ライフサイエンスコーパス: arginine residue

1 ssociation of an 8-aa fragment with a single arginine residue.

2 oove, primarily through a deeply penetrating arginine residue.

3 minus and a noncovalent interaction with the arginine residue.

4 ith concomitant covalent modification of the arginine residue.

5 mpartment of which 12 contained at least one arginine residue.

6 l was the side chain guanidine moiety of the arginine residue.

7 ations are heterozygous, and affect a single arginine residue.

8 the substrate makes with a highly conserved arginine residue.

9 isassembly of the active site mediated by an arginine residue.

10 l but significant contribution from a single arginine residue.

11 t by strict spatial localization of specific arginine residues.

12 post-translational hydrolytic deimination of arginine residues.

13 nduction, was determined to be methylated at arginine residues.

14 ligands are indeed able to interact with the arginine residues.

15 nzymatic digestion specifically at lysine or arginine residues.

16 trates with N-acetyl glucosamine (GlcNAc) on arginine residues.

17 Cdelta that incorporate one or more of these arginine residues.

18 at the side chain amino groups of lysine and arginine residues.

19 ferase PRMT1, which methylates RACO-1 on two arginine residues.

20 similar shifts assignable to carboxylate and arginine residues.

21 at Thr-69 or a truncation of three terminal arginine residues.

22 hese factors are activated by methylation of arginine residues.

23 bscurin consists, in part, of six lysine and arginine residues.

24 nal stabilizing interactions provided by two arginine residues.

25 he CTD contains four clusters of consecutive arginine residues.

26 boring sites, and that is rich in serine and arginine residues.

27 genetic modifications by methylating histone arginine residues.

28 nal peptides containing an essential pair of arginine residues.

29 onist interact preferentially with different arginine residues.

30 ltransferase that symmetrically dimethylates arginine residues.

31 alyse three distinct types of methylation on arginine residues.

32 Invariant arginine residues 144 and 435 positioned in the vicinity

33 terization of a novel motif containing three arginine residues (405RRR407) within the GABA(A)R beta3-

34 An inherited mutation converting arginine residue 9 in PLN to cysteine (R9C) results in d

35 ly, we have shown that replacements of these arginine residues abrogate the T2S process due to a redu

36 ther PTMs, such as methylation of lysine and arginine residues, acetylation, and nitrosylation of thi

37 A pair of arginine residues adjacent to the active site affect cat

38 tic studies showed that the substitutions at arginine residues affected the turnover of the enzyme si

39 We propose that an arginine residue allows for Zn(II) regulation in SmtB an

40 that TRIP8b binding to the CNBD required an arginine residue also necessary for cAMP binding.

41 nated peptides or proteins with at least one arginine residue and other basic residues, such as lysin

42 ved to disassemble into the fully unmodified arginine residue and pyruvate in aqueous solution.

43 We found that a specific arginine residue and several aromatic residues, as well

44 formed by stacking of the side chains of two arginine residues and by salt bridges formed between the

45 t interacts with pectin through a cluster of arginine residues and de-methylesterified pectin present

46 ontacts are found between charged lysine and arginine residues and DNA phosphate groups and other bin

47 protonated peptides containing at least two arginine residues and may also occur for large protonate

48 ified with hydroimidazolone modifications of arginine residues and products of their hydrolysis) by b

49 The mutations occur at specific arginine residues and result in the acquisition of a nov

50 residues within the cyclic peptide ring with arginine residues and shown to have antiproliferative ac

51 r-huPAD4 citrullinates ADAMTS13 on specific arginine residues and that this modification dramaticall

52 on between the positively charged lysine and arginine residues and the negatively charged phosphate g

53 istone methylation occurs on both lysine and arginine residues, and its dynamic regulation plays a cr

54 he tautomeric states of the SF histidine and arginine residues; and observe four SF water positions t

55 Remarkably, the flexible lysine or arginine residue appears to be a universal module that a

56 Proteins with methyl arginine residues are also enriched at the tip and base

57 Since arginine residues are frequently present within protein

58 aphy, we demonstrate that neither lysine nor arginine residues are methylated and that a 3-methylhist

59 electrostatics; within this code lysine and arginine residues are non-equivalent and prenyl chain le

60 The mutated arginine residues are part of a basic patch that is esse

61 Two conserved arginine residues are present in the active site: Arg-51

62 involving the mobile loops and the critical arginine residues Arg-182 and Arg-327.

63 l groups was explained by the presence of an arginine residue (Arg(105)) and tyrosine residue (Tyr(10

64 nd that matriptase cleaves APP at a specific arginine residue (Arg-102) both in vitro and in cells.

65 owever, the template pocket is not empty; an arginine residue (Arg-283) occupies the space vacated by

66 TM7 contains a buried arginine residue (Arg-735) that is essential for proton

67 Consistent with these models, two arginine residues (Arg(436) and Arg(440)) within the MA

68 The side chains of two highly conserved arginine residues (Arg(83) and Arg(110)) and a conserved

69 ral spectroscopy assays, we identified three arginine residues (Arg-97, Arg-277, and Arg-303) that ar

70 teraction and signaling, while a more remote arginine residue, Arg(261), was found to enhance these S

71 found that EHEC NleB1 glycosylated two GAPDH arginine residues, Arg(197) and Arg(200), and that these

72 Our results showed that two specific arginine residues, Arg-141 and Arg-120, are important fo

73 conserved catalytic pentad that includes two arginine residues, Arg-191 and Arg-308.

74 with mutation of one of six highly conserved arginine residues, Arg-69 in Sin, was partially rescued

75 ehydrogenase is mutated at a key active site arginine residue (Arg172 in IDH2) in many cancers, leadi

76 l for the transfer of N-acetylglucosamine to arginine residues (arginine-GlcNAcylation).

77 at mediate assembly, via interaction with an arginine residue at a similar register to these aspartic

78 ApoE4 contains an arginine residue at position 112, whereas apoE3 has a cy

79 An arginine residue at position 136 was found to be essenti

80 showed that the molecular determinant was an arginine residue at position 245 (R245) in its transmemb

81 This work identified the arginine residue at position 68 of L13a as being essenti

82 al cap of THIK-1 showed that mutation of the arginine residue at position 92, which is in the linker

83 he cleaved Eph isoforms and identified a key arginine residue at the cleavage site, in agreement with

84 whereas plasmin prefers a positively charged arginine residue at the corresponding position in its su

85 rminal ligation partner contains a lysine or arginine residue at the site of ligation.

86 ty, consisted of four peptides containing an arginine residue at their C-termini.

87 talytic activity and involves methylation of arginine residues at Akt consensus site motifs, which is

88 We then introduced arginine residues at all positions in the 12 TM segments

89 e active site, is blocked by RTB, we mutated arginine residues at or near the interface of RTB to det

90 lling the position of neighboring lysine and arginine residues at the membrane-water interface.

91 Arginine residues at the RTA/RTB interface are involved

92 Mutation of all six lysine and arginine residues between the NPXXY and residue 340 to g

93 , we demonstrate that Ash2L is methylated on arginine residues both in vitro and in cells.

94 vity filter are an intramembrane loop and an arginine residue, both highly conserved, which constrict

95 aB can be methylated reversibly on lysine or arginine residues by histone-modifying enzymes, includin

96 Modifications of arginine residues by methylglyoxal lead to two adducts (

97 , a low degree of citrullination of internal arginine residues by PPAD was also detected using mass s

98 BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase

99 by the catabolism of proteins methylated on arginine residues by protein arginine methyltransferases

100 tegrin receptor via modification of critical arginine residues by reactive carbonyl species (RCS) gly

101 mino acids and peptides containing lysine or arginine residues by using fluorescence spectroscopy, NM

102 al positive charges between the two constant arginine residues can give rise to extraordinary high SH

103 Methylated arginine residues can promote AGO2 protein degradation a

104 king of proteins by methyl group addition to arginine residues can promote their recognition by bindi

105 e (IDH)1 and IDH2 mutations at three hotspot arginine residues cause an enzymatic gain of function th

106 Here we examined the role of basic arginine residues common to aPKC pseudosubstrate sequenc

107 More importantly, the introduction of the arginine residue commonly found at this position in PA s

108 Conserved arginine residues comprise the substrate-binding pocket,

109 mbrane region of TARM1 contained a conserved arginine residue, consistent with association with a sig

110 s key proton donor/acceptor (Asp-684) and an arginine residue controlling the pKa of the aspartate.

111 We identified a highly conserved arginine residue critical for both the biochemical and c

112 propose that interaction of ligand with this arginine residue dictates conformational changes that mo

113 manner of DNA recognition, whereby only two arginine residues directly recognize the consensus seque

114 Several flagellar proteins are methylated on arginine residues during flagellar resorption; however,

115 avage from the serine and threonine (but not arginine) residues, during permethylation.

116 The two conserved arginine residues each tolerate one substitution that re

117 Neutralization of four arginine residues eliminated plasma membrane binding.

118 Arginine residues form a positively charged patch to bin

119 post-translational modifications of protein arginine residues found in nature.

120 r because its catalytic assembly requires an arginine residue from a neighboring subunit.

121 ose, individual free amino acids, lysine and arginine residues, glucosone, 1-deoxyglucosone, 3-deoxyg

122 gh interactions mediated in part by critical arginine residues, hydrophobicity at residue 29, and mul

123 To date, mutations in three active site arginine residues, IDH1 R132, IDH2 R172 and IDH2 R140, h

124 An arginine residue implicated in malonate binding by proka

125 Binding to Scap requires an arginine residue in exon 18 of SREBP2.

126 An arginine residue in the 49-kDa subunit is symmetrically

127 ealed that glutamate recognition requires an arginine residue in the base of the binding site, which

128 Here, we show that a highly conserved arginine residue in the C-terminal domain of diverse HPV

129 novo missense substitution in an equivalent arginine residue in the C-terminal helicase domain of SM

130 A hallmark of SH2 domains is the arginine residue in the conserved FLVR motif that forms

131 inhibition of immune activation required an arginine residue in the cytoplasmic domain that is criti

132 ubstitution (R704C) that targets a conserved arginine residue in the cytoplasmic sequence of all neur

133 chloroplasts, conserve either a lysine or an arginine residue in the equivalent position.

134 We find that the arginine residue in the FLVR motif does not directly con

135 We identify a crucial arginine residue in the GAF domain that is essential for

136 We identified a highly conserved arginine residue in the Jas motif that is critical for c

137 xamerization hot spot that is centered on an arginine residue in the NAD(+)-binding domain.

138 Another arginine residue in the PSST subunit is hydroxylated and

139 strom resolution revealed the presence of an arginine residue in the region otherwise occupied by cal

140 normal cell growth requires conversion of an arginine residue in the RNA polymerase II C-terminal dom

141 th the absence of a conserved Tyr(P)-binding arginine residue in the SH2 domain.

142 and depends on the presence of a particular arginine residue in the voltage sensor.

143 (-) T cells possessed a non-germline-encoded arginine residue in their CDR3alpha and CDR3beta loops,

144 e by substituting the highly conserved first arginine residue in transmembrane segment 4 (domain 1),

145 identify and unveil the role of a conserved arginine residue in trimeric dUTPases that meets all the

146 NAD+ intermediate was proposed to react with arginine residues in a proximity dependent manner.

147 that catalyze the mono- and dimethylation of arginine residues in a variety of proteins.

148 -end-tracking module, we find that conserved arginine residues in CLASP2 form extensive hydrogen-bond

149 CR) in C. rodentium) that modifies conserved arginine residues in death domain-containing host protei

150 5) catalyzes the symmetric di-methylation of arginine residues in histones H3 and H4, marks that are

151 ly, LMWP (Sequence: VSRRRRRRGGRRRR), with 10 arginine residues in its structure, could function as a

152 unique specificity of PRMT7 for methylating arginine residues in lysine- and arginine-rich regions.

153 iwi and Miwi2 via symmetrically dimethylated arginine residues in Miwi and Miwi2.

154 analysis in EC identified five dimethylated arginine residues in p65, four of which are uncharacteri

155 to see whether such effects are general for arginine residues in proteins that bind highly charged s

156 s modified by citrullination, which converts arginine residues in proteins to citrulline.

157 Methylation of arginine residues in proteins, an enzyme-mediated post-t

158 ble intermediate preferentially reacted with arginine residues in proximity to the NAD+ binding pocke

159 have been studied only for the two outermost arginine residues in S4 voltage sensor segments of domai

160 , La(3+) is displaced by outward movement of arginine residues in S4; La(3+), therefore, is not prese

161 d to generate only omega-N(G)-monomethylated arginine residues in small peptides, suggesting that it

162 ptidase activity, with a unique loop and two arginine residues in the active site cavity orienting th

163 Pitt-Hopkins syndrome mutations affect five arginine residues in the basic region, two of them (R569

164 Mutation of a pair of conserved arginine residues in the Dicer-2 PAZ domain blocked clea

165 Mutations affecting arginine residues in the fourth transmembrane helix (S4)

166 This amplification required arginine residues in the ICOSL cytoplasmic tail that rec

167 Replacement of all five (or certain) arginine residues in the pseudosubstrate sequence of PKC

168 HypoPP) result in loss of positively charged arginine residues in the S4 segments of either SCN4A or

169 at interrupts the series of regularly spaced arginine residues in the S4 voltage sensor.

170 We identify specific methylated arginine residues in the Scd6 RGG-motif in vivo We provi

171 Additionally, mutations of arginine residues in the Sug(1-19) tag suggest that the

172 d that human alpha2C-AR has a high number of arginine residues in the third intracellular loop and in

173 However, mutation of arginine residues in the TMH3-4-5-6 region (R4.60, R6.58

174 PIWI proteins via symmetrically dimethylated arginine residues in their N-terminal domain.

175 hat interact with two key positively charged arginine residues in transmembrane domains V and VII of

176 'molecular tweezer' specific for lysine and arginine residues, inhibits the formation of infectivity

177 s, as well as by converting already-glycated arginine residues into citrulline.

178 nal modification formed by the conversion of arginine residues into the citrulline amino acid by prot

179 the heterozygous, point mutations mapping to arginine residues involved in the substrate binding insp

180 Adjacent to the catalytic triad, another arginine residue is positioned to recognize the substrat

181 del expressing an RPS19 mutation in which an arginine residue is replaced with a tryptophan residue a

182 divalent metal ions, the side chain of this arginine residue is required for the precise positioning

183 methylation modification on histone protein arginine residues is a regulatory mechanism to control s

184 inding to peptides of alternating lysine and arginine residues (KR)n.

185 tely 90 bp of DNA through several lysine and arginine residues localized around its homodimerization

186 ed by the mutation of a single glycine to an arginine residue located in a loop of the protein.

187 When RTA is separated from RTB, arginine residues located at the interface are exposed t

188 hypokalaemic periodic paralysis mutations at arginine residues located below the gating pore constric

189 sic domain (PBD) composed of nine lysine and arginine residues located between the conserved N- and C

190 n an earlier study, a double mutation of two arginine residues located in a short cytoplasmic loop be

191 e first methyl group in M48L, especially for arginine residues located in the center of the peptide s

192 Positively charged arginine residues located in the flexible loop II were f

193 At low concentrations, genipin binds to arginine residues located in the UCP funnel, which leads

194 is the high-affinity GAG ligand, lysine and arginine residues located in two non-overlapping domains

195 mal DNA with a binding interface composed of arginine residues located within the ZnF alpha-helix.

196 Multiple arginine residues, located near the catalytic site and a

197 nd modeling studies indicate that lysine and arginine residues mediate binding and that they are loca

198 We next generated HSV-1 with the same pUS9 arginine residues mutated to asparagine (HSV-1pUS9KBDM)

199 at the introduction of a single lipid-facing arginine residue near the middle of the beta barrel of t

200 yses, we also demonstrated the importance of arginine residues near the membrane interface, which may

201 The insert coded for three arginine residues, occurred in a region associated with

202 om Escherichia coli, revealed that the basic arginine residue of the mutant G87R points toward the me

203 compounds explain the mechanism by which an arginine residue of the phosphagen specificity loop is c

204 phospholipids stabilize two voltage-sensing arginine residues of certain voltage-gated potassium cha

205 together, our results identify the conserved arginine residues of EYA1 that play an important role fo

206 N-methylated (both mono- and di-methylated) arginine residues of histones and other proteins, includ

207 T responsible for symmetric dimethylation of arginine residues of histones and other proteins.

208 h the addition of methyl groups to lysine or arginine residues of histones H3 and H4 by means of hist

209 e that forms adducts on cysteine, lysine and arginine residues of proteins, thereby affecting their f

210 and 91 of the 23S rRNA and interacting with arginine residues of ribosomal protein L16.

211 introduction of monomethylation marks at the arginine residues of substrate proteins.

212 of potassium channels proposed that the four arginine residues of the voltage-sensing S4 helix (left)

213 T3 catalyzes the asymmetric dimethylation of arginine residues of various proteins.

214 Highly conserved and essential arginine residues, often called arginine fingers, are lo

215 nes by catalyzing symmetric dimethylation of arginine residues on histone tails.

216 nal silencing of target genes by methylating arginine residues on histone tails.

217 ic regulator that symmetrically dimethylates arginine residues on histones H3 and H4 to silence gene

218 target genes via symmetric dimethylation of arginine residues on histones H4R3, H3R8 and H2AR3.

219 uantitate changes in methylation of specific arginine residues on hnRNP-A1.

220 nsferase (PRMT) 9 symmetrically dimethylates arginine residues on splicing factor SF3B2 (SAP145) and

221 he two-terminal omega-guanidino nitrogens of arginine residues on substrate proteins.

222 ltransferase that symmetrically dimethylates arginine residues on target proteins to alter target pro

223 Two arginine residues on the opposite face of the molecule (

224 inine methyltransferase 7 (PRMT7) methylates arginine residues on various protein substrates and is i

225 ing predicted the contributions of different arginine residues, other than at 3.36, in human GPR35 fo

226 Of two arginine residues paired on one face of HD5, Arg-28 is c

227 re we report that protein phosphorylation on arginine residues plays a physiologically significant ro

228 ne amino acids of p5 have been replaced with arginine residues predisposing the peptide toward the al

229 by Arg583 and Arg587, while four additional arginine residues present within the same regulatory hel

230 differentially affected by mutations of two arginine residues, previously found to be important for

231 lly cleave proteins C-terminal to lysine and arginine residues prior to LCMS/MS analysis of the resul

232 tion of mono- and symmetrically dimethylated arginine residues, PRMT5 is also mechanistically unique.

233 The strictly conserved arginine residue proximal to the active site tyrosine of

234 nd results in the preferential alkylation of arginine residues proximal to the NAD+ binding pocket.

235 Mutations at the arginine residue (R132) in isocitrate dehydrogenase 1 (I

236 (IDH2) mutations, which occur at active site arginine residues R140 and R172.

237 synthetase (GshB) is glycosylated by NleB on arginine residue R256.

238 Mutation of a conserved arginine residue (R298S) in the cytosolic domain of NBCe

239 Here, we demonstrate that 2 conserved arginine residues, R304 and R306, of EYA1 are essential

240 R01 acts by binding to the target lysine and arginine residues rather than by a non-specific, colloid

241 A competitive inhibitor rich in arginine residues reduced the number of enzymatic cleava

242 Substitutions of this arginine residue rendered mTORC1 signaling insensitive t

243 equence motifs with successive lysine and/or arginine residues represent a source of missed cleaved s

244 tramolecular interactions with and sequester arginine residues required for EB1 binding.

245 hat catalyzes the symmetric dimethylation of arginine residues (Rsme2).

246 The simulations showed that numerous arginine residues scattered throughout the FnIII surface

247 rate recognition motif consists of a pair of arginine residues separated by one residue (RXR motif).

248 binding to p32, and mutation of these three arginine residues significantly weakened the replication

249 y a charged linker region rich in serine and arginine residues (SR linker).

250 y a charged linker region rich in serine and arginine residues (SR-rich linker).

251 -synonymous mutations specifically targeting arginine residues, SRGAP2C is unique compared to SRGAP2B

252 -fit substrate binding mechanism mediated by arginine residue switching between salt bridge and pi-pi

253 In solution, however, the arginine residues tend to be protonated at pH values low

254 (called R704C), which mutates a cytoplasmic arginine residue that is conserved in all neuroligins.

255 We identify an arginine residue that is critical for ligand coordinatio

256 In the crystal structure, Arg(16), an arginine residue that is present in this isoform but not

257 t on a set of two spatially close C-terminal arginine residues that are distant from the FAD binding

258 o be capable of ADP-ribosylating 6 candidate arginine residues that are located in the effector bindi

259 The conformational freedom of the charged arginine residues that compose the protease recognition

260 tational analysis of HD5, we have identified arginine residues that contribute to antiviral activity

261 s, which potentially could interact with the arginine residues that distinguish the atypical C1 domai

262 e double-stranded RNA product and lysine and arginine residues that interact with the phosphates of b

263 In particular, we identified several arginine residues that interact with the polyanionic sub

264 -85 and Asp-212 in bacteriorhodopsin) and an arginine residue (the homolog of Arg-82) form a complex

265 itrullinates histone arginine and monomethyl-arginine residues thereby regulating histone Arg methyla

266 The mutation of these pUS9 arginine residues to asparagine blocked the binding of b

267 hough agonists require interaction with both arginine residues to bind the receptor, antagonists requ

268 se (PAD) enzyme family that converts protein arginine residues to citrulline, a process known as deim

269 atalyze the post-translational hydrolysis of arginine residues to form citrulline.

270 e measured the contributions of tyrosine and arginine residues to phase separation experimentally thr

271 methylating the guanidino nitrogen atoms of arginine residues to regulate cellular processes such as

272 e N terminus as well as a strictly conserved arginine residue toward the C terminus of ORF52 play cri

273 The NRF-2beta NLS contains only two lysine/arginine residues, unlike other known importin-alpha:bet

274 Regeneration of the arginine residue using hydroxylamine fully restored the

275 stabilizing the position of the active site arginine residue via hydrogen bonding.

276 The arginine residue was essential for the Bacillus subtilis

277 The role of individual CRT arginine residues was determined by site-directed mutage

278 ral mutants with substitutions of lysine for arginine residues were created as single, double, and tr

279 reased levels of GO-derived modifications of arginine residues were detected within the assembly inte

280 ne or by a modified ZIP in which all but the arginine residues were replaced by alanine.

281 Furthermore, two N-terminal arginine residues were required for efficient translocat

282 s unaffected by alanine substitutions of the arginine residues, which only partially reduced the abil

283 f the resulting peptides at carboxy-terminal arginine residues, which were identified by mass spectro

284 mine whether peptides built exclusively from arginine residues will interact with different nAChR sub

285 n is the post-translational conversion of an arginine residue within a protein to the non-coded amino

286 tion of cathepsin G or citrullination of the arginine residue within an LC3-interacting region motif

287 Citrullination of a single arginine residue within the DNA-binding site of H1 resul

288 that phosphorylation of CtsR on a conserved arginine residue within the winged helix-turn-helix doma

289 The important arginine residue within the Xaa-Arg-Gly triplet is recog

290 ct on PRMT9 recognition of SF3B2, moving the arginine residue within this sequence abolished methylat

291 mplex virus 1 protein ICP27 is methylated on arginine residues within an RGG box, and arginine methyl

292 In this study, we found two arginine residues within histone H2B, which are specific

293 ized that PAD-mediated citrullination of the arginine residues within LL-37 will abrogate its immunom

294 ween the rat and human ortholog nonconserved arginine residues within proximity of a key conserved ar

295 t catalyzes the symmetrical dimethylation of arginine residues within target proteins, has been impli

296 Mutagenesis of conserved arginine residues within the C-terminal coiled-coil disr

297 ro pulldown assay to define a series of five arginine residues within the conserved pUS9 basic domain

298 urthermore, we found that positively charged arginine residues within the disordered region of the N-

299 edicted to form ionic lock interactions with arginine residues within the FFA2 or FFA3 agonist bindin

300 Mutations of arginine residues within the putative DNA recognition he