ライフサイエンスコーパス: Arg residue

1 except near a conserved, positively charged Arg residue.

2 terminus, causing release of the C-terminal Arg residue.

3 e SERA5 gene, or replace Ser596 with a bulky Arg residue.

4 eaks indicates that they arise from a single Arg residue.

5 nts from cleavage at the C terminus of the L-Arg residue.

6 nd with the side chain of the C-terminal Lys/Arg residue.

7 lation and asymmetric dimethylation at three Arg residues.

8 est by a high degree of alignment of Lys and Arg residues.

9 omains, which together in bull P1 contain 19 Arg residues.

10 intermediates that contain C-terminal Lys or Arg residues.

11 al aromatic residues with positively charged Arg residues.

12 mide substrates with N-terminal Leu, Met and Arg residues.

13 short amino acids motifs enriched in Lys and Arg residues.

14 yzed substrates with N-terminal Leu, Met and Arg residues.

15 which resides in a stretch of Lys, His, and Arg residues.

16 s, the most active being those with 16 and 8 Arg residues.

17 enzyme is specific for COOH-terminal Lys or Arg residues.

18 t within the CR2-binding site on gp350 using Arg residues.

19 S4 segment carrying three positively charged Arg residues.

20 r access pathway for the transport of the S4 Arg residues.

21 llination of proteins via the deimination of Arg residues.

22 xyl terminus, to include an area rich in Ser-Arg residues.

23 riants were detected, with 6 (19%) involving Arg residues.

24 ightly held charge of a protonated arginine (Arg) residue.

25 strom of the flavin is a conserved arginine (Arg) residue.

26 channel blocked by the hydrocarbon chains of Arg+ residues.

27 IgG reduced this binding significantly, the Arg residues (162-163) of the C1q-A chain, which are tho

28 ve scanned the sequence -Gln-Ala-His-Ser-Asn-Arg- (residues 30-35 of [DPhe12,Nle21,38]Ac-hCRF4-41) wi

29 Mutation of three Arg residues, 93, 97, and 101, to Ala in thrombin (throm

30 were separately replaced with Ala, Ser, and Arg residues; all six mutants displayed no detectable ca

31 Therefore, the Arg residues allow D1 to take on a specific conformation

32 ned the relative impact of mutation of these Arg residues alone and in combination on the above react

33 -triphosphatase identified the motif Cys and Arg residues and an upstream Asp as required for activit

34 ariety of new fluorogenic peptides with a P3 Arg residue, and we demonstrated their superiority compa

35 ptide contains uniformly (13)C/(15)N-labeled Arg residues, and the RNA samples were unlabeled.

36 cally inactive because the essential Cys and Arg residues are absent.

37 Because cationic Arg residues are determinants of Crp4 bactericidal pepti

38 These two Arg residues are essential for autophagy, suggesting tha

39 f the native enzyme, suggesting that the two Arg residues are involved in substrate binding.

40 tereochemical interactions of catalytic site Arg residues are paramount.

41 Furthermore, Trp and Arg residues are required for the ability of PMX53 to ac

42 ractions individually with two transmembrane Arg residues (Arg-183(5.39) and Arg-258(7.35)) to create

43 SK1/PKARIalpha association requires all four Arg residues (Arg-93-96) in the pseudosubstrate site of

44 VIII) occurs through proteolysis at three P1 Arg residues: Arg(372) and Arg(740) in the FVIII heavy c

45 tatic/H-bonding interactions involving three Arg residues (Arg48, Arg51, and Arg53) projecting from t

46 -R(10)18A-NH(2)) had only positively charged Arg residues as the receptor binding domain.

47 endent on the presence of the highly charged Arg residue at 3056, and viruses with this phenotype and

48 Instead, we show that burying a single Arg residue at an interior position is sufficient to spe

49 age of a chromogenic substrate with a single Arg residue at P1 was NS2B-independent.

50 but their GPA contained the Gly rather than Arg residue at position 61.

51 Replacement of the Arg residue at position 82 in bacteriorhodopsin by Gln o

52 between the beta4 and beta5 strands, and an Arg residue at the beginning of the catalytic domain.

53 showed that mutation of a positively charged Arg residue at the beta-dimer interface and high NaCl co

54 sidue donated by the rasGAP protein, and the Arg residue at the core of the GTP or GDP sensing switch

55 th a Bowman-Birk inhibitor reported here, an Arg residue at the P1 position of the inhibitor is bound

56 observed that all sensitive viruses have an Arg residue at the P4 position of the cleavage site betw

57 Lys23 and Arg9, each containing an upstream Arg residue at the P6 and P5 position, respectively.

58 OmpT cleave peptides with three consecutive Arg residues at different sites, a difference in specifi

59 We found that both these Arg residues at positions 104 and 106 were required for

60 Arg residues at positions 295, 141, and 363 are involved

61 sidues to Ala, we demonstrated that only the Arg residues at positions 331 and 332 were required for

62 The peptide that was identified contained Arg residues at positions 331 and 332.

63 We found that mutating two Arg residues at positions 36 and 37 in the C-domain of I

64 e results indicate that the highly conserved Arg residues at positions 365 and 375 may play a role in

65 On the basis of exon sequences, there are no Arg residues at the predicted C-terminus of the mature g

66 Here we show that, in contrast, Arg residues at the same internal positions exhibit no d

67 utation of an absolutely conserved arginine (Arg) residue at position 50 to alanine (R50A) of the sim

68 ing of a chain of poly-L-Asp residues with L-Arg residues attached to the B-carboxylate sidechains by

69 Single mutations of the Asp (or Glu) and Arg residues blocked kinase function both in yeast cells

70 antigen possessed a P7-Leu instead of the P7-Arg residue, but nevertheless was accommodated within th

71 Four conserved Arg residues can function in the activation of the phosp

72 Replacement of Trp 185 by an Arg residue caused displacement of TM2 toward the outsid

73 s of the hD4R are substituted with arginine (Arg) residues, cellular hD4R protein levels increase.

74 Mutation of the two Arg residues close to the nonannular binding sites had n

75 contrast, mutation of lysines 66-68 to basic Arg residues did not decrease (and in some cases enhance

76 close to the PtdIns(3)P-binding pocket or an Arg residue directly involved in PtdIns(3)P binding abro

77 This catalytic cation is analogous to the Arg residue donated by the rasGAP protein, and the Arg r

78 m-phosphate complexation, where the cationic Arg residues drag the anionic phosphate groups along as

79 lix alpha2 in recognizing a constellation of Arg residues embedded in a hydrophobic patch on the surf

80 OVA with Arg to Ser replacements of all four Arg residues enhancing binding to this Ag.

81 In Arp K3(1) an Arg residue fills site 72, replacing the key aromatic re

82 utagenesis was used to investigate the seven Arg residues for activity (74, 75, 160, 162, 266, 306 an

83 The side chain of the active-site Arg residue forms a bidentate hydrogen bond with two of

84 H104 in HsPNP with the corresponding Glu and Arg residues found in BtPNP.

85 lytic effect by releasing C-terminal Lys and Arg residues from partially degraded fibrin.

86 dues from both proteins, including a pair of Arg residues from PriC and the C terminus of SSB.

87 Thus, Arg residues function as determinants of Crp4 bactericid

88 1 was extended at the C-terminus by a single Arg residue giving rise to analog 90 (BMS-200261) which

89 D4 to catalyze the deimination of methylated Arg residues has also been evaluated, and the results in

90 We hypothesize that these four Arg residues have developed as a result of somatic mutat

91 Several Arg residues have very downfield-shifted proton NMR resp

92 The role of the Arg residues, however, was surprisingly independent of t

93 Mutations were made to an Arg residue in a conserved SRC motif in the delta' and g

94 In contrast, mutation of the equivalent Arg residue in an extender AT domain resulted in a prote

95 te recognition is facilitated by a conserved Arg residue in CTDNEP1 that binds and orients the substr

96 an essential requirement for this conserved Arg residue in determining Hib PS-binding affinity.

97 A critical Arg residue in each SH2 domain was mutated to Ala.

98 Mutation of the P1 Arg residue in factor X to Gln prevented activation by t

99 f ISD with MALDI FTICR, the influence of the Arg residue in ISD fragmentation is less straightforward

100 Modifying the Arg residue in kalata with a keto aldehyde significantly

101 me high binding affinity, confirmed that the Arg residue in position 7, which is known to be crucial

102 Mutation of a critical Arg residue in the basic-leucine zipper domain of either

103 We conclude that, although the Arg residue in the FLVRES motif is invariant in most if

104 catalytic triad and unconventionally uses an Arg residue in the formation of an oxyanion hole.

105 attributed to a conformational change of the Arg residue in the stromal loop region.

106 n has a short cytoplasmic tail and a charged Arg residue in the transmembrane region that, by analogy

107 A conserved Arg residue in the wedge is required for Okazaki fragmen

108 These enzymes have a highly conserved Arg residue in their catalytic loop which is present two

109 talyze the post-translational methylation of Arg residues in a variety of different proteins involved

110 tic enzymes that catalyze the methylation of Arg residues in a variety of proteins (e.g., histones H3

111 s, Drp1-x01 required oligomeric assembly and Arg residues in alternative exon 3 for microtubule targe

112 These results illustrate that these Arg residues in anion binding exosite 2 contribute very

113 position, a strong nonpreference for Lys and Arg residues in any position, and the first evidence tha

114 mutagenesis was applied to the corresponding Arg residues in both the small and large subunits of mai

115 e derived from IS4 by altering the number of Arg residues in CDR3.

116 These results indicate a role for V(H)CDR3 Arg residues in chromatin specificity of lupus-derived a

117 Because of the reported role of V(H)CDR3 Arg residues in dsDNA binding and the near identity of t

118 In contrast, there are only three Arg residues in each of the alpha and beta chains.

119 Of four Arg residues in IS4VH CDR3 substituted to Ser, two at po

120 second finger-like structure and a number of Arg residues in L1 that form a positively charged, shelf

121 sed to identify three phenylglyoxal-modified Arg residues in monomeric rabbit muscle CK.

122 role of high alpha-defensin Arg content, all Arg residues in mouse Paneth cell alpha-defensin cryptdi

123 mblies and cellular dispositions, homologous Arg residues in neuroligin-3 (Arg-451), in butyrylcholin

124 We also identified three Arg residues in nsP4, R545, R546, and R547, that are nee

125 ionic interactions between Asp-19 (P(6)) and Arg residues in plasmin (Arg-644, Arg-719, and Arg-767),

126 P. gingivalis among bacteria, which converts Arg residues in polypeptide chains into citrulline.

127 Taken together, our results demonstrate that Arg residues in S1-S4 voltage-sensing domains reside in

128 d the important functional roles of internal Arg residues in situations where a charge is needed in t

129 we tested the contributions of two V(H)CDR3 Arg residues in SN5-18 to chromatin specificity.

130 ransfer difference NMR results discover that Arg residues in SRSF1 RS interact with the guanine base

131 All Arg residues in the 5-base specific (UACAU) mRNA interfe

132 irected mutagenesis were used for studies of Arg residues in the active site of SULT1A1.

133 y neurotransmitter receptors often relies on Arg residues in the binding site, leading to the assumpt

134 series of melanotropin analogues with His or Arg residues in the core pharmacophores of MTII, SHU9119

135 resent study, we show that altering specific Arg residues in the H chain of a human pathogenic beta2G

136 The single substitution of any of the four Arg residues in the helical segments did not affect impo

137 e within the phosphate-binding loop, and two Arg residues in the LID domain are proposed as substitut

138 eas substitutions for the individual Lys and Arg residues in the N-terminal region were tolerated.

139 Substitution of both Arg residues in the N-terminal segment (R3Q/R10Q) caused

140 cking Arg-NLS-Gln ING4 mutant, which has all Arg residues in the NLS mutated to Gln, loses its affini

141 channels are controlled by several conserved Arg residues in the S4 helix of the voltage-sensing doma

142 these results demonstrate that the conserved Arg residues in the SRH of both D1 and D2 play critical

143 The Arg residues in these two mutants are restricted to a hi

144 e exceptions (e.g., Lys and Arg) to the twin Arg residues in this motif have been noted.

145 structure mapping identified several Lys and Arg residues in this region that form salt bridges with

146 residues, in contrast to the larger Lys and Arg residues in yeast and plant orthologs.

147 C:G base pairs H-bond with conserved His or Arg residues in ZnF8, ZnF9, and ZnF11, and the consensus

148 first time the replacement of all arginine (Arg) residues in a protein with canavanine (Can), a toxi

149 Serpin-1A, with a P1 Arg residue, inhibited both trypsin and plasmin.

150 Cationic peptides containing Lys and Arg residues interact with DNA via charge-charge interac

151 hat only the side chains of specific Lys and Arg residues interact with the surface.

152 eta 2GPI was achieved by the introduction of Arg residues into the 3H9 H chain variable region at pos

153 analyses of Sdh1 implicate C-terminal region Arg residues involvement in covalent flavinylation and S

154 One of the Arg residues is in the region corresponding to the "safe

155 the invariant Lys residue as well as the two Arg residues, its phosphate-binding loop is examined and

156 d units, specifically, of consecutive Lys or Arg residues (K/R repeats) and Asp or Glu (D/E repeats)

157 Such targeting of Arg residues, leading to significant changes in coding a

158 demonstrate that citrullination of selected Arg residues leads to progressive disruption of HSP90 te

159 ement, in the Pro3 analogue, with additional Arg residues led to analogues with improved kappa affini

160 In addition, one His and two Arg residues lie in close vicinity of the binuclear meta

161 in-tyrosine kinases contain a catalytic loop Arg residue located either two or four positions downstr

162 ively spliced AT-hook indicated that Lys and Arg residues made essential DNA contacts, whereas Gly an

163 The Arg residues may be important not only for Sdh5 associat

164 586A/R588A/R591A (all three of the indicated Arg residues mutated to Ala), had wild-type activity and

165 We show that (i) substitutions of the Arg residue of TL contacted by Tgt confer resistance to

166 The (15)Nepsilon resonances of all six Arg residues of 4-OT were assigned, and the assignments

167 eport that alterations in the 0-layer Gln or Arg residues of Vam7p or Nyv1p, respectively, strongly i

168 Mutation of the arginine (Arg) residue of the highly conserved LNDR motif has been

169 harged GAGs and positively charged arginine (Arg) residues of collagen protein.

170 We have demonstrated that a highly conserved Arg residue on loop 1 of RHBDL2 plays a critical role in

171 open conformation, two of the four conserved Arg residues on S4 are on a lipid-facing surface and two

172 Methylation of arginine (Arg) residues on histones creates a new binding epitope,

173 To investigate the role of the Arg residues, one or two arginines were replaced by Ala.

174 Gly207, and is further stabilized by the two Arg residues opposing the pSer202/pThr205.

175 hanced by N-terminal addition of four Lys or Arg residues or a second Tat peptide.

176 and demonstrated that its positively charged Arg residues, particularly Arg6 and Arg7, were crucial f

177 , alpha-defensins contain an average of nine Arg residues per Lys residue.

178 In this pathway for peptide translocation, Arg residues play a fundamental role not only in the bin

179 than for binding, while Arg-65 and two other Arg residues play a greater role in binding than in resi

180 d concentration-dependent manner, suggesting Arg residues play an important role in the catalytic act

181 e bacterial species tested regardless of the Arg residue position.

182 nspires via interaction of the quencher with Arg residues positioned on the peptide substrate.

183 Within these domains, a strictly conserved Arg residue present in both activating cofactors, but no

184 In this arrangement, the highly conserved Arg residue present in either cofactor comes into close

185 d a key epitope corresponding to an internal Arg residue (R502 [HSP90beta]/R510 [HSP90alpha]) that is

186 ecific missense mutation of the codon for an Arg residue required for sialic acid recognition.

187 R2 binding of gp350 utilized the same set of Arg residues required for recognition of its natural lig

188 with a neutral (Met, Gln, or Ala) or basic (Arg) residue results in an approximately 10(4)- or 250-f

189 The repeated motif contains Arg residues spaced by a hydrophobic segment that may be

190 d included those having the alpha-subunit 96(Arg) residue substituted by Gln, Leu, or Ala, the alpha-

191 N9PP orthologs share a stringently conserved Arg residue that forms a salt bridge with the substrate

192 a much longer surface loop, and the critical Arg residue that is required for ascorbate binding in AP

193 on of Trp-222 in the loading AT domain to an Arg residue that is universally conserved in all extende

194 hydrophobic pocket near a cluster of Asp and Arg residues that are essential for catalysis, with the

195 HORMA structure reveals a pair of conserved Arg residues that constitute a putative phosphate sensor

196 The conformations of the Arg residues that interlock helix A and B appear to be p

197 een of MICU1 identifies two highly-conserved Arg residues that might contact the DIME-Asp.

198 ced affinity for hydrolysis after Lys versus Arg residues; therefore, the ability to autolytically ac

199 els, suggesting that movements of protonated Arg residues through the membrane will be prohibited.

200 Mutation of this critical Arg residue to Ala in either of the hexameric enzymes pr

201 Mutation of a single conserved Arg residue to Ala in the cJun spacer region (R285A) led

202 orption, leading to proton mobilization from Arg residues to a less favored protonation site.

203 By changing each of the Arg residues to Ala, we demonstrated that only the Arg r

204 PAD4 catalyzes the hydrolytic deimination of Arg residues to produce Cit and ammonia.

205 sical basis behind the remarkable ability of Arg residues to remain protonated in environments otherw

206 Here, we show that a conserved Arg residue uses a two-pronged strategy to select agains

207 experiments, surface accessibility maps for Arg residues were compared for the free fPollambda versu

208 However, for both mZP2 and mZP3, Arg residues were released by carboxypeptidase B, consis

209 (HNP1) and several HNP1 analogs where three Arg residues were replaced by each of the following six

210 ass spectrometry analysis confirmed that all Arg residues were replaced with Can.

211 nhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are

212 re active than KSHV-GPCR, suggesting that an Arg residue, which is constrained outside the bundle by

213 ss-II myosins begins with a highly conserved Arg residue (whose mutation in human beta-cardiac myosin

214 n which we replaced seven C-terminal Lys and Arg residues with Ala and added a Cys residue at either

215 ed the consequences of replacing each of the Arg residues with lysine, glutamine, histidine, or alani

216 The interaction of these positively charged Arg residues with the lipid membrane has been of intense

217 jacent C residues of the CCA sequence and an Arg residue within a highly conserved sequence motif in

218 Substitution of Arg residues within alpha-26 with Glu, or substitution o

219 Arg residues within S1-S4 domains are well hydrated and

220 thin the effector binding region (EF) or two Arg residues within the C-terminal tail (TL).

221 which contained Arg-->Ala mutations at four Arg residues within the effector binding region (EF) or

222 The roles of all three Arg residues within the PlcH RRRTFLK consensus motif wer

223 Conserved twin arginine (Arg) residues within the Tat signal sequence consensus m

224 minimal 9-mer peptide, R6A-1, do not contain Arg residues yet retain high affinity (K(D) = 60 and 200