ライフサイエンスコーパス: single amino acid

1 acids, thus creating synonymous codons for a single amino acid.

2 ess protein stability at the resolution of a single amino acid.

3 -4-amino-4-carboxylic acid substituted for a single amino acid.

4 ion in S/N is attributable to differences of single amino acids.

5 trate that inward rectification depends on a single amino acid (Ala(254)) at the inner pore mouth of

6 ect/imperfect hexamers and repeat coding for single amino acid/amino acid pair runs.

7 A single amino acid and various oligopeptides are grafted

8 tion is a robust feature within proteins and single amino acids and discuss potential applications.

9 sis ICP55 was responsible for the removal of single amino acids, and its action explained the -3 argi

10 approximately 60%) of mutations affecting a single amino acid, Arg882 (R882), in the catalytic domai

11 glucose than on other sugars, namely when a single amino acid (arginine, glutamate, or proline) is t

12 A single amino acid (Asn to Ile) substitution in the homeo

13 However, apoE4 differs from apoE3 by only a single amino acid at position 112, which is arginine in

14 By using reverse genetics, we found that a single amino acid at position 158 of the hemagglutinin (

15 Previous studies identified a single amino acid at residue 296 in the protruding (P) d

16 he binding to LIMP-2 is not dependent upon a single amino acid, but the interactions of GCase with LI

17 ApoE4 differs from its wild-type ApoE3 by a single amino acid C112R in the 299-amino-acid-long seque

18 Here, we show that single amino acids can be identified by trapping the mol

19 mutations in proteins, in which exchange of single amino acids can radically alter structure and fun

20 entities represented in PRO corresponding to single amino acid chains are categorized by level of spe

21 We tested the hypothesis that a single amino acid change (Arg135Gly) in a highly conserv

22 It is documented herein that a single amino acid change at position 439 of the BlaR1 pr

23 wn that complement polymorphisms affecting a single amino acid change cause subtle changes in individ

24 A single amino acid change converting DLD to DWD within PI

25 vealed the two proteins were isoforms, and a single amino acid change distinguished S28 and S29.

26 Furthermore, we show that a single amino acid change in EC2 attenuates Hh-induced Sm

27 A single amino acid change in IR75b is sufficient to recod

28 Importantly, a single amino acid change in the amyloidogenic TDP-43 pep

29 By creating a single amino acid change in the D-Ala-D-Ala ligase enzym

30 This could be explained by a single amino acid change in the filovirus receptor, NPC1

31 e evolved strain, among which we confirmed a single amino acid change in the hexose transporter HXT7

32 oreover, the full-length DDX43 protein, with single amino acid change in the KH domain, had reduced u

33 Our results demonstrate that a single amino acid change in the RRV VP4 gene influences

34 eate a mutant of RRV (RRV(VP4-R446G)) with a single amino acid change in the VP4 protein compared to

35 Furthermore, introducing a single amino acid change into the two nebulin repeats of

36 ted transgenic plants expressing UVR8 with a single amino acid change of tryptophan-285 to alanine.

37 age analysis we examined the effects of this single amino acid change on binding and uptake of Alexa4

38 However, a single amino acid change two residues upstream of the ac

39 ApoE isoforms vary by a single amino acid change, and it is a challenge to disti

40 h a molecular mass of 34.15 kDa, differ by a single amino acid change.

41 rgo profound tuning at the minimal cost of a single amino acid change.

42 difference can be attributed primarily to a single amino acid change: Glu198 on the rat alpha3 subun

43 A single-amino-acid change (ExoRL81A) at the site of ExoR

44 ound that similar to the ROD10/ROD14 Envs, a single-amino-acid change (T568I) in the ectodomain of th

45 ry, and passaging experiments selected for a single-amino-acid change in capsid (CA) that leads to re

46 vity in DNA end resection is attenuated by a single-amino-acid change that reflects a KAP-1 polymorph

47 2 antagonism to an inactive Env protein by a single-amino-acid change.

48 Single amino acid changes around Cys-739 in FL-NCX1 and

49 Single amino acid changes in cps genes encoding glycosyl

50 Further, we show that single amino acid changes in L4 are necessary and suffic

51 These data suggest that single amino acid changes in proteins involved in dendri

52 similar rate but differ in cell shape due to single amino acid changes in the actin homolog MreB.

53 responsive to riboflavin were shown to have single amino acid changes in the FADS domain.

54 Here, we provide definitive evidence that single amino acid changes in the nuclearly encoded F1FO-

55 Single amino acid changes in the SAMHD1-degrading Vpx ma

56 tematic interrogation of mechanisms by which single amino acid changes in various regions of gp120 (i

57 ppeared to destabilize the CypA protein; the single amino acid changes led to rapid degradation of th

58 These data indicate that single amino acid changes that enhance the fusion activi

59 We identified single amino acid changes within A3G in two AGM subspeci

60 itulation of this motif by the addition of a single amino acid conferred targeting function on an N-t

61 Mutations of COX15 causing single amino acid conversions associated with fatal infa

62 missense mutations affecting p.Arg1809 and a single amino acid deletion p.Met922del.

63 erization of the mutations revealed that the single-amino-acid deletion affecting the TEL patch surfa

64 al human mitochondria encodes a 9-mer with a single amino acid difference from P9 with 89% homology t

65 7), are required for GlcN modification and a single amino acid difference in LpxA is responsible for

66 reactive Th1/Th17 cells is hindered due to a single amino acid difference in the OSP(142-161) region

67 We showed that a single amino acid difference in this motif between mamma

68 ng mouse polyomavirus, we demonstrate that a single amino acid difference in VP1 known to shift viral

69 nes, each expressing the same protein with a single amino acid difference, and with all native regula

70 Hence, the puzzle remains: how a single-amino-acid difference between the ApoE3 and ApoE4

71 We previously reported that a single-amino-acid difference between the laboratory-adap

72 y examples for precisely defined motifs with single amino acid differences, and find that the effecti

73 mutant monomer and vice versa revealed that single-amino acid differences between seed and monomer p

74 eal that posttranslational modification of a single amino acid directly modulates the function of dys

75 Here, we describe the consequences of the single amino acid exchange at position 179 in the ankyri

76 An FtsH variant (FtsH(trap)) carrying a single amino acid exchange in the proteolytic center was

77 RNA deamination, generating a channel with a single amino acid exchange located in the inner pore cav

78 CV-1 contained the single amino acid exchange R28E.

79 ereditary spastic paraplegia and explain why single amino acid exchanges lead to a dominant negative

80 Single amino acid exchanges revealed D317 as a critical

81 stic fibrosis is caused by the deletion of a single amino acid (F508) from CFTR and the resulting mis

82 ing mitochondrial proteins by the removal of single amino acids from mitochondrial processing peptida

83 ICP55 also removed single amino acids from mitochondrial proteins known to

84 Humans express a repertoire of single-amino acid genetic variants of SP-A that may be a

85 We examined how a single amino acid, glutamate (GLM), modulates intestinal

86 of TT2 and PAP4 we found that exchange of a single amino acid, Gly/Arg(39) in the R2 domain combined

87 Using collagen ultrafiltration and single amino acid (hydroxyproline) methods, these specim

88 in-2 may be achieved by mutations of crucial single amino acids, i.e. cysteine 128.

89 d toxin CdtB subunit after substitution of a single amino acid in ArtA, while ArtB can form a functio

90 ys, isoallelic strains that varied by only a single amino acid in CovS, and transcriptome analyses to

91 ex are independently associated with CIAG: a single amino acid in HLA-DQB1 (126Q) (P=4.7 x 10(-14), o

92 esistant to lenalidomide but that changing a single amino acid in mouse Crbn to the corresponding hum

93 Previously, we determined that there is a single amino acid in scaffolding protein required for P2

94 emonstrate that the identity and position of single amino acid in short inorganic binding protein-seg

95 A single amino acid in SIRT1, Glu(230), located in a struc

96 A single amino acid in the conserved cis-proline loop of t

97 s show that phosphorylation of the NHE3 at a single amino acid in the distal part of the C-terminus a

98 3 and MsexD2 demonstrated that swapping of a single amino acid in the fatty acyl substrate binding tu

99 In addition, we identified a single amino acid in YopK that is essential for transloc

100 the molecular mechanisms and contribution of single amino acids in OST interaction with its substrate

101 elationships, we created a library of random single-amino-acid IN mutations that could mimic the type

102 coid receptor (GR) isoforms that differ by a single amino acid insertion in the lever arm, a domain t

103 er, elongation pausing during starvation for single amino acids is highly sensitive to the kinetics o

104 Of all nutrients, the single amino acid leucine (Leu) possesses the most marke

105 s the first molecular contact site mapped to single amino acid level between these two proteins.

106 utionary trade off in enzyme function at the single amino acid level.

107 mutations focus on either the entire-gene or single amino-acid level.

108 s further evolved, modern strains acquired a single amino-acid modification within Pla that optimizes

109 Single amino acid modifications identified a novel pepti

110 Thus, single amino acid modifications with no impact on CD55 s

111 r connecting their two active domains, and a single amino acid mutant (F19Y), were used as probes to

112 y, we screened a library of all 361 possible single-amino-acid mutant forms of ST by using the T84 ce

113 We identified single amino acid mutants of alpha-COP that selectively

114 t on ampicillin resistance of ~12,500 unique single amino acid mutants of the TEM-1, TEM-17, TEM-19,

115 -IVa, two of the wild type enzyme and two of single amino acid mutants, each in complex with either a

116 teins, we created a large library of random, single-amino-acid mutants in HIV-1 integrase (IN), cover

117 We discovered that a single amino acid mutation (Met-48 to Phe) in the PRMT1

118 rus, we generated a recombinant virus with a single amino acid mutation at this site through a revers

119 A new methodology termed Single Amino Acid Mutation based change in Binding free

120 A single amino acid mutation in SPA that abrogates assembl

121 bit TrkB kinase activity as a result of this single amino acid mutation in the ATP binding domain.

122 one of these HAstV strains and found that a single amino acid mutation induces a structural change i

123 These observations beg the question of how a single amino acid mutation may have such wide ranging co

124 A single amino acid mutation near the active site of the C

125 inding to human receptors; however, should a single amino acid mutation occur, this would result in s

126 basolateral targeting of TbetaRIII through a single amino acid mutation of proline 826 in the cytosol

127 The single amino acid mutation results in measureable cataly

128 is functionally important in vivo as well: a single amino acid mutation that reduces activity leads t

129 and subsequent experiments confirmed that a single amino acid mutation to the core transcriptional r

130 These studies confirmed that a single amino acid mutation was sufficient to reverse the

131 Single amino-acid mutation of potential signal-transduct

132 We identify a single-amino acid mutation conferring resistance to myco

133 AV1 and AAV8 were modified to bind HS with a single-amino-acid mutation and tested in mice.

134 tem that allows comparison of the effects of single amino acid mutations in the same biochemical back

135 ralization sensitivity of pseudoviruses with single amino acid mutations in various regions of gp120

136 Based on this structure, we identified single amino acid mutations targeted at the binding inte

137 the basis of the structure were confirmed by single amino acid mutations that abolished binding in vi

138 el experimental approach to quantify how all single amino acid mutations to HIV Envelope (Env) affect

139 entify structural differences induced by the single amino acid mutations.

140 Single amino-acid mutations in the putative pore region

141 the variation in integration efficiency upon single amino-acid mutations, and the orientation of tran

142 three independent lines of knockin mice with single-amino acid mutations of conserved class II MHC am

143 Mutation of a single amino acid on a 34-mer PEDF peptide increased min

144 ons mediated by multiple REs, suggesting how single amino acid oncogenic CARD11 mutations can perturb

145 outing of this antigen through exchange of a single amino acid or ablation of an essential autophagy

146 nts of the following analytes: salts, drugs, single amino acids, peptides (from dipeptides to hexapep

147 Single amino acid point mutations in the conserved eIF2a

148 Identifying the effect of single amino acid point mutations on the thermodynamic e

149 s that can bind selectively to proteins with single amino-acid point mutations offer the potential to

150 sulting in 636 novel peptides, including 510 single amino acid polymorphism (SAP) peptides, 2 INDEL p

151 irulence protein SpvD and demonstrate that a single amino acid polymorphism can affect the overall vi

152 Previously we developed SAAPdap (Single Amino Acid Polymorphism Data Analysis Pipeline) a

153 rphism Data Analysis Pipeline) and SAAPpred (Single Amino Acid Polymorphism Predictor) that use a com

154 located within a reading frame can result in single amino acid polymorphisms (SAPs), leading to alter

155 n the context of DNA binding, variation at a single amino acid position promotes divergence of the At

156 illustrate the significance of mutations in single amino-acid position for particular bone tissue pa

157 To determine if this single amino acid (R) influences the pathogenicity of th

158 Introduction of a single amino acid RAF1 mutant (RAF1 Ser259Ala), which re

159 in amino-acid homopolymers that consist of a single amino acid repeated from several to dozens of tim

160 tative monoclonal antibodies revealed that a single amino acid replacement at residue K163 in the Sa

161 We observed that no single amino acid replacement is capable of recreating t

162 unctional roles, we constructed full sets of single amino acid replacement mutants at E402 and R404 a

163 4,000-fold resistance observed was due to a single amino acid replacement, Ala(301) to Ser.

164 ns are vulnerable towards disease-associated single amino acid replacements affecting protein stabili

165 Single amino acid replacements I32V, V47I, and M76L incr

166 Single amino acid replacements locally affect folding an

167 The phenotypic difference mapped to a single amino acid residue at position 162 in the E2 enve

168 Furthermore, substitution of a single amino acid residue in the PRR of the non-human-tr

169 orm chimera and site-directed mutagenesis, a single amino acid residue in this core (Met(25) in ssSPT

170 We further determined that a single amino acid residue substitution in NY1682 hemaggl

171 The mechanism by which a single amino acid residue substitution leads to dysfunct

172 n ovine but not in Culicoides cells due to a single amino acid residue that, most likely, leads to ra

173 Substitution of a single amino acid residue within the degenerin region of

174 enicity thus depends on the identity of this single amino acid residue.

175 a large number of exopeptidases that cleave single amino acid residues from the N-terminus of peptid

176 While previous efforts have identified single amino acid residues in APOBEC3 proteins required

177 or entire PTS1 domains and position-specific single amino acid residues, including residues upstream

178 Enlarging the URS by a single amino acid resulted in increased translational in

179 structural difference between variants was a single amino acid resulting from a codon insertion, and

180 Here we show that changing a single amino acid (S442D) from serine in type 2 EBNA-2 t

181 Here we identify a single amino acid (Ser in type 1 EBV, Asp in type 2 EBV)

182 Changing the polar character of a single amino acid side chain (Ser-228) to a nonpolar res

183 ime due to the reversible light-switching of single amino acid side-chains, adding a dynamic dimensio

184 ocking studies, we found that replacing this single amino acid significantly changed the PPO's substr

185 Herein, we demonstrate that replacement of a single amino acid stereocenter with a stereodynamic nitr

186 ccessful generation of global gene-knockout, single-amino-acid-substituted, as well as floxed mice th

187 t the infectivity of B virus isolates with a single amino acid substitution (D122N) in the IgV-core o

188 study demonstrated that a MACV strain with a single amino acid substitution (F438I) in the transmembr

189 Indeed, this single amino acid substitution (G-->V) at a residue inva

190 e strains carried hly mutations leading to a single amino acid substitution (G299V) or a premature st

191 xic form of diphtheria toxin that contains a single amino acid substitution (G52E).

192 from the same parental stock and differ by a single amino acid substitution (H1047R) caused by a sing

193 t disruption of the SpoIIQ LytM domain via a single amino acid substitution (H120S) impairs engulfmen

194 ression, but this activity was restored by a single amino acid substitution (K186E), which was respon

195 We find that the blue trait maps to a single amino acid substitution (R644W) in an uncharacter

196 Here we show that a naturally occurring single amino acid substitution (tyrosine to cysteine) at

197 For example, a single amino acid substitution (W424G) in the active sit

198 Thus, a single amino acid substitution can significantly alter t

199 This simple switch in mechanism by a single amino acid substitution could potentially generat

200 y minor variants comprised from conservative single amino acid substitution events.

201 A single amino acid substitution evolved together with thi

202 ults demonstrate that a change as small as a single amino acid substitution in a FAD enzyme might res

203 We show that a single amino acid substitution in an abscisic acid-respo

204 s a devastating genetic disorder caused by a single amino acid substitution in beta-globin.

205 s with the disease phenotype that produces a single amino acid substitution in eukaryotic elongation

206 One virus had a single amino acid substitution in Gc.

207 A single amino acid substitution in MgtC that prevents bin

208 he Arabidopsis thaliana accession Cvi-0 to a single amino acid substitution in MITOGEN-ACTIVATED PROT

209 za B/Yamanashi/166/1998 viruses containing a single amino acid substitution in NA generated by revers

210 Both mutations cause a single amino acid substitution in one OPR repeat.

211 Such ability was restored by a single amino acid substitution in position 186 (K186E) t

212 A single amino acid substitution in that domain abolished

213 ant of zebrafish Abcc4 was identified with a single amino acid substitution in the cytoplasmic loop T

214 tetraploid wheat accessions revealed that a single amino acid substitution in the DNA-binding domain

215 in vitro evolution also revealed that just a single amino acid substitution in the envelope can confe

216 We investigated the role of a single amino acid substitution in the hemagglutinin clea

217 Twelve selection steps, each resulting in a single amino acid substitution in the hemagglutinin glob

218 Taken together, the study demonstrates how a single amino acid substitution in the histidine kinase r

219 fied Snf1 alpha subunit with a conservative, single amino acid substitution in the kinase domain is p

220 be reengineered in both TRPV1 orthologs by a single amino acid substitution in the N-terminal ankyrin

221 Thus, a single amino acid substitution in the regulatory domain

222 seems to be intrinsically restricted, and a single amino acid substitution is sufficient to drastica

223 ity of both ALA1 and ALA2 was abolished by a single amino acid substitution known to inactivate the f

224 We engineered a collection of single amino acid substitution mutants at residues (A370

225 A single amino acid substitution of IKZF3 conferred resist

226 ructose 6-P-specific enzyme was started by a single amino acid substitution resulting in negative sel

227 pic analysis of the two iNK TCR types with a single amino acid substitution revealed that the stainin

228 iosynthetic enzyme from IPMDH results from a single amino acid substitution that alters substrate spe

229 t PrP mutants were designed to contain every single amino acid substitution that distinguishes rabbit

230 286A) and fHbp(E313A), which each contains a single amino acid substitution that leads to a marked re

231 accumulation is most likely attributed to a single amino acid substitution that leads to different O

232 se inhibitor 1A (SERPINA1) gene leading to a single amino acid substitution that results in an unfold

233 Resistance to C1 was conferred by a single amino acid substitution within the compound-bindi

234 M) were calculated for nearly every possible single amino acid substitution within this fragment.

235 Furthermore, a single amino acid substitution, N195D, in HTLV-1 SU (Ach

236 of site-specific mutant HAs indicate that a single amino acid substitution, Thr-30 --> Ser, influenc

237 A single amino acid substitution-based adaptive coevolutio

238 n) in which self-assembly was abolished by a single amino acid substitution.

239 t mice and (2) Syt12 knockin mice carrying a single amino-acid substitution [the serine-97-to-alanine

240 To exploit a single amino-acid substitution among the binding pockets

241 We demonstrate that a single amino-acid substitution in a banana lectin, repla

242 esynaptic LTP at mossy-fiber synapses, and a single amino-acid substitution that blocks the cAMP-depe

243 he N-linked glycosylation site is mutated by single-amino-acid substitution are highly attenuated and

244 We identified two single amino acid substitutions (D39V and N90A) that sta

245 find that subunits lacking M4 or containing single amino acid substitutions along an "interacting" f

246 many predictors of the functional impact of single amino acid substitutions are publicly available.

247 eby qualifying mutated epitopes that include single amino acid substitutions as effective vaccines.

248 Single amino acid substitutions at conserved residues we

249 We found that Prf variants with single amino acid substitutions at D1416 in the IHD moti

250 approach and generated mutant receptors with single amino acid substitutions at selected positions of

251 Novel recombinants of Hb S with single amino acid substitutions at the putative axial (r

252 o fibrillate through the N terminus and that single amino acid substitutions can lead to changes in t

253 f transcripts, the mechanisms by which these single amino acid substitutions change gene expression r

254 e OGT but are not fully rescued by OGTs with single amino acid substitutions corresponding to mutatio

255 rrestin recruitment, by different effects of single amino acid substitutions in ACKR3 on arrestin in

256 We use single amino acid substitutions in DAXX that abrogate fo

257 Single amino acid substitutions in p97 have been linked

258 int mutations in their genomes, which led to single amino acid substitutions in proteins of interest.

259 Single amino acid substitutions in the C-terminal membra

260 e multifocal leukoencephalopathy (PML) carry single amino acid substitutions in the domain of the VP1

261 ctivation or inactivation by introduction of single amino acid substitutions in the transmembrane dom

262 Here, we identified single amino acid substitutions in Vps13 (vacuolar prote

263 We show that single amino acid substitutions near the receptor bindin

264 mapping information as a guide to introduce single amino acid substitutions of nine different residu

265 We identified single amino acid substitutions that are likely responsi

266 We identified nine single amino acid substitutions that could not complemen

267 Two single amino acid substitutions that reduced and abolish

268 Single amino acid substitutions to benenodin-1 generate

269 A number of single amino acid substitutions were identified that equ

270 Single amino acid substitutions were introduced into the

271 a) to study the molecular consequences of 16 single amino acid substitutions, classified as pathogeni

272 tion of the Galpha:RGS protein pair based on single amino acid substitutions.

273 in human populations that result in specific single amino acid substitutions.

274 y and genetically characterize in vivo three single amino acid substitutions: beta' E677G, beta V146F

275 ELANE mutations were diverse; there were 65 single amino acid substitutions; 61 of these mutations (

276 and dilated cardiomyopathy that result from single amino-acid substitutions in one of several of the

277 s sequence variants in LMNA, which result in single amino-acid substitutions, were identified in pati

278 struct a library encoding all 9,595 possible single-amino acid substitutions.

279 C-terminal regulatory domain was provided by single-amino-acid substitutions at conserved cysteines (

280 replication, recombinant viruses containing single-amino-acid substitutions in the N protein were re

281 We show that certain single-amino-acid substitutions in the prion protein Sup

282 ts of BamD depletion were partly reversed by single-amino-acid substitutions mapping within the beta-

283 sulting in a set of fragments differing by a single amino acid that remain spatially confined on the

284 a causal locus that mapped to MPC1, changing single amino acids that are conserved throughout eukaryo

285 ric effects emerging from the insertion of a single amino acid, the two alphabeta monomers are rotate

286 Mutational analysis revealed that a single amino acid (Thr(24)) in the extracellular domain

287 ression of USP7 or substitution in ICP0 of a single amino acid to abolish binding to USP7 accelerated

288 findings indicate that paramyxoviruses use a single amino acid to distinguish MDA5 from RIG-I and hav

289 The mutation, a deletion of a single amino acid (V636) from the extreme C terminus of

290 We show that a single amino acid variant in the BC loop of pig nectin-4

291 Many of these variants lead to single amino acid variants (SAVs), and accurate predicti

292 gle nucleotide variants, also referred to as single amino acid variants (SAVs).

293 unrelated individuals differ by about 10,000 single amino acid variants (SAVs).

294 In vivo analysis of single amino acid variants of this chelatase suggests th

295 Results of in vivo and in vitro analyses of single-amino-acid variants affecting a HX11CCXXC(83) mot

296 in Tat-transactivation has been traced to a single amino acid variation between the two proteins, wh

297 d a large-scale structural analysis of human single amino acid variations (SAVs) and demonstrated tha

298 triguingly, replacement of only one specific single amino acid was sufficient for such a monooxygenas

299 , our results point to a critical role for a single amino acid within the membrane-proximal region of

300 in the previous studies, to targeting only a single amino acid without compromising the intensity of