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1 mutant was then reduced in size by strategic amino acid replacement.
2 idue Asp-83 in catalysis was demonstrated by amino acid replacement.
3 tion acts at many sites of rapid, successive amino acid replacement.
4  an indel event must be compensated by local amino acid replacement.
5 er degree of evolutionary constraint against amino acid replacement.
6 nslocation are essentially unaffected by the amino acid replacement.
7 hat combines protein secondary structure and amino acid replacement.
8 tide substitutions in both regions result in amino-acid replacement.
9 sect orders by purifying selection acting on amino acid replacements.
10 for fimH and papG) for functionally adaptive amino acid replacements.
11 effects of purifying selection on individual amino acid replacements.
12 agnitude of selective forces associated with amino acid replacements.
13 ive as the best round 8 enzyme, which has 13 amino acid replacements.
14 , either by itself or accompanied with other amino acid replacements.
15 number of, sometimes highly nonconservative, amino acid replacements.
16 ons that presumably code for nonconservative amino acid replacements.
17 d nucleotide substitutions did not result in amino acid replacements.
18  coadapted changes is fully explained by two amino acid replacements.
19 acterize the molecular defects caused by the amino acid replacements.
20 inding interfaces are frequently affected by amino acid replacements.
21 d SOD1 monomers showed little sensitivity to amino acid replacements.
22 which Glu-348 is substituted by conservative amino acid replacements.
23 ns, indicating strong positive selection for 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                           In a comparison of amino-acid replacements among species of the mustard wee
32 ion is employed to demonstrate that a single amino acid replacement analogue of con-T, con-T[K7gamma]
33 conformational changes induced by the single amino acid replacement and generate novel structural inf
34 ection, with positive selection favoring the amino acid replacement and purifying selection maintaini
35 ies of P. gingivalis A7436 hmuR mutants with amino acid replacements and characterized the ability of
36 ly 1 of the 6 genes showed a large number of amino acid replacements and in-frame insertions/deletion
37                  However, introduction of 22 amino acid replacements and one deletion, including subs
38  frequent exon deletions and duplications to amino acid replacements and protein truncations, we isol
39 the Drosophila nbs gene, ranging from single amino acid replacements and small in-frame deletions to
40           The result is frequent reversal of amino acid replacements and, at short evolutionary dista
41   Y-linked genes show faster accumulation of amino-acid replacements and loss of expression, compared
42     All 10 of these CTL epitopes accumulated amino-acid replacements and showed evidence of positive
43 <<1.0, suggestive of selective constraint on amino acid replacements, and no estimates were >1.0, eit
44                Empirically derived models of amino acid replacement are employed to study the associa
45                    The evolutionary rates of amino acid replacement are significantly higher in the t
46 el" assumes two categories of sites at which amino acid replacements are either neutral or deleteriou
47               An alternative to this is that amino acid replacements are spatially clustered and this
48  and strengthen the hypothesis that parallel amino-acid replacements are associated with adaptive cha
49 lso able to determine the 3D distribution of amino acid replacements as they accumulated during evolu
50 hat encodes a variant protein with a radical amino acid replacement associated with the two FLC haplo
51 h hormone and receptor both exhibit a single amino acid replacement at a site known to have functiona
52 tion generally tolerates variable amounts of amino acid replacement at different positions in a prote
53                                    Moreover, amino acid replacement at K163 was not highlighted by st
54                          We found that every amino acid replacement at N381 destroyed Tsr function, a
55 onism is directly related to the size of the amino acid replacement at position 121, and it can be re
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                                              Amino acid replacements at one site in this region were
75 ly neutral or that positive selection drives amino acid replacements at only a subset of the loci.
76   Circular dichroism spectra showed that the amino acid replacements at position 86 did not change th
77 of human carbonic anhydrase II (HCA II) with amino acid replacements at residues in contact with wate
78 enic escape resulted from individual, single amino acid replacements at sites well separated in curre
79             One set of P1 mutants identified amino acid replacements at surface-exposed residues dist
80 tes are caused mainly by additive effects of amino acid replacements at ten sites.
81 stic interactions frequently result in rapid amino acid replacements at the protein-protein interface
82                                         (ii) Amino acid replacements at the putative Aer methylation
83 ed to a single-ring species by site-directed amino acid replacements at the ring interface and that t
84 ructed and characterized all possible single amino acid replacements at the Tsr control cable residue
85 cted and characterized mutant receptors with amino acid replacements at the two nearly invariant hair
86  critical for Tsr function, because only two amino acid replacements at this residue abrogated serine
87 n missense mutations, F417S, and a series of amino acid replacements at this site (ie, F417W, F417Y,
88 , we created and characterized a full set of amino acid replacements at this Tsr residue.
89 henotype are mainly attributable to repeated amino acid replacements at two epistatically interacting
90                                              Amino acid replacements at Tyr211 and Gln255, which part
91  explain experimental mutagenesis studies of amino acid replacements away from the association interf
92 me of chimpanzees with as much as 30% of all amino acid replacements being adaptive.
93 o acids than parallel changes, and divergent amino acid replacements between the primates were signif
94 FB alleles were not identical, harbouring 12 amino-acid replacements between those of P. tenella SFB(
95 ensive map of sites within PA where a single amino acid replacement can give a DN phenotype, we used
96 These results demonstrate that destabilizing amino acid replacements can be accommodated in a native
97 mall increases in expression and even single amino acid replacements can be subject to natural select
98                     We also asked why single amino acid replacements can so destabilize the native st
99 ngle codon site, because a large fraction of amino acid replacements cannot be achieved after just on
100 age and for the fact that different types of amino acid replacement come to clinical attention with d
101 ining on Y chromosomes have accumulated more amino acid replacements, contain more unpreferred change
102 different proteins, the evolutionary rate of amino acid replacements correlates negatively with WM in
103 acterially expressed wild-type StAR and four amino acid replacement/deletion mutants that cause lipoi
104 A-site motif of SGDEF and analysis of single amino acid replacements demonstrated that the first posi
105 ociated binding energies for the flavin, the amino acid replacements destabilize both the oxidized an
106 nced digestive efficiencies through parallel amino acid replacements driven by darwinian selection.
107           We propose an alternative model of amino acid replacement during protein evolution based up
108 caled selection intensity (gamma = N(e)s) of amino acid replacements eligible to become polymorphic o
109                                     The P11L amino acid replacement encoded by the minor allele creat
110                            Several predicted amino acid replacements encoded by bovine TLR2 and TLR6,
111                                              Amino acid replacements encoded by the prion protein gen
112                         None of the other 18 amino acid replacements engineered here showed normal ch
113 of UV pigments in some species are caused by amino acid replacements F49V/F86S/L116V/S118A and S90C,
114 he contemporary frog pigment is explained by amino acid replacements F86M, V91I, T93P, V109A, E113D,
115          Compared with the absence of OPN1LW amino acid replacement fixation since divergence from ch
116 ction at the molecular level is an excess of amino acid replacement fixed differences per replacement
117  has identified phenylalanine as the optimal amino acid replacement for H24 in the context of apo sta
118                         We examined inferred amino acid replacements for 16 genes that encode the pro
119  nine analogues bearing natural or unnatural amino acid replacements for valine B12 by chemical synth
120     Sequence analysis revealed that a single amino acid replacement from aspartic acid to asparagine
121 he beta(2)-adrenergic receptor (beta(2)-AR), amino acid replacements guided by molecular modeling wer
122  While there is compelling evidence that the amino acid replacement has been a target of positive sel
123                       Here, effects of other amino acid replacements have been explored using a foldi
124 McDonald-Kreitman-based tests) indicate that amino acid replacements have contributed disproportionat
125        We estimate that approximately 46% of amino acid replacements have N(e)s < 2, approximately 84
126                                       Single amino acid replacements I32V, V47I, and M76L increased t
127                  Mutants containing a single amino acid replacement identified the following 14 resid
128                             We studied 4 key amino acid replacements implicated in pyrimethamine resi
129 perimental evidence documenting an unnatural amino acid replacement in a GPCR expressed in its native
130             For any mutation due to a single amino acid replacement in a protein, the method provides
131 sted the occurrence of somatic mutations and amino acid replacement in complementarity-determining re
132 elopment, we created mice harboring a single amino acid replacement in GATA-4 that impairs its physic
133 +) T cells is a dominant force driving early amino acid replacement in HCV viral populations.
134                               The process of amino acid replacement in proteins is context-dependent,
135                           Caused by a single amino acid replacement in the arginine repressor, these
136 unusually strong purifying selection against amino acid replacement in the IDH enzyme.
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                        A mutation causing an amino acid replacement in this desaturase results in los
140                                  The rate of amino acid replacements in a lineage appears to be 1.0 x
141 e least mutual constraint on nonconservative amino acid replacements in both overlapping coding seque
142 cation by evidence of positive selection and amino acid replacements in carbohydrate-recognition doma
143 nce in yeast are related when the equivalent amino acid replacements in Cln3p and Btn1p are compared.
144 ies being recurrently recruited to identical amino acid replacements in distant lineages.
145 he resistance profiles conferred by specific amino acid replacements in HIV-2 reverse transcriptase.
146  strategy for predicting the set of possible amino acid replacements in HIV.
147                                     Over 100 amino acid replacements in human Cu,Zn superoxide dismut
148  Collectively, these data show that specific amino acid replacements in motif B confer broad-spectrum
149 irus type-1 (HIV-1) containing random single amino acid replacements in motif B of reverse transcript
150   We have estimated the selective effects of amino acid replacements in natural populations by compar
151                                              Amino acid replacements in only one of these regions enh
152  properties of mutant Tsr receptors that had amino acid replacements in packing layer 3 of the HAMP b
153 rmined that 2 of the 17 epitopes accumulated amino acid replacements in SIV-infected macaques by the
154 ii) extensions to the N and C termini, (iii) amino acid replacements in surface residues, (iv) tandem
155 57BL/6 and TCR alpha transgenic mice, single amino acid replacements in TCR-contact residues of the V
156                            Twenty-two single amino acid replacements in TFIIB were defined and charac
157                                        Three amino acid replacements in the Aer-PAS domain, S28G, A65
158 of the function of BirA variants with single amino acid replacements in the alternative dimerization
159 b57, entailed a significant concentration of amino acid replacements in the complementarity-determini
160                                      Several amino acid replacements in the HAMP domain of Tsr, parti
161     Previously, we observed a high number of amino acid replacements in the human COX IV subunit comp
162  large, statistically significant, number of amino acid replacements in the mature protein coding reg
163     The Guizhou/China cVDPV strains shared 4 amino acid replacements in the NAg sites: 3 located at t
164  peptides that were scrambled or had certain amino acid replacements in the predicted integrin-bindin
165 ng our hypothesis that one or a few specific amino acid replacements in the protein are necessary to
166                                       Single amino acid replacements in the putative hydrophobic core
167  evolutionary analyses suggest that specific amino acid replacements in the SWS1 and SWS2 pigments, r
168                                              Amino acid replacements in the Tar trimer contact region
169              The mutant heavy (H) chains had amino acid replacements in the V(H) complementarity-dete
170                                       Single amino acid replacements in the ZBD (H33A and C36S) resul
171 atio of silent substitutions in set genes to amino acid replacements in their products suggests that
172 imarily from changes in the position of, and amino acid replacements in, a helix in the beta-barrel d
173                                  Many of the amino-acid replacements in these epitopes reduced or eli
174 SIFT analyses of nonsynonymous SNPs encoding amino acid replacements indicated that the majority of t
175 unctions responded differently to individual amino acid replacements, indicating that they were disti
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 thologous proteins was characterized with 34 amino acid replacement matrices, sequence context analys
184                                 Conservative amino acid replacement may reconcile the fast evolutiona
185 on transport chain components, these encoded amino acid replacements may be viewed as part of a serie
186 ptors, particularly those with a hydrophobic amino acid replacement, may not bind CheW/CheA because t
187 a) sequence (RKPPSGKK [aa 162 to 169]) by an amino acid replacement method.
188 o acids will extend the use of the unnatural amino acid replacement methodology to amino acids that a
189                            Nearly all of the amino acid replacements most significantly correlated wi
190  account for these observations, the rate of amino acid replacement must have been 15 or more times g
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                          Single and multiple amino acid replacements of Cct6p were constructed by oli
214                  Both mutants contain single amino acid replacements of residues predicted to be on t
215                             The impact of an amino acid replacement on the organism's fitness can var
216 further tested local and nonlocal effects of amino acid replacements on helix-coil dynamics.
217 emonstrate that understanding the effects of amino acid replacements on ligand binding requires measu
218                               The effects of amino acid replacements on lipid association of the C-te
219 we highlighted the effects of large-to-small amino acid replacements on rates for ligand entry and ex
220                               The effects of amino acid replacements on the backbone dynamics of bovi
221 gest that fully understanding the effects of amino acid replacements on the functional and thermodyna
222  and VK247, which differ by three diagnostic amino acid replacements, one in each of the 5' and 3' te
223                          Nonlocal effects of amino acid replacements only influence helix unfolding (
224                   On the basis of systematic amino acid replacements, only five YSA residues appear t
225                   Preparation may consist of amino acid replacements or changing solution conditions
226 expectedly, positive Darwinian selection for amino acid replacements outside the active site of JGW p
227 the McDonald-Kreitman (MK) test to show that amino acid replacement polymorphism in animal mitochondr
228                     In Est-6, there are nine amino acid replacement polymorphisms, one of which accou
229 12A has low diversity, but many variants are amino acid replacements, possibly due to independent sel
230 ween secondary structure environment and the amino acid replacement process is also observed.
231                                              Amino acid replacements produced different constellation
232  Arabidopsis 43-kD Rubisco activase with the amino acid replacements Q111E and Q111D in a phosphate-b
233  in cluster I of the rpoB gene, resulting in amino acid replacements (Q469R, H482R, H482Y, or S487L)
234 epresentation of nucleotide changes yielding amino acid replacement (R mutations), nor was there any
235 or of CDR (complementary determining region) amino acid replacement (R) mutations.
236                                Unexpectedly, amino acid replacement R488I, occurring at a heptad a po
237 40 x 10 A(3) contiguous spatial clusters for amino acid replacement rate estimation.
238                                              Amino acid replacement rate matrices are a crucial compo
239 ple, fast and accurate procedure to estimate amino acid replacement rate matrices from large data set
240 actual data under study; however, estimating amino acid replacement rate matrices requires large prot
241 oteins or taxa with optimized, data-specific amino acid replacement rate matrices.
242 ty that different time distances of the same amino acid replacement rate matrix lead to the same grou
243  A statistically significant increase in the amino acid replacement rate was observed in epitopes ver
244 COX8L have also undergone an acceleration in amino acid replacement rates in anthropoid primates.
245 patial autocorrelation was observed for site amino acid replacement rates in vasopressin receptor fam
246 atural selection would drastically constrain amino acid replacement rates of CYC and COX.
247 mmals, CYC and COX show markedly accelerated amino acid replacement rates, with the COX acceleration
248 erlapping sub-alignments prior to estimating amino acid replacement rates.
249 ese studies show that functionally important amino acid replacements result in substrate discriminati
250                                 Furthermore, amino acid replacements revealed that most residues in t
251 tion analysis of RLF derivatives with single amino acid replacements revealed that the most important
252                            Subsequent Pro234 amino acid replacement reveals its participation in both
253 tates that positive selection in favor of an amino acid replacement should often cause a burst of two
254                                Consequently, amino acid replacements should occur at a higher rate in
255 through proteins retain function and contain amino acid replacements similar to those derived from en
256  and divergence between synonymous sites and amino acid replacement sites in a gene is potentially in
257 ivalents iron and cobalt, with several small amino acid replacements still enabling robust uptake.
258 ese clades are distinguished by a cluster of amino acid replacement substitutions in ORF I.
259                                           No amino acid replacement substitutions were indicated in a
260 equence variation includes a minimum of five amino acid replacement substitutions; (4) segregation of
261 dition, the ratio of silent substitutions to amino acid replacements suggests that a short segment in
262 ed through a single hydrophobic-to-ionizable amino acid replacement that generates a partially buried
263 larly strong association with the process of amino acid replacement that it experiences.
264 sequenced the rhodopsin gene to identify the amino acid replacements that affect shifts in maximum wa
265  of beneficial mutations is 47.7%, and among amino acid replacements that become fixed the average pr
266 97A (threonine to alanine) but also by other amino acid replacements that cause minor lambda(max)-shi
267 ptor functionality was rescued by additional amino acid replacements that differed among poison frog
268 uences of equine and canine viruses revealed amino acid replacements that distinguished the viruses f
269                                              Amino acid replacements that enable activation without e
270 ased, particularly among those that generate amino acid replacements that enhance affinity of the B c
271 olerance of the KDO8PP catalytic platform to amino acid replacements that in turn influence substrate
272 tion was suggested by finding some recurrent amino acid replacements that may contribute increased af
273                                  Most of the amino acid replacements that occurred in the Nasonia lin
274                  The trace also hypothesizes amino acid replacements that preceded the first recorded
275 ion of amino acid composition occurs through amino acid replacements that result in a balanced loss a
276 es that evolved under positive selection and amino acid replacements that result in radical physicoch
277                        A series of quadruple amino acid replacements that spanned the helix propensit
278                                 Eight of the amino-acid replacements that occurred on the lineage lea
279 t accessibility and secondary structure with amino acid replacement, the process of protein evolution
280                                       Single amino acid replacements throughout the targeted region c
281 h showed that in Daphnia pulex, the ratio of amino acid replacement to silent substitution in mitocho
282  might allow more neutral and nearly neutral amino acid replacements to be fixed.
283 possibility is that there is no tendency for amino acid replacements to be spatially clustered during
284 he crystal structure and kinetic analyses of amino acid replacement variants.
285  unusual haplotype structure associated with amino acid replacement variation in exon 3 that is consi
286                 Alanine scanning followed by amino acid replacements was used to construct mutants of
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.

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