ライフサイエンスコーパス: charged amino acid

1 smembrane segments, none of which contains a charged amino acid.

2 y by forming a salt bridge with a positively charged amino acid.

3 ing, as did substitution of all the flanking charged amino acids.

4 ytoplasmic retention potential of positively charged amino acids.

5 ts Uch37-binding surface to a region rich in charged amino acids.

6 us GP75 proteins, as well as hydrophobic and charged amino acids.

7 rough careful selection of electrostatically charged amino acids.

8 mbrane-interacting (hydrophobic) residues to charged amino acids.

9 n DNA via a channel consisting of positively charged amino acids.

10 calized, 37 contained clusters of positively charged amino acids.

11 en both residues were replaced by positively charged amino acids.

12 cid region of GIV that is enriched in highly charged amino acids.

13 1) were mutated to neutral and/or oppositely charged amino acids.

14 the protein before the level of the ring of charged amino acids.

15 enerally transports uncharged and negatively charged amino acids.

16 -1 barrel and the displacement of particular charged amino acids.

17 igh replacement to silent ratio resulting in charged amino acids.

18 esence of cyclodextrins or chiral positively charged amino acids.

19 c acid (BCH), but not inhibited by L-Ala and charged amino acids.

20 ion damage alters scattering from negatively charged amino acids.

21 o a channel with a preference for negatively charged amino acids.

22 Adjacent or clustered charged amino acids (2 to 4), scattered along the 2C(ATP

23 ns demonstrate strong affinity to negatively charged amino acids, a considerable influx of calcium in

24 r CAA increased with each unit of positively charged amino acids, according to multinomial logistic r

25 by salt-bridge interactions between specific charged amino acids across the dimer interface.

26 mutation in the gpat6-a mutant introduces a charged amino acid adjacent to the active site of a GPAT

27 ne end of the binding groove and is the sole charged amino acid adjacent to the ligand.

28 rostatic interactions (EIs) between pairs of charged amino acids affects A beta 40 and A beta 42 olig

29 tion, even allowing for the incorporation of charged amino acids and bisheterocyclization.

30 onsequently, the localizations of negatively charged amino acids and calcium ions in the Abeta bindin

31 of conserved cysteine residues, clusters of charged amino acids and clusters of hydrophobic/aromatic

32 n a nonapeptide, which is rich in positively charged amino acids and creates a bipartite NLS.

33 enhancing electrostatic interactions between charged amino acids and lipid polar headgroups.

34 static interactions between three positively charged amino acids and negatively charged phosphate gro

35 C-terminal domains is lined with positively charged amino acids and represents a conduit for polypho

36 inding cavity festooned with four negatively charged amino acids and surprisingly limited hydrophobic

37 e roles of the angle subtended by positively charged amino acids and the positioning of the proline r

38 lectrostatic interactions between positively charged amino acids and the ribosomal tunnel.

39 atches, we selectively mutated three to four charged amino acids and thus generated five mutants (pat

40 " motif, (2) a furin site of four positively charged amino acids, and (3) a double tyrosine near the

41 le regions with higher content of positively charged amino acids; and longer CDR3 and maintenance of

42 mutation of apolar and polar amino acids to charged amino acids are destabilizing, but the reasons a

43 analogs of SP-B(1-25) also suggest that the charged amino acids are important in determining the pos

44 A number of conserved negatively charged amino acids are located within domain III in the

45 fects in signaling caused by substitution of charged amino acids are not caused by changes in the abu

46 Four positively charged amino acids are positioned around the active sit

47 Substitutions at position 94 with polar or charged amino acids are tolerated poorly or not at all,

48 es (including aromatic, aliphatic, polar and charged amino acids) are subjected to continuous enzymat

49 genesis studies showed that three positively charged amino acids (Arg-9, Lys-10, and Lys-22) contribu

50 central pore equidistant (5-7 A) between six charged amino acids, Arg-302 and Lys-319 opposing Glu-26

51 oltage comes from the movement of positively charged amino acids, arginine or lysine, across the memb

52 eanalyze a method that implicated positively charged amino acids as the major determinant of ribosoma

53 ogen-bond network is established between the charged amino acids Asp(228), Asp(229), and Arg(226), an

54 ge to amino acid side chains, and negatively charged amino acids (Asp/Glu) can sometimes mimic the ph

55 onRACK constitutes a change from a polar non-charged amino acid (asparagine) in epsilonRACK to a pola

56 positively charged lysine and the negatively charged amino acids aspartate and glutamate.

57 conserved, negatively rather than positively charged amino acid (aspartate 120) near the N1-C2=O posi

58 acid (asparagine) in epsilonRACK to a polar charged amino acid (aspartate) in epsilonPKC.

59 stitution of Glu-506 with another negatively charged amino acid aspartic acid, suggesting the importa

60 of ions adsorbed on the graphene as well as charged amino acids associated with the immobilized prot

61 The results demonstrate that a negatively charged amino acid at position 955 of HKalpha2 promotes

62 es rather than the absence of a specifically charged amino acid at these three positions.

63 Peptides containing positively charged amino acids at position 1182 or hydrophobic resi

64 tylation requires the presence of positively charged amino acids at positions 8 and 16 of H4, positio

65 173GG can be rescued by restoring positively charged amino acids at the adjacent positions 174 and 17

66 e that a short segment containing positively charged amino acids at the N terminus of PrP plays an es

67 The results show that the positively charged amino acids at the SNAP-25 C terminus promote ti

68 ubstantial barrier to membrane insertion for charged amino acids, but the coarse-grained model still

69 as varying the angle subtended by positively charged amino acids can attenuate hemolytic potential al

70 ered vaccinia virus mutants with clusters of charged amino acids changed to alanines and determined t

71 phobic sequence of 18 aa and (ii) positively charged amino acids close to the C-terminal end of the h

72 fragments of ERM proteins at the positively charged amino acid cluster within the NEP cytoplasmic do

73 oplasmic domain of NEP contains a positively charged amino acid cluster, previously identified as a b

74 or point mutations replacing the positively charged amino acid cluster.

75 or site), both of which recognize positively charged amino acid clusters in NLSs.

76 ple charge-screening models, indicating that charged amino acids contribute to the remarkable stabili

77 is consistent with the EC-3 loop negatively charged amino acid, D275 (identified via Glide docking s

78 iameter and is lined by a ring of negatively charged amino acids: D487, E488, and D489.

79 The increased usage of charged amino acids (DEHKR) may be one way of maintainin

80 The negatively charged amino acid-dependent sumoylation motif (NDSM) ca

81 moylation motif, termed the NDSM (negatively charged amino acid-dependent sumoylation motif), helps d

82 e, but herein we also demonstrate that these charged amino acids do not play a major role in the matu

83 in transmembrane domain 7 with a negatively charged amino acid eliminates the ability of glutamate t

84 Substitution of Asn(11) with a positively charged amino acid essentially abolished the activity of

85 otassium flow by interacting with negatively charged amino acids facing the ion permeation vestibule

86 ICK toxins, HpTx2 binding does not require a charged amino acid for interaction.

87 hree noncharged residues is required between charged amino acids for the charge state with the highes

88 ening is dictated by the charge of the first charged amino acid found within the extension.

89 has been attributed to the high frequency of charged amino acids found in bacterial collagen.

90 These findings suggest that these negatively charged amino acids function to force the P22R-bound DNA

91 only requires a certain number of positively charged amino acids, Gag binding to genomic RNA for pack

92 vidual or simultaneous neutralization of the charged amino acids Glu(321) and Lys(324) abolished the

93 nvestigated the adsorption of the oppositely charged amino acids glutamate and lysine with and withou

94 By contrast, we find that positively charged amino acids greatly retard ribosomes downstream

95 conserved charged residues to the oppositely charged amino acid had an increased likelihood of genera

96 ls in highly accessible surfaces bordered by charged amino acids implies site directed S-nitrosylatio

97 ne zipper, (ii) placement of asparagine or a charged amino acid in the hydrophobic interface and (iii

98 We also found that D643, a negatively charged amino acid in the pore, is crucial for channel p

99 membrane domain (S4) and a single negatively charged amino acid in the third transmembrane domain (S3

100 rns; simulations indicated that a positively charged amino acid in this location alters the interacti

101 However, substitution of all three charged amino acids in a conserved beta-turn that is pre

102 ing mutagenesis demonstrated that positively charged amino acids in CL-3 were critical for NPM bindin

103 Experiments verifying the importance of charged amino acids in conferring ARF and Aux/IAA intera

104 ittle is known about the importance of these charged amino acids in determining dimer/monomer status

105 Cys(114) , and neighbouring hydrophobic and charged amino acids in DksA orthologues, phylogeneticall

106 Positively and negatively charged amino acids in extramembrane domains represent c

107 GR1 indicated that the clustered positively charged amino acids in GR1 play important roles in Pol p

108 We demonstrate that mutation of any of these charged amino acids in KCa3.1 or KCa2.3 to alanine, glut

109 his loop is variable and contains negatively charged amino acids in plants, in which these leaders ac

110 sigma70, K593 and R599, and three negatively charged amino acids in RhaR, D276, E284, and D285, that

111 The catalytic glutamate is one of ~250 charged amino acids in SecA, and yet neutralization of i

112 indicate that the accumulation of positively charged amino acids in short linear motifs (SLiMs), and

113 nt study, we first identified two positively charged amino acids in sigma70, K593 and R599, and three

114 e predict that plant leucine zippers rely on charged amino acids in the a position to drive heterodim

115 Mutating key positively charged amino acids in the C-terminal region adjacent to

116 packaging signals in the RNA and positively charged amino acids in the capsid protein but also that

117 Charged amino acids in the central region of RsbT were l

118 Two charged amino acids in the D2 pore, Arg599 and Glu554, p

119 aptures the increased selective pressure for charged amino acids in the dominant epitope of hemagglut

120 ated based on the hypothesis that negatively charged amino acids in the extracellular loops of TRPML3

121 We systematically mutated negatively charged amino acids in the first and second extracellula

122 ly determined the contribution of negatively charged amino acids in the gamma' chain, both individual

123 by the side chain orientation of positively charged amino acids in the heavy chain of residues 99-10

124 A scuPA variant in which the charged amino acids in the heparin binding site (HBS) in

125 o illustrate the critical role of positively charged amino acids in the Jas domain in mediating the J

126 Several conserved charged amino acids in the long alpha-helix of IF(1) are

127 -X(2)-Phi3-X-Phi4 pattern and for negatively charged amino acids in the nonhydrophobic positions of e

128 e rings implies that the adjacent positively charged amino acids in the peptide are close to the leve

129 Positively charged amino acids in the proximal tail of the beta2-ad

130 Two conserved, positively charged amino acids in the region 157-171 (lysines at po

131 Mutations of positively charged amino acids in the S4 transmembrane segment of a

132 Substitution of positively charged amino acids in this domain in full-length Lon wi

133 lectrostatic roles of two sets of positively charged amino acids in U1A that do not make hydrogen bon

134 y of side-chain model compounds of polar and charged amino acids in vacuum using density function the

135 ope A became dominant in 1989, the number of charged amino acids increased in epitope A and decreased

136 The number of charged amino acids increased in the dominant epitope B

137 However, conserved charged amino acids inhibit Dsg:Dsg and Dsc:Dsc interact

138 a disrupting domain consisting of a chain of charged amino acids, inhibited Abeta-associated toxicity

139 Inserting a negatively charged amino acid into hexa-arginine dramatically weake

140 electrostatic consequences of introducing a charged amino acid into the nascent peptide.

141 monstrate asymmetry of distribution of kNBC1 charged amino acids involved in ion recognition in putat

142 The effect of charged amino acids is additive, with ribosomal occupanc

143 Our results show that the extreme bias in charged amino acids is not necessary for antirestriction

144 In contrast, the a-a' pairs containing charged amino acids (K, R, and E) show the least range i

145 monstrate here that simultaneous addition of charged amino acids L-Arg and L-Glu at 50 mM to the buff

146 ion of Arg155 with a neutral or a negatively charged amino acid largely decreased OCP binding to the

147 s engineered to contain different numbers of charged amino acids localized to known regions of the tu

148 tion also displays an increased frequency of charged amino acids localized to the complementarity-det

149 re of these interactions, natural positively charged amino acids Lys and Arg have multiple methylenes

150 acids Gly, Leu, Ala, Ile and two positively charged amino acids Lys and Arg were composed of more th

151 ucine 170 to either positively or negatively charged amino acids (lys or glu) disrupted the calcium-d

152 of arrestin is released and exposes several charged amino acids (Lys14, Lys15, Arg18, Lys20, Lys110,

153 fragments, administration of the negatively charged amino acid lysine was largely ineffective in pre

154 e presence of Hg(2+) ions and the positively charged amino acid, lysine.

155 Some of the positively charged amino acids may be involved in ATP binding.

156 etween adjacent helices, which suggests that charged amino acids may play a dual role in collagen sta

157 y charged sol-gel coating and the negatively charged amino acid molecules.

158 helices that include four or more positively charged amino acids, most commonly arginine.

159 e a structurally highly conserved negatively charged amino acid motif that is strictly required for M

160 Of the six charged amino acids, mutation of H263 or R264 also negat

161 ded at the C terminus (POmega) and contained charged amino acids not more than 3 residues after the a

162 e electrostatic attraction of the positively charged amino acids of AKAP18delta to negatively charged

163 lysis indicated that the internal positively charged amino acids of M2 are required for its nuclear l

164 membranes couples the domains of positively charged amino acids of secretory vesicle SNARE proteins

165 Mutagenesis of basically charged amino acids of the basic thumb to alanines follo

166 ned using site-directed mutagenesis in which charged amino acids of the Tra domain were replaced by a

167 ne frataxin trimer, with conserved polar and charged amino acids of the two proteins positioned at hy

168 ontent, the effect of neutral and negatively charged amino acids on DNA-DNA intermolecular forces was

169 Conserved charged amino acids on one side of the beta-propeller st

170 avirulent viral variants acquire positively charged amino acids on surface-exposed structural protei

171 tion to model the evolution of the number of charged amino acids on the dominant epitope in the hemag

172 ombination, but the topography of negatively charged amino acids on the polar surface was altered, an

173 In this study, we identified four positively charged amino acids on the serine protease domain that a

174 hermore, five patches containing clusters of charged amino acids on the surface of TAg were identifie

175 This study examines the contributions of charged amino acids on the surface of the Rous sarcoma v

176 d a microtubule is facilitated by positively charged amino acids on two separate regions of the CHD,

177 types demonstrated that addition of either a charged amino acid or altering a cysteine residue in the

178 Mutant Tsr molecules with a charged amino acid or proline replacement exhibited the

179 residues in predicted functional domains or charged amino acid pairs/triplets, and rescued viruses w

180 We propose these aromatic and charged amino acids participate in either undecaprenyl p

181 We found that charged amino acids play a dominant role during the proc

182 Our results suggest that S3 and S4 charged amino acids play an evolutionarily conserved rol

183 extensive analyses, we show that positively charged amino acids play an important, but not exclusive

184 t this interaction localizes to a cluster of charged amino acids (positions 46-56) but not to an adja

185 stitution of the rictor Gly-934 residue to a charged amino acid prevents formation of the rictor/Sin1

186 pendent K+ channels, arising from positively charged amino acids primarily within the S4 transmembran

187 s identified the critical role of positively charged amino acids R108, R113, R160, and K157 on the su

188 Hydrophobin-II mutants show that a charged amino acid reduces the hydrophobicity of a large

189 Receptors with proline or charged amino acid replacements at critical hydrophobic

190 ependent transporters, in which a positively charged amino acid replaces the cotransported cation.

191 Based on a predicted G structure, charged amino acids residing in regions that could be ho

192 y pi-pi interaction) and with the positively charged amino acid residue Arg707 (charge-charge interac

193 These variants were obtained by replacing a charged amino acid residue at different sites on lysozym

194 activation and show that a single positively charged amino acid residue is entirely responsible for t

195 c acid in the central gate with a positively charged amino acid residue reverses the ion selectivity

196 t of salt bridges between different types of charged amino-acid residue pairs on alpha-helix folding.

197 The mutation of C1INH at all four positively charged amino acid residues (Arg(18), Lys(22), Lys(30),

198 p2 is a contiguous strip of seven negatively charged amino acid residues (negatively charged strip or

199 Electrostatic interactions between the charged amino acid residues and the lipid headgroups are

200 domains, and conserved patches of positively charged amino acid residues appear to mediate the intera

201 with this, other nearby conserved negatively charged amino acid residues are essential for ACS6 stabi

202 These results show that interactions between charged amino acid residues are important both to direct

203 Charged amino acid residues are often significant contri

204 egy is used to probe the effect of modifying charged amino acid residues around, but not directly bou

205 a "snorkeling" model, in which the flanking charged amino acid residues at 681 and 694 are buried in

206 Mutagenesis of positively charged amino acid residues at a putative anion binding

207 e have shown that the addition of negatively charged amino acid residues at several positions within

208 is mainly mediated by a patch of positively charged amino acid residues at the interface of domains

209 e 2a polymerase activity and that negatively charged amino acid residues between positions 110 and 12

210 Interactions of charged amino acid residues between the surfaces of trop

211 r results indicate that (i) substitutions of charged amino acid residues E131 in transmembrane domain

212 erminal domain and a set of three negatively charged amino acid residues in a predicted helix-loop-he

213 A computational model containing all the charged amino acid residues in the AroA active site clos

214 mutants suggest that clusters of positively charged amino acid residues in the CTD are required for

215 Two positively charged amino acid residues in the Jas domain were ident

216 Mutations of conserved, positively charged amino acid residues in the loop caused decreased

217 position and form ion pairs with negatively charged amino acid residues in the S2 and S3 segments of

218 The RyRs have many negatively charged amino acid residues in the two regions linking t

219 ter assay screen, we have identified several charged amino acid residues in TLR4 and MD-2 that are im

220 The insertion of charged amino acid residues into the hydrophobic part of

221 ains two high-density clusters of positively charged amino acid residues located in the cytoplasmic N

222 used to study how the microstructure of some charged amino acid residues may affect a protein's reten

223 ty of the LAA residue adjacent to positively charged amino acid residues may effectively modulate the

224 id bHLH domain has been modified to position charged amino acid residues near one face of the DNA dou

225 hensive study to demonstrate that positively charged amino acid residues on the surface of the E2 gly

226 constant is dictated by the distribution of charged amino acid residues on the surface of the PCu's.

227 We further proposed that five negatively charged amino acid residues surrounding this bond mediat

228 he force of the electric field on positively charged amino acid residues termed "gating charges," whi

229 In a search for positively charged amino acid residues that may be involved in reco

230 tion (MNDO-PSDCI) methods have revealed that charged amino acid residues within 8 A of the pigment mo

231 pear to form salt bridges between positively charged amino acid residues within regions of high exces

232 structural and functional roles of conserved charged amino acid residues, a nuoA knock-out mutant and

233 ue to a balance of positively and negatively charged amino acid residues, is very positively charged

234 s two distinct surface patches of oppositely charged amino acid residues, mediating front-to-back mul

235 etween negatively charged DNA and positively charged amino acid residues, the translocation speed of

236 ntified six clusters of conserved positively charged amino acid residues, which are in direct contact

237 ne proteins often are flanked by aromatic or charged amino acid residues, which may "anchor" the tran

238 ele class, 3, is conserved in its pattern of charged amino acid residues.

239 ent upon the presence of multiple positively charged amino acid residues.

240 ilayers due to the differing distribution of charged amino acid residues.

241 ycosylation sites and at the four positively charged amino acid residues.

242 0, a domain that contains a series of highly charged amino acid residues.

243 s well as the roles of all its 43 negatively charged amino acid residues.

244 age dependences to a large extent are set by charged amino-acid residues of the extracellular linkers

245 channels, which electrostatically affect the charged amino-acid residues of the voltage sensor S4.

246 Incorporating charged amino-acid residues to improve peptide solubilit

247 Although positively charged amino acids result in the Tyr-84 swing, amino ac

248 c toxin interaction, and if substituted with charged amino acids, result in the loss of toxin binding

249 patch by the substitution of hydrophilic or charged amino acids resulted in a loss of the interactio

250 ividually, the substitution of uncharged for charged amino acids resulted in only minor changes in bi

251 cluster with histidines (another positively charged amino acid) resulted in low efficiency of recept

252 re, it has been thought that complementarily charged amino acid(s) are critically involved in substra

253 A charged-amino-acid second-site substitution in the TM in

254 )/HCO(3)(-) exchanger in which four specific charged amino acids seem necessary for ion transport.

255 romosomes both depend on a short, positively charged amino acid sequence connecting the two hydrophob

256 , many of which are interspersed with highly charged amino acid sequences.

257 gnize minor-groove geometry using positively charged amino acids (shape readout).

258 ests that electrostatic interactions between charged amino acid side chains play an important role in

259 ssibility mutagenesis to identify positively charged amino acid side chains that attract cytoplasmic

260 such as transient pores and the insertion of charged amino acid side chains, may be common and perhap

261 strongly modulated by interactions involving charged amino acid side chains; and 7) Norrin-CRD bindin

262 s is scarce, because of a lack of negatively charged amino acid side-chain residues that would enable

263 Electrostatic interactions with positively charged amino acid site chains (His12/Lys41), together w

264 Charged amino acids specific to slc4a gene family member

265 re distinctly nonrandom, with a dominance of charged amino acid substitutions encoded by G-to-A trans

266 Charged amino acids such as Arginine play important role

267 f adenine nucleotides with Kir6.2 positively charged amino acids such as K185 and R201 on the C-termi

268 es containing an increasing number of basic (charged) amino acids, such as arginine, lysine, and hist

269 P5 position, with preference for positively charged amino acids, suggesting that electrostatic inter

270 Our results show that two charged amino acids that are specific for the alpha3-gro

271 GPR35 contains numerous positively charged amino acids that face into the binding pocket th

272 hese results indicate selective pressure for charged amino acids that increase the affinity of the vi

273 We identify a minimal region of negatively charged amino acids that is necessary and sufficient for

274 s (one positively charged and two negatively charged amino acids) that we term the SB triad.

275 mbrane translocation potential of negatively charged amino acids, thus increasing the cytoplasmic ret

276 assembly of specific AAB heterotrimers using charged amino acids to form intrahelix electrostatic int

277 ad series of aliphatic, aromatic, polar, and charged amino acids to give the following peptides: d[Gl

278 s of a rigid cyclic "cap" and two negatively charged amino acids to interact with a positive charge.

279 sequences of replaced V(H) genes contribute charged amino acids to the CDR3 region, a hallmark of au

280 Introduction of negatively charged amino acids to the hydrophobic face or of helix-

281 nesis to examine the contributions of RsbT's charged amino acids to the protein's stability and activ

282 electrostatic contribution of its negatively charged amino acids using directed evolution of a synthe

283 A negatively charged amino acid was preferred by DQ0604 in pocket 6 d

284 gainst HIV-1 or SIVagm Vif when a negatively charged amino acid was replaced with a lysine at positio

285 g altered alleles of I6 in which clusters of charged amino acids were changed to alanine residues.

286 lmitoylated sites are enriched in positively-charged amino acids, which could facilitate palmitoyl gr

287 membrane and contain an excess of positively charged amino acids, which react to an electric field.

288 tion of Glu-590 with aspartate, a negatively charged amino acid with only one methyl group less than

289 s were made by replacing single or clustered charged amino acids with alanines.

290 Likewise, substitutions of the positively charged amino acids with neutral or negatively charged r

291 mone syndrome mutations affects a cluster of charged amino acids with potential for ionic bond format

292 , we showed that spatial localization of the charged amino acids with respect to the FG sequence dete

293 were surrounded by negatively or positively charged amino acids within a 6-A distance.

294 dues for RACK1, in particular the positively charged amino acids within residues 44-54 of G beta1, ar

295 rth position, and (iii) a lack of negatively charged amino acids within the first 12 residues.

296 lowed down, due to protonation of negatively charged amino acids within the retinal binding pocket, e

297 gned and synthesized a peptide that utilizes charged amino acids within the ubiquitous Xaa-Yaa-Gly tr

298 electrostatic interaction between oppositely charged amino acids within their G loops that is conserv

299 ion, in intact cells, mutation of positively charged amino acids within this putative NLS in the full

300 site is probably mediated by the positively charged amino acids within this track, with negatively c