ライフサイエンスコーパス: amino acid replacement

1 olates of the same emm type had an identical amino acid replacement.

2 mutant was then reduced in size by strategic amino acid replacement.

3 idue Asp-83 in catalysis was demonstrated by amino acid replacement.

4 tion acts at many sites of rapid, successive amino acid replacement.

5 an indel event must be compensated by local amino acid replacement.

6 er degree of evolutionary constraint against amino acid replacement.

7 nslocation are essentially unaffected by the amino acid replacement.

8 hat combines protein secondary structure and amino acid replacement.

9 ns, indicating strong positive selection for amino acid replacements.

10 sect orders by purifying selection acting on amino acid replacements.

11 for fimH and papG) for functionally adaptive amino acid replacements.

12 effects of purifying selection on individual amino acid replacements.

13 agnitude of selective forces associated with amino acid replacements.

14 ive as the best round 8 enzyme, which has 13 amino acid replacements.

15 , either by itself or accompanied with other amino acid replacements.

16 number of, sometimes highly nonconservative, amino acid replacements.

17 ons that presumably code for nonconservative amino acid replacements.

18 d nucleotide substitutions did not result in amino acid replacements.

19 coadapted changes is fully explained by two amino acid replacements.

20 acterize the molecular defects caused by the amino acid replacements.

21 inding interfaces are frequently affected by amino acid replacements.

22 d SOD1 monomers showed little sensitivity to amino acid replacements.

23 which Glu-348 is substituted by conservative amino acid replacements.

24 m and divergence of conservative and radical amino acid replacements (a protein-based conservative-ra

25 iately after the acute phase, and found that amino-acid replacements accumulated primarily in Tat CTL

26 mbrial adhesin of Escherichia coli, acquires amino acid replacements adaptive in extraintestinal nich

27 c-site mutations, whereas V97K and Y104K are amino acid replacements adjacent to and outside of the c

28 utant proteins demonstrated that none of the amino acid replacements affected the formation of the ac

29 vulnerable towards disease-associated single amino acid replacements affecting protein stability and

30 fold resistance observed was due to a single amino acid replacement, Ala(301) to Ser.

31 Single amino acid replacements along the entire length of RocA

32 In a comparison of amino-acid replacements among species of the mustard wee

33 ion is employed to demonstrate that a single amino acid replacement analogue of con-T, con-T[K7gamma]

34 conformational changes induced by the single amino acid replacement and generate novel structural inf

35 ection, with positive selection favoring the amino acid replacement and purifying selection maintaini

36 ies of P. gingivalis A7436 hmuR mutants with amino acid replacements and characterized the ability of

37 ly 1 of the 6 genes showed a large number of amino acid replacements and in-frame insertions/deletion

38 However, introduction of 22 amino acid replacements and one deletion, including subs

39 frequent exon deletions and duplications to amino acid replacements and protein truncations, we isol

40 the Drosophila nbs gene, ranging from single amino acid replacements and small in-frame deletions to

41 The result is frequent reversal of amino acid replacements and, at short evolutionary dista

42 Y-linked genes show faster accumulation of amino-acid replacements and loss of expression, compared

43 All 10 of these CTL epitopes accumulated amino-acid replacements and showed evidence of positive

44 <<1.0, suggestive of selective constraint on amino acid replacements, and no estimates were >1.0, eit

45 Empirically derived models of amino acid replacement are employed to study the associa

46 The evolutionary rates of amino acid replacement are significantly higher in the t

47 el" assumes two categories of sites at which amino acid replacements are either neutral or deleteriou

48 An alternative to this is that amino acid replacements are spatially clustered and this

49 and strengthen the hypothesis that parallel amino-acid replacements are associated with adaptive cha

50 lso able to determine the 3D distribution of amino acid replacements as they accumulated during evolu

51 hat encodes a variant protein with a radical amino acid replacement associated with the two FLC haplo

52 h hormone and receptor both exhibit a single amino acid replacement at a site known to have functiona

53 tion generally tolerates variable amounts of amino acid replacement at different positions in a prote

54 Moreover, amino acid replacement at K163 was not highlighted by st

55 We found that every amino acid replacement at N381 destroyed Tsr function, a

56 e, liaS, resulting in an arginine-to-glycine amino acid replacement at position 135 of LiaS (LiaS(R13

57 monoclonal antibodies revealed that a single amino acid replacement at residue K163 in the Sa antigen

58 explained by a tendency for similar rates of amino acid replacement at sites that are nearby in prote

59 position undergo predictable change after an amino acid replacement at that position.

60 The SWS1 pigment contains no amino acid replacement at the currently known 25 critica

61 3(2H)-pyridinone moiety (the "@-unit") as an amino acid replacement at the i - 1 or i + 4 positions r

62 SSB-113 carries a single amino acid replacement at the penultimate residue of the

63 otide patterns consistent with selection for amino acid replacement at the putative antigen-binding s

64 adaptations seem to have occurred largely by amino acid replacements at 12 sites, and most of those a

65 long with the fimA loci), they acquire point amino acid replacements at a higher rate than either hou

66 et vision in others has evolved by different amino acid replacements at approximately 10 specific sit

67 Receptors with proline or charged amino acid replacements at critical hydrophobic packing

68 We created random amino acid replacements at each of the 14 connector resi

69 rine receptor, Tsr, we generated a series of amino acid replacements at each residue of the AS1 and A

70 Several amino acid replacements at each residue were silent, but

71 duplications and losses and show convergent amino acid replacements at important points along the an

72 and characterized CheA and CheW mutants with amino acid replacements at key interface 2 residues.

73 dominant-negative phenotype; interestingly, amino acid replacements at multiple sites were less effe

74 ly neutral or that positive selection drives amino acid replacements at only a subset of the loci.

75 Circular dichroism spectra showed that the amino acid replacements at position 86 did not change th

76 of human carbonic anhydrase II (HCA II) with amino acid replacements at residues in contact with wate

77 enic escape resulted from individual, single amino acid replacements at sites well separated in curre

78 One set of P1 mutants identified amino acid replacements at surface-exposed residues dist

79 tes are caused mainly by additive effects of amino acid replacements at ten sites.

80 stic interactions frequently result in rapid amino acid replacements at the protein-protein interface

81 (ii) Amino acid replacements at the putative Aer methylation

82 ed to a single-ring species by site-directed amino acid replacements at the ring interface and that t

83 ructed and characterized all possible single amino acid replacements at the Tsr control cable residue

84 cted and characterized mutant receptors with amino acid replacements at the two nearly invariant hair

85 critical for Tsr function, because only two amino acid replacements at this residue abrogated serine

86 n missense mutations, F417S, and a series of amino acid replacements at this site (ie, F417W, F417Y,

87 , we created and characterized a full set of amino acid replacements at this Tsr residue.

88 henotype are mainly attributable to repeated amino acid replacements at two epistatically interacting

89 Amino acid replacements at Tyr211 and Gln255, which part

90 explain experimental mutagenesis studies of amino acid replacements away from the association interf

91 me of chimpanzees with as much as 30% of all amino acid replacements being adaptive.

92 o acids than parallel changes, and divergent amino acid replacements between the primates were signif

93 FB alleles were not identical, harbouring 12 amino-acid replacements between those of P. tenella SFB(

94 ensive map of sites within PA where a single amino acid replacement can give a DN phenotype, we used

95 These results demonstrate that destabilizing amino acid replacements can be accommodated in a native

96 mall increases in expression and even single amino acid replacements can be subject to natural select

97 We also asked why single amino acid replacements can so destabilize the native st

98 ngle codon site, because a large fraction of amino acid replacements cannot be achieved after just on

99 age and for the fact that different types of amino acid replacement come to clinical attention with d

100 ining on Y chromosomes have accumulated more amino acid replacements, contain more unpreferred change

101 different proteins, the evolutionary rate of amino acid replacements correlates negatively with WM in

102 acterially expressed wild-type StAR and four amino acid replacement/deletion mutants that cause lipoi

103 A-site motif of SGDEF and analysis of single amino acid replacements demonstrated that the first posi

104 ociated binding energies for the flavin, the amino acid replacements destabilize both the oxidized an

105 nced digestive efficiencies through parallel amino acid replacements driven by darwinian selection.

106 We propose an alternative model of amino acid replacement during protein evolution based up

107 caled selection intensity (gamma = N(e)s) of amino acid replacements eligible to become polymorphic o

108 The P11L amino acid replacement encoded by the minor allele creat

109 Several predicted amino acid replacements encoded by bovine TLR2 and TLR6,

110 Amino acid replacements encoded by the prion protein gen

111 None of the other 18 amino acid replacements engineered here showed normal ch

112 of UV pigments in some species are caused by amino acid replacements F49V/F86S/L116V/S118A and S90C,

113 he contemporary frog pigment is explained by amino acid replacements F86M, V91I, T93P, V109A, E113D,

114 Compared with the absence of OPN1LW amino acid replacement fixation since divergence from ch

115 ction at the molecular level is an excess of amino acid replacement fixed differences per replacement

116 has identified phenylalanine as the optimal amino acid replacement for H24 in the context of apo sta

117 We examined inferred amino acid replacements for 16 genes that encode the pro

118 nine analogues bearing natural or unnatural amino acid replacements for valine B12 by chemical synth

119 Sequence analysis revealed that a single amino acid replacement from aspartic acid to asparagine

120 he beta(2)-adrenergic receptor (beta(2)-AR), amino acid replacements guided by molecular modeling wer

121 While there is compelling evidence that the amino acid replacement has been a target of positive sel

122 Here, effects of other amino acid replacements have been explored using a foldi

123 McDonald-Kreitman-based tests) indicate that amino acid replacements have contributed disproportionat

124 We estimate that approximately 46% of amino acid replacements have N(e)s < 2, approximately 84

125 Single amino acid replacements I32V, V47I, and M76L increased t

126 Mutants containing a single amino acid replacement identified the following 14 resid

127 We studied 4 key amino acid replacements implicated in pyrimethamine resi

128 perimental evidence documenting an unnatural amino acid replacement in a GPCR expressed in its native

129 For any mutation due to a single amino acid replacement in a protein, the method provides

130 sted the occurrence of somatic mutations and amino acid replacement in complementarity-determining re

131 elopment, we created mice harboring a single amino acid replacement in GATA-4 that impairs its physic

132 +) T cells is a dominant force driving early amino acid replacement in HCV viral populations.

133 strains to test the hypothesis that a single amino acid replacement in PBP2X conferred a fitness adva

134 enzylpenicillin, the strain with a Pro601Leu amino acid replacement in PBP2X that confers reduced bet

135 The process of amino acid replacement in proteins is context-dependent,

136 Caused by a single amino acid replacement in the arginine repressor, these

137 A second amino acid replacement in the same HAMP packing layer al

138 We propose that this single amino acid replacement in the selectivity filter made DM

139 e MastR-T74D mutant, which contains a single amino acid replacement in the TSD motif.

140 A mutation causing an amino acid replacement in this desaturase results in los

141 lity in vivo In summary, we show that single amino acid replacements in a regulatory accessory protei

142 e least mutual constraint on nonconservative amino acid replacements in both overlapping coding seque

143 cation by evidence of positive selection and amino acid replacements in carbohydrate-recognition doma

144 nce in yeast are related when the equivalent amino acid replacements in Cln3p and Btn1p are compared.

145 ies being recurrently recruited to identical amino acid replacements in distant lineages.

146 he resistance profiles conferred by specific amino acid replacements in HIV-2 reverse transcriptase.

147 strategy for predicting the set of possible amino acid replacements in HIV.

148 Over 100 amino acid replacements in human Cu,Zn superoxide dismut

149 , and this inhibition was relieved by single amino acid replacements in IMP dehydrogenase.

150 Collectively, these data show that specific amino acid replacements in motif B confer broad-spectrum

151 irus type-1 (HIV-1) containing random single amino acid replacements in motif B of reverse transcript

152 We have estimated the selective effects of amino acid replacements in natural populations by compar

153 Amino acid replacements in only one of these regions enh

154 properties of mutant Tsr receptors that had amino acid replacements in packing layer 3 of the HAMP b

155 Virtually all analyzed strains had single amino acid replacements in penicillin-binding protein 2X

156 rmined that 2 of the 17 epitopes accumulated amino acid replacements in SIV-infected macaques by the

157 ii) extensions to the N and C termini, (iii) amino acid replacements in surface residues, (iv) tandem

158 57BL/6 and TCR alpha transgenic mice, single amino acid replacements in TCR-contact residues of the V

159 Twenty-two single amino acid replacements in TFIIB were defined and charac

160 Three amino acid replacements in the Aer-PAS domain, S28G, A65

161 of the function of BirA variants with single amino acid replacements in the alternative dimerization

162 b57, entailed a significant concentration of amino acid replacements in the complementarity-determini

163 Several amino acid replacements in the HAMP domain of Tsr, parti

164 large, statistically significant, number of amino acid replacements in the mature protein coding reg

165 The Guizhou/China cVDPV strains shared 4 amino acid replacements in the NAg sites: 3 located at t

166 We brought to light that single amino acid replacements in the plastoquinone (PQ)-bindin

167 ng our hypothesis that one or a few specific amino acid replacements in the protein are necessary to

168 evolutionary analyses suggest that specific amino acid replacements in the SWS1 and SWS2 pigments, r

169 Amino acid replacements in the Tar trimer contact region

170 The mutant heavy (H) chains had amino acid replacements in the V(H) complementarity-dete

171 Single amino acid replacements in the ZBD (H33A and C36S) resul

172 atio of silent substitutions in set genes to amino acid replacements in their products suggests that

173 imarily from changes in the position of, and amino acid replacements in, a helix in the beta-barrel d

174 Many of the amino-acid replacements in these epitopes reduced or eli

175 SIFT analyses of nonsynonymous SNPs encoding amino acid replacements indicated that the majority of t

176 Single and double amino acid replacements involving arginine and/or aromat

177 ons of the substitution process, the rate of amino acid replacement is 30.4 x 10(-10)/site/year when

178 We observed that no single amino acid replacement is capable of recreating the rang

179 However, a relatively high rate of amino acid replacement is observed in the polymerase aci

180 vidence that a significant fraction of fixed amino acid replacements is neutral or nearly neutral or

181 The well-known ADH-Slow (S)/Fast (F) amino acid replacement leads to a twofold increase in ac

182 Single amino acid replacements locally affect folding and unfol

183 tween protein and chromophore induced by the amino-acid replacements, lowered the energy gap between

184 thologous proteins was characterized with 34 amino acid replacement matrices, sequence context analys

185 Conservative amino acid replacement may reconcile the fast evolutiona

186 on transport chain components, these encoded amino acid replacements may be viewed as part of a serie

187 ptors, particularly those with a hydrophobic amino acid replacement, may not bind CheW/CheA because t

188 a) sequence (RKPPSGKK [aa 162 to 169]) by an amino acid replacement method.

189 o acids will extend the use of the unnatural amino acid replacement methodology to amino acids that a

190 Nearly all of the amino acid replacements most significantly correlated wi

191 account for these observations, the rate of amino acid replacement must have been eight or more time

192 domain in the C terminus of AvrXa10 by using amino acid replacement mutagenesis.

193 cy of our UmuC(V) model by investigating how amino acid replacement mutants affect lesion bypass effi

194 al roles, we constructed full sets of single amino acid replacement mutants at E402 and R404 and char

195 These data suggest that the StAR amino acid replacement mutants that cause lipoid CAH are

196 One (mutC216(F97C)) of eight single-amino-acid replacement mutants identified yielded a gene

197 The results showed that all of the single-amino-acid-replacement mutants exhibited either reduced

198 llia receptors that remain intact have fixed amino acid replacement mutations at a higher rate relati

199 ells was supported by the strong bias toward amino acid replacement mutations in ACPA(+) antibodies a

200 utation and the preferential accumulation of amino acid replacement mutations in complementarity dete

201 We found a statistically significant bias of amino acid replacement mutations to the complementarity-

202 Common heavy-light chain combinations and amino acid replacement mutations were seen for clones wi

203 We found 14 different mutations, including 7 amino acid replacement mutations.

204 to determine the functional significance of amino acid replacements observed in the human population

205 Some amino acid replacements occur at or adjacent to sites at

206 Amino acid replacements occur convergently in domains th

207 Parallel amino acid replacements occurred at the same sites in th

208 netic analysis of coding sequences show that amino acid replacements occurred in early mammalian evol

209 The major episode of enhanced amino-acid replacement occurred after the separation of

210 Amino acid replacement of any one of these three loop re

211 expressed protein ligation (EPL) and in vivo amino acid replacement of tryptophans with tryptophan (T

212 exert positive Darwinian selection favoring amino acid replacements of an epitope of simian immunode

213 Both mutants contain single amino acid replacements of residues predicted to be on t

214 The impact of an amino acid replacement on the organism's fitness can var

215 further tested local and nonlocal effects of amino acid replacements on helix-coil dynamics.

216 emonstrate that understanding the effects of amino acid replacements on ligand binding requires measu

217 The effects of amino acid replacements on lipid association of the C-te

218 we highlighted the effects of large-to-small amino acid replacements on rates for ligand entry and ex

219 The effects of amino acid replacements on the backbone dynamics of bovi

220 and VK247, which differ by three diagnostic amino acid replacements, one in each of the 5' and 3' te

221 Nonlocal effects of amino acid replacements only influence helix unfolding (

222 On the basis of systematic amino acid replacements, only five YSA residues appear t

223 Preparation may consist of amino acid replacements or changing solution conditions

224 expectedly, positive Darwinian selection for amino acid replacements outside the active site of JGW p

225 the McDonald-Kreitman (MK) test to show that amino acid replacement polymorphism in animal mitochondr

226 In Est-6, there are nine amino acid replacement polymorphisms, one of which accou

227 12A has low diversity, but many variants are amino acid replacements, possibly due to independent sel

228 ween secondary structure environment and the amino acid replacement process is also observed.

229 Amino acid replacements produced different constellation

230 Arabidopsis 43-kD Rubisco activase with the amino acid replacements Q111E and Q111D in a phosphate-b

231 in cluster I of the rpoB gene, resulting in amino acid replacements (Q469R, H482R, H482Y, or S487L)

232 epresentation of nucleotide changes yielding amino acid replacement (R mutations), nor was there any

233 or of CDR (complementary determining region) amino acid replacement (R) mutations.

234 Unexpectedly, amino acid replacement R488I, occurring at a heptad a po

235 40 x 10 A(3) contiguous spatial clusters for amino acid replacement rate estimation.

236 Amino acid replacement rate matrices are a crucial compo

237 ple, fast and accurate procedure to estimate amino acid replacement rate matrices from large data set

238 actual data under study; however, estimating amino acid replacement rate matrices requires large prot

239 oteins or taxa with optimized, data-specific amino acid replacement rate matrices.

240 ty that different time distances of the same amino acid replacement rate matrix lead to the same grou

241 A statistically significant increase in the amino acid replacement rate was observed in epitopes ver

242 COX8L have also undergone an acceleration in amino acid replacement rates in anthropoid primates.

243 patial autocorrelation was observed for site amino acid replacement rates in vasopressin receptor fam

244 atural selection would drastically constrain amino acid replacement rates of CYC and COX.

245 mmals, CYC and COX show markedly accelerated amino acid replacement rates, with the COX acceleration

246 erlapping sub-alignments prior to estimating amino acid replacement rates.

247 s observed in algal mutants hosting a single amino acid replacement residing in a D1 domain far from

248 ese studies show that functionally important amino acid replacements result in substrate discriminati

249 Furthermore, amino acid replacements revealed that most residues in t

250 tion analysis of RLF derivatives with single amino acid replacements revealed that the most important

251 Subsequent Pro234 amino acid replacement reveals its participation in both

252 tates that positive selection in favor of an amino acid replacement should often cause a burst of two

253 Consequently, amino acid replacements should occur at a higher rate in

254 through proteins retain function and contain amino acid replacements similar to those derived from en

255 and divergence between synonymous sites and amino acid replacement sites in a gene is potentially in

256 ivalents iron and cobalt, with several small amino acid replacements still enabling robust uptake.

257 No amino acid replacement substitutions were indicated in a

258 equence variation includes a minimum of five amino acid replacement substitutions; (4) segregation of

259 dition, the ratio of silent substitutions to amino acid replacements suggests that a short segment in

260 ed through a single hydrophobic-to-ionizable amino acid replacement that generates a partially buried

261 larly strong association with the process of amino acid replacement that it experiences.

262 sequenced the rhodopsin gene to identify the amino acid replacements that affect shifts in maximum wa

263 of beneficial mutations is 47.7%, and among amino acid replacements that become fixed the average pr

264 97A (threonine to alanine) but also by other amino acid replacements that cause minor lambda(max)-shi

265 ptor functionality was rescued by additional amino acid replacements that differed among poison frog

266 uences of equine and canine viruses revealed amino acid replacements that distinguished the viruses f

267 Amino acid replacements that enable activation without e

268 ased, particularly among those that generate amino acid replacements that enhance affinity of the B c

269 PD mutations are missense mutations, causing amino acid replacements that entail deficiency of G6PD e

270 olerance of the KDO8PP catalytic platform to amino acid replacements that in turn influence substrate

271 tion was suggested by finding some recurrent amino acid replacements that may contribute increased af

272 Most of the amino acid replacements that occurred in the Nasonia lin

273 The trace also hypothesizes amino acid replacements that preceded the first recorded

274 ion of amino acid composition occurs through amino acid replacements that result in a balanced loss a

275 es that evolved under positive selection and amino acid replacements that result in radical physicoch

276 A series of quadruple amino acid replacements that spanned the helix propensit

277 Eight of the amino-acid replacements that occurred on the lineage lea

278 t accessibility and secondary structure with amino acid replacement, the process of protein evolution

279 Single amino acid replacements throughout the targeted region c

280 h showed that in Daphnia pulex, the ratio of amino acid replacement to silent substitution in mitocho

281 might allow more neutral and nearly neutral amino acid replacements to be fixed.

282 possibility is that there is no tendency for amino acid replacements to be spatially clustered during

283 he crystal structure and kinetic analyses of amino acid replacement variants.

284 unusual haplotype structure associated with amino acid replacement variation in exon 3 that is consi

285 Alanine scanning followed by amino acid replacements was used to construct mutants of

286 , strains of the same emm type with the same amino acid replacement were clonally related by descent.

287 ecombinant InhA proteins with defined single amino acid replacements were expressed in Escherichia co

288 Three amino acid replacements were made at each site, the firs

289 Amino acid replacements were mapped onto the crystal str

290 as determined, and structural changes due to amino acid replacements were monitored by nuclear magnet

291 Pronounced genetic changes, including excess amino acid replacements, were detected in all population

292 The mutation in TG01 caused an amino acid replacement, whereas the mutation in TG10 res

293 Fractions of amino acid replacements which reduce fitness by >10(-2),

294 ys of human and frog nAChR revealed that one amino acid replacement, which evolved three times in poi

295 to understand the probability that a random amino acid replacement will lead to a protein's function

296 ese alpha-spectrin peptides that have single amino acid replacements with a beta-spectrin model pepti

297 models do not predict spatial clustering of amino acid replacements with respect to tertiary structu

298 However, single, double, or triple amino acid replacements within the native CAX1 Cad did n

299 Deletion mutants and single-site amino acid replacements within the propeptide of a carbo

300 s may evade the CTL response by accumulating amino-acid replacements within CTL epitopes.