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 oxycytidine 5'-triphosphate with a surrogate arginine residue.

10 to compete with 1,2-cyclohexanedione for the arginine residue.

11 l but significant contribution from a single arginine residue.

12 genetic modifications by methylating histone arginine residues.

13 nzymatic digestion specifically at lysine or arginine residues.

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

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

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

17 similar shifts assignable to carboxylate and arginine residues.

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

19 hese factors are activated by methylation of arginine residues.

20 nal peptides containing an essential pair of arginine residues.

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

22 nal stabilizing interactions provided by two arginine residues.

23 he CTD contains four clusters of consecutive arginine residues.

24 ith PRMT5/WDR77, an enzyme that dimethylates arginine residues.

25 contains a flexible C-terminal tail rich in arginine residues.

26 ies specific for asymmetrically dimethylated arginine residues.

27 lyze the mono- and dimethylation of peptidyl arginine residues.

28 onist interact preferentially with different arginine residues.

29 ltransferase that symmetrically dimethylates arginine residues.

30 alyse three distinct types of methylation on arginine residues.

31 t by strict spatial localization of specific arginine residues.

32 post-translational hydrolytic deimination of arginine residues.

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

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

35 Invariant arginine residues 144 and 435 positioned in the vicinity

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

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

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

39 MT1- dependent methylation of RUNX1 at these arginine residues abrogates its association with SIN3A,

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

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

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

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

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

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

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

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

48 2-cyclohexanedione specifically modifies one arginine residue and the modified DAFP-1 loses its enhan

49 Protonated peptides containing histidine or arginine residues and a free carboxyl group (His-Ala-Ile

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

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

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

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

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

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

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

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

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

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

60 Since arginine residues are frequently present within protein

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

86 Substitution with an arginine residue at this position disrupts the network,

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 e containing the PXpsiPXR motif and flanking arginine residues at the S1 site.

93 In striking contrast, these two additional arginine residues augment the binding of the nSH3 domain

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

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

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

97 ven blocking the free carboxyl group of this arginine residue by amidation, eliminated the binding an

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

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

100 via two distinct mechanisms: modification of arginine residues by MGO inhibits cell adhesion, whereas

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

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

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

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

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

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

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

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

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

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

111 Conserved arginine residues comprise the substrate-binding pocket,

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

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

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

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

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

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

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

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

120 Neutralization of four arginine residues eliminated plasma membrane binding.

121 f the free energy profile for transfer of an arginine residue, embedded within a hydrophobic alpha-he

122 mutagenesis suggests that the two additional arginine residues flanking the PXpsiPXR motif at the S1

123 Each transporter requires two conserved arginine residues for activity.

124 Arginine residues form a positively charged patch to bin

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

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

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

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

129 An arginine residue implicated in malonate binding by proka

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

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

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

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

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

135 ed to make a salt-bridge interaction with an arginine residue in the FXR-binding pocket that is norma

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

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

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

139 Another arginine residue in the PSST subunit is hydroxylated and

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

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

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

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

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

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

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

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

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

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

150 Most modified arginine residues in known PRMT1 substrates reside in re

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

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

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

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

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

156 n arginine methyltransferases that methylate arginine residues in proteins.

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

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

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

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

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

162 Mutagenesis of key arginine residues in the DNA contact sequence results in

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

164 To examine the role of arginine residues in the phosphoryl transfer reaction, w

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

166 perturbs the side-chain conformations of the arginine residues in the RG-rich region.

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

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

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

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

171 oxyacid family, largely due to the number of arginine residues in the vicinity of the substrate alpha

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

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

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

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

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

177 These studies indicated that an arginine residue is critical for the enhancing ability o

178 y of DAFP-1 and the guanidinium group of the arginine residue is important for its interaction with t

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

208 Alteration of either the cysteine and arginine residues of the Cys-X(5)-Arg motif led to the l

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

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

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

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

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

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

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

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

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

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

219 k showed that substitution of four conserved arginine residues on the basic face with alanines result

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

221 valent pathway involving ADP-ribosylation of arginine residues on the P2X(7)R ectodomain.

222 Mutations of three arginine residues on these loops cause decreased TREX2 a

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

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

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

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

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

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

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

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

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

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

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

234 with site-directed mutations in a conserved arginine residue (R160) of the active site containing Eu

235 rginine-specific antibody, we identified two arginine residues (R206 and R210) within the region of R

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

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

238 A nearby arginine residue (R48) participates in a guanidinium sta

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

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

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

242 sential for InsP(6) binding and 5 lysine and arginine residues resulting in loss of activity at low I

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

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

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

246 RGG domain and, in particular, mutating all arginine residues severely reduced the association of Tb

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

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

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

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

251 tatic and hydrogen bond interactions with an arginine residue that is conserved in all known CD1 prot

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

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

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

255 lanked at its C-terminus with two additional arginine residues that are absolutely required for high-

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

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

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

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

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

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

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

263 -85 and Asp-212 in bacteriorhodopsin) and an arginine residue (the homolog of Arg-82) form a complex

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

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

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

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

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

269 complexes, here we show that the binding of arginine residues to narrow minor grooves is a widely us

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

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

272 Regeneration of the arginine residue using hydroxylamine fully restored the

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

274 The arginine residue was essential for the Bacillus subtilis

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

276 Fourteen of 16 lysine residues and 18 of 19 arginine residues were accessible to trypsin.

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

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

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

280 At the NFR motif the asparagine and arginine residues were sensitive to MTS reagents, wherea

281 hesis of mutants in which the four conserved arginine residues were substituted individually or toget

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

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

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

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

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

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

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

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

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

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

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

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

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

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

298 Mutations of arginine residues within the putative DNA recognition he

299 nd by mass spectrometric analysis that three arginine residues within the RGG box were methylated.

300 ults demonstrate that the replacement of all arginine residues within this motif with alanines render