcium-activated enzyme peptidylarginine deiminase 4 (PAD4).

59 Intriguingly, knocking out peptidylarginine deiminase 4 (PAD4, a key enzyme for NET formation) or DN

60 Expression of peptidylarginine deiminase 4 (PAD4, encoded by Padi4 in mice), an enzyme

61 autocitrullination sites in Protein Arginine Deiminase 4 (PAD4, R372 and R374) and show that the R372

62 Peptidylarginine deiminase 4 (PAD4/PADI4) counteracts the functions of pr

63 Peptidylarginine deiminase 4 (PADI4) catalyzes the deimination of histone

64 apoptotic cancer cells in a peptidylarginine deiminase 4 (Padi4) dependent manner.

65 Peptidyl arginine deiminase 4 (PADI4) inhibition in mice blocked NETosis a

66 t gene and binding partner peptidyl-arginine deiminase 4 (PADI4).

67 lular traps (NETs) through peptidyl arginine deiminase 4 (PADI4).

68 Peptidylarginine deiminase 4 deficiency prevents heart failure and preser

69 functional haplotype of the peptidylarginine deiminase 4 gene (PADI4) has recently been identified as

70 Here, we report that peptidylarginine deiminase 4, a histone citrullination enzyme, is involve

71 Inhibition of protein arginine deiminase 4, an enzyme important for the release of neut

72 Peptidylarginine deiminase 4, an enzyme that mediates chromatin decondens

73 enzyme initiating NETosis, peptidylarginine deiminase 4, and activates the NOD-like receptor family,

74 duced by citrullination by peptidyl arginine deiminase 4, or digestion by serine proteases.

75 tion mark of p300 GBD is removed by peptidyl deiminase 4, thereby enhancing the p300-GRIP1 interactio

76 Neutrophils from peptidylarginine deiminase 4-(PAD4(-/-)) deficient mice, which lack the e

77 r trap formation involving peptidyl arginine deiminase 4.

78 histone citrullination by peptidyl arginine deiminase-4 (PADI4) in contact to particulate agents to

79 PAD4 (protein-arginine deiminase-4) is a calcium-dependent enzyme that is essen

80 s via DNase infusion, or in peptidylarginine deiminase-4-deficient mice (which have impaired NET prod

81 e nuclear DNA catalyzed by peptidyl arginine deiminase-4.

82 (64 kDa) and trimeric reactive intermediate deiminase A (RidA, 43 kDa) were detected.

83 Arginine deiminase accelerates substrate hydrolysis 6 x 10(12)-fo

84 termined that strain 1457 devoid of arginine deiminase activity (1457 DeltaADI) was significantly les

85 Subsequently, total peptidylarginine deiminase activity and extent of protein deimination in

86 Protein arginine deiminase activity depends on high intracellular calcium

87 ant Manfredo strains for the enzyme arginine deiminase (AD) showed that significant activity was pres

88 L-arginine deiminase (ADI) catalyzes the hydrolysis of L-arginine t

89 Arginine deiminase (ADI) catalyzes the hydrolytic conversion of L

90 L-arginine deiminase (ADI) catalyzes the irreversible hydrolysis of

91 l-Arginine deiminase (ADI) catalyzes the irreversible hydrolysis of

92 o evaluate the effects of pegylated arginine deiminase (ADI) in terms of toxicity, tumor response, al

93 Arginine deiminase (ADI) inhibits growth in various ASS-deficient

94 on the use of recombinant bacterial arginine deiminase (ADI) isolated from the cells of a recombinant

95 rcA2) to assess the function of the arginine deiminase (ADI) pathway in organic acid resistance and b

96 of the amino acid arginine via the arginine deiminase (ADI) pathway supplements energy production an

97 le to therapeutic intervention with arginine deiminase (ADI), an enzyme responsible for consuming the

98 rginine deprivation using pegylated arginine deiminase (ADI-PEG 20) against primary AMLs in a xenogra

99 Purpose Pegylated arginine deiminase (ADI-PEG 20) depletes essential amino acid lev

100 arginine-degrading enzyme pegylated arginine deiminase (ADI-PEG 20).

101 arginine deprivation with pegylated arginine deiminase (ADI-PEG20) as a therapeutic.

102 e arginine-lowering agent pegylated arginine deiminase (ADI-PEG20) has not been evaluated in a random

103 The development of pegylated arginine deiminase (ADI-PEG20) has renewed interest in arginine d

104 ding recombinant protein, pegylated arginine deiminase (ADI-PEG20), has been in clinical trials for t

105 o arginine depletion with pegylated arginine deiminase (ADI-PEG20).

106 Arginine deiminase (ADI; EC 3.5.3.6.), an arginine-degrading enzy

107 ying enzymes (GMEs) consists of the agmatine deiminases (AgDs).

108 u2ABCA' that contains two genes for agmatine deiminases (agu2A and agu2A').

109 ing ornithine carbamoyltransferase, arginine deiminase, alpha-enolase, and alpha- and beta-giardins,

110 transcript levels of genes encoding arginine deiminase and a putative serine dehydratase.

111 Arginase, arginine deiminase and arginine decarboxylase are potential enzym

112 se 2 randomized clinical trial, the Arginine Deiminase and Mesothelioma (ADAM) study, was conducted b

113 s of polyamine biosynthetic enzymes agmatine deiminase and N-carbamoylputrescine amidohydrolase in ar

114 e anr gene (anaerobic regulation of arginine deiminase and nitrate reduction) that controls anaerobic

115 of arginine deprivation (pegylated arginine deiminase) and chemotherapy (cisplatin), offering new in

116 or acetaldehyde dehydrogenase ExaC, arginine deiminase ArcA, and glyceraldehyde 3-phosphate dehydroge

117 s and P. gingivalis, and identified arginine deiminase (ArcA) of S. cristatus as the signaling molecu

118 erived from Streptococcus cristatus arginine deiminase (ArcA) was able to repress the expression and

119 ent mutants were constructed within arginine deiminase (arcA1 and arcA2) to assess the function of th

120 wo coupled recognition modules, a creatinine deiminase (CD) enzyme and a 2-nitrophenol (2NPh) titrati

121 protein cross-linking) and peptidyl-arginine deiminase (conversion of arginines to citrullines with l

122 In peptidyl arginine deiminase-deficient mice, not forming NETs, inflammation

123 eactive oxygen species- and peptidylarginine deiminase-dependent pathways.

124 sed as transducer and immobilized creatinine deiminase (EC 3.5.4.21)--as a biosensitive element.

125 he citrulline formed by the peptidylarginine deiminase enzyme modification functions to unfold protei

126 y (t(1/2)=4.8h) whereas a bacterial arginine deiminase evaluated in phase II clinical trials was repo

127 activity correlates with levels of arginine deiminase expression in S. cristatus.

128 The peptidylarginine deiminase family member PAD4 (also called PADI4) is mark

129 ial kinetic characterization of the agmatine deiminase from Helicobacter pylori and described the syn

130 L-Arginine deiminase from Pseudomonas aeruginosa (PaADI) catalyzes

131 film assays of mutants of all three agmatine deiminase genes in PA14 revealed that deletion of agu2AB

132 nd highly upregulated expression of arginine deiminase genes were observed in the double mutant.

133 Peptidyl arginine deiminases have been shown to be hyperactive in neurodeg

134 biofilm growth and the function of arginine deiminase in USA300 clones led us to genetically inactiv

135 Peptidylarginine deiminase inhibition blocked NET formation, reduced athe

136 Peptidylarginine deiminase inhibition is a strategy that can decrease in

137 injections of Cl-amidine, a peptidylarginine deiminase inhibitor.

138 Peptidylarginine deiminase IV (PAD4), one of the key enzymatic drivers of

139 Peptidylarginine deiminase IV (PADI4, PAD4) deregulation promotes the dev

140 tion network and identified peptidylarginine deiminases, kallikreins, serine proteinase inhibitor fam

141 for egg and embryo-abundant peptidylarginine deiminase-like protein.

142 n be solubilized following peptidyl-arginine deiminase modification.

143 lly inactivate the sole copy of the arginine deiminase operon by deleting the arginine/ornithine anti

144 n P. aeruginosa GMSF enzymes PaADI, agmatine deiminase (PaAgDI), and N(omega),N(omega)-dimethylargini

145 on of H3R26 is catalyzed by peptidylarginine deiminase (PAD) 2 and not by PAD4 (which citrullinates H

146 Peptidyl arginine deiminase (PAD) catalyzes the post-translational citrull

147 d was PAD3, a member of the peptidylarginine deiminase (PAD) enzyme family that converts protein argi

148 al to the calcium-dependent peptidylarginine deiminase (PAD) enzyme family.

149 Peptidyl arginine deiminase (PAD) enzymes are a known modifier of proteoly

150 Protein arginine deiminase (PAD) enzymes catalyze the conversion of prote

151 protein or influencing the peptidylarginine deiminase (PAD) enzymes found in the monocyte/macrophage

152 he citrulline amino acid by protein arginine deiminase (PAD) family members.

153 the first purification of a peptidylarginine deiminase (PAD) from a prokaryote.

154 ly found that Cl-amidine, a peptidylarginine deiminase (PAD) inhibitor, improves survival in a mouse

155 vivo, LL-37 is exposed to peptidyl arginine deiminase (PAD), an enzyme released by inflammatory cell

156 spectrometric sequencing of peptidylarginine deiminase (PAD)-modified protein.

157 pendent on the activity of peptidyl arginine deiminase (PAD).

158 o histone citrullination by protein arginine deiminase (PAD)4, exocytosis of chromatin and enzymes as

159 se (DDAH); EC 3.5.3.18] and peptidylarginine deiminase (PAD; EC 3.5.3.15) catalyze hydrolysis of subs

160 Protein arginine deiminases (PAD) 4 is an enzyme that catalyzes citrullin

161 Peptidylarginine deiminases (PAD) convert cationic peptidyl arginine to n

162 Cl-amidine, an inhibitor of peptidylarginine deiminases (PAD), to block NET formation and were evalua

163 arginine, are generated by peptidyl arginine deiminases (PAD).

164 Peptidylarginine deiminases (PAD1-4) are calcium dependent enzymes respon

165 arginine to citrulline by peptidyl arginine deiminase (PAD4), change protein structure and function.

166 Peptidylarginine deiminase (PADI) enzymes are increasingly being associat

167 Citrullinating peptidylarginine deiminase (Padi) enzymes were expressed in murine and hu

168 Peptidylarginine deiminases (PADI) catalyze posttranslational modificatio

169 e proteins and bone-marrow-specific arginine deiminase PADI4.

170 c vertebrate enzymes called peptidylarginine deiminases (PADIs) and is associated with the developmen

171 The protein arginine deiminases (PADs) are a family of enzymes that catalyze

172 Peptidylarginine deiminases (PADs) are enzymes that convert arginine to c

173 Protein arginine deiminases (PADs) catalyze the hydrolysis of peptidyl ar

174 Protein arginine deiminases (PADs) catalyze the post-translational hydrol

175 Peptidylarginine deiminases (PADs) have an important role in the pathogen

176 Protein arginine deiminases (PADs) hydrolyze the side chain of arginine t

177 rains lacking the bacterial peptidylarginine deiminases (PADs) or gingipains were created to assess t

178 Peptidylarginine deiminases (PADs), a family of calcium-dependent enzymes

179 ated via the actions of the protein arginine deiminases (PADs), are known to develop in the murine co

180 a family of enzymes called peptidylarginine deiminases (PADs), is the conversion of arginine into ci

181 oantibodies are produced by protein arginine deiminases (PADs), particularly PAD4.

182 that systemic inhibition of peptidylarginine deiminases (PADs), the enzymes mediating citrullination,

183 he reaction is catalyzed by peptidylarginine deiminases (PADs), which are found in vertebrates but no

184 f arginine-to-citrulline by protein arginine deiminases (PADs), whose dysregulation is implicated in

185 group of enzymes called the protein arginine deiminases (PADs).

186 vels of arginine catabolism via the arginine deiminase pathway (ADS), acidogenicity, and global metab

187 ATL included those involved in the arginine deiminase pathway and a total of 140 carbohydrate transp

188 ile genetic element that encodes an arginine deiminase pathway and an oligopeptide permease system th

189 e in the expression of genes in the arginine deiminase pathway during stringent response activation.

190 hrough pyruvate fermentation or the arginine deiminase pathway, and we add lineages capable of molecu

191 ginine catabolism by enzymes of the arginine deiminase pathway, encoded by the arcDABC operon.

192 ed to be unrelated to ArcD from the arginine deiminase pathway.

193 e phosphorylation and ATP-providing arginine deiminase pathway.

194 of Porphyromonas gingivalis peptidylarginine deiminase (PPAD) can influence citrullination of protein

195 y of a unique P. gingivalis peptidylarginine deiminase (PPAD) produced by this bacterium, which is ca

196 One of these is peptidylarginine deiminase (PPAD), an enzyme unique to P. gingivalis amon

197 Padi family, encoding the peptidyl arginine deiminases responsible for citrulline protein modificati

198 metabolism by oral bacteria via the arginine deiminase system (ADS) increases the local pH, which can

199 The arginine deiminase system (ADS) is associated with arginine catab

200 The arginine deiminase system (ADS) is responsible for the production

201 The arginine deiminase system (ADS) of S. gordonii enables cells to p

202 occus mutans expresses a functional agmatine deiminase system (AgDS) encoded by the agmatine-inducibl

203 An operon encoding enzymes of the agmatine deiminase system (AgDS) has been identified in the cario

204 Induction of the agmatine deiminase system (AgDS) of Streptococcus mutans requires

205 that the constitutive ACME-encoded arginine-deiminase system (Arc) allows USA300 to thrive in acidic

206 sion and anaerobic induction of the arginine deiminase system.

207 thine produced by species using the arginine deiminase system.

208 , both arginine-free conditions and arginine deiminase treatment were demonstrated to kill fibrotic f

209 and the deiminating enzymes peptidylarginine deiminase type 2 (PAD-2) and PAD-4.

210 he citrullinating enzymes, peptidyl arginine deiminase type 4 (PAD-4), is genetically associated with

211 citrullinated proteins and peptidylarginine deiminase type 4 (PAD-4).

212 Inhibition of protein-arginine deiminase type 4 (PAD4), a regulator of NETosis, had no

213 ormation via inhibition of peptidyl arginine deiminase type 4 or abrogation of reactive oxygen specie

214 phil elastase (NE(-/-)) or peptidyl arginine deiminase type IV (Pad4(-/-)) (enzymes that formation of

215 apping studies of neonatal peptidyl arginine deiminase type IV (Padi4)-specific thymocytes reveal dis

216 PAD4 (peptidylarginine deiminase type IV), an enzyme essential for neutrophil e

217 lactosaminyltransferase 3, peptidyl arginine deiminase type-2, and interleukin-15 receptor subunit a.

218 up to 5.6%.) PADI3 encodes peptidyl arginine deiminase, type III (PADI3), an enzyme that post-transla

219 plets is first modified by peptidyl-arginine deiminase which denatures it and makes it more soluble.

220 termed PPAD (Porphyromonas peptidylarginine deiminase), which is genetically unrelated to eukaryotic

221 Peptidylarginine deiminases, which are commonly found in mammalian cells,

222 signaling and activation of peptidylarginine deiminase with the resultant increased cellular abundanc