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1 t space for the imidazole ring of the mutant phenylalanine residue.
2 rved, nonglycine residues, a glutamate and a phenylalanine residue.
3 ing M2 domain of beta4 that includes the 13' phenylalanine residue.
4 ant FKBP with a compensating truncation of a phenylalanine residue.
5 in these peptides with a nonphosphorylatable phenylalanine residue.
6 edge-to-face" orientation with a neighboring phenylalanine residue.
7 first selective chemical modification of the phenylalanine residue.
8 pore that is gated by an extremely conserved phenylalanine residue.
9 on-pi solvation by tryptophan, tyrosine, and phenylalanine residues.
10 ormation, particularly in peptides that lack phenylalanine residues.
11 gh the intercalation of two sets of adjacent phenylalanine residues.
12 analog that stably modifies tyrosine but not phenylalanine residues.
13 when hydroxyl radical oxidizes protein-bound phenylalanine residues.
14  three critical and evolutionarily invariant phenylalanine residues.
15 le Arg-Gly-(Gly) sequences interspersed with phenylalanine residues.
16 for lysine, arginine, leucine, tyrosine, and phenylalanine residues.
17  to a central serine or threonine flanked by phenylalanine residues.
18  T189 in the ion selectivity filter, and all phenylalanine residues.
19  of mutating two conserved F(-)-coordinating phenylalanine residues.
20 n comparison to a control complex containing phenylalanine residues.
21  L150; and almost undetectable with L179 and phenylalanine residues.
22 t the C-terminus promoted by the presence of phenylalanine residues.
23 ion modules that have two flanking conserved phenylalanine residues.
24 Our results indicate that the elimination of phenylalanine residue 211 or 213 abolishes the UQ-depend
25 core domain demonstrated that replacement of phenylalanine residues 413, 425, and 429 with alanine re
26                  At the active site of CheA, phenylalanine residues 455 and 459 occupy positions near
27                                  Deletion of phenylalanine residue 508 (DeltaF508) in the cystic fibr
28 0% of CF chromosomes carry a deletion of the phenylalanine residue 508 (deltaF508) of CFTR, roughly 5
29 ies of injected tRNA charged with the native phenylalanine residue, a fluorescent NBD-alanine, or nit
30 , but mutating two tyrosine residues and one phenylalanine residue abolished the inhibitory action.
31                Its core contains a conserved phenylalanine residue adjoining three architectural elem
32 mechanisms of nonradiative deactivation of a phenylalanine residue after near-UV photoexcitation have
33 xyl terminus of CFTR; however, mutation to a phenylalanine residue (an amino acid found at position 1
34 amily Enterobacteriaceae, such as a terminal phenylalanine residue and a region in the amino portion
35 68 and Phe93 are broader than those of other phenylalanine residues and can be deconvoluted into two
36 etween the high beta-sheet propensity of the phenylalanine residues and charge-charge interactions th
37 ophobic and rich in alanine, glycine, and/or phenylalanine residues and contain a canonical fusion tr
38  of an extended cleft lined with hydrophobic phenylalanine residues and flanked by basic amino acids.
39 ils postulate that Tyr-37 is near one of the phenylalanine residues, and it is known that Tyr-37 inte
40  from an ammonium salt incorporating d- or l-phenylalanine residues as chiral stereogenic covalent un
41 ydrophobic groups other than the traditional phenylalanine residues as important for efficacy and aff
42 (iii) substitution of the nonpolar alpha-381-phenylalanine residue, as well as substitution of either
43 t inhibitors with side-chains smaller than a phenylalanine residue at P3 and P3', preferably medium-s
44 tant juxtaposition of an upwardly projecting phenylalanine residue at peptide position 6 that likely
45                             We show that the phenylalanine residue at position 126 of mouse MD-2 is i
46 for the D2-ATRP form, which bears a single d-phenylalanine residue at position 2.
47                                            A phenylalanine residue at position 37 intercalates into a
48 ce, resulting in a change from a serine to a phenylalanine residue at position 37.
49 avocytochrome P450 BM3, there is a conserved phenylalanine residue at position 393 (Phe393), close to
50                                          The phenylalanine residue at position 48 is likely to be of
51 e most common mutation, DeltaF508, omits the phenylalanine residue at position 508 in the first nucle
52 l-CFTR (where F508del is the deletion of the phenylalanine residue at position 508) at the plasma mem
53 we demonstrate that substitution of a single phenylalanine residue at position 983 (F983) with alanin
54 cture reveals an extended CDR H3 loop with a phenylalanine residue at the apex and shows a striking p
55  However, nonconservative substitutions to a phenylalanine residue at the apex of the H3 loop also ma
56                                    Second, a phenylalanine residue at the center of the ATP pocket st
57 truct a 21-mer polypeptide with an unnatural phenylalanine residue at the center.
58 PfEMP1 protein family to bind to a conserved phenylalanine residue at the membrane distal tip of CD36
59 37 suggests a function of the camel-specific phenylalanine residue at this position in the hydrophobi
60                                   Although a phenylalanine residue at this position within M2 is cons
61 ophilic groups, aromatic amino acids, or a D-phenylalanine residue at this position.
62                                Deletion of a phenylalanine residue at Yor1p position 670 led to a mut
63 en heptad "Phe-zipper" protein (Phe-14) with phenylalanine residues at all 14 hydrophobic a and d pos
64         Of particular interest are invariant phenylalanine residues at consecutive positions in the B
65     Additional mutagenesis revealed that two phenylalanine residues at positions 334 and 335 mediated
66 91 while manganese peroxidase (MnP) contains phenylalanine residues at the corresponding positions.
67                  In this work, six conserved phenylalanine residues at this proposed active site were
68 ned by replacing the appropriate tyrosine or phenylalanine residue by leucine in the wild-type crysta
69 ntaining the singly charged p-(carboxymethyl)phenylalanine residue (cmF) as a phosphotyrosine (Tyr(P)
70              We find that the removal of any phenylalanine residue completely abrogates assembly abil
71 re in the N-terminal helix (helix 1) and the phenylalanine residues constituting the hydrophobic core
72 N and 19S activators, a penultimate tyrosine/phenylalanine residue contacts the proteasome Gly-19 car
73                Specific, overlapping sets of phenylalanine residues contribute selectively to DAT rec
74 alis (gTBP) is highly divergent, lacking key phenylalanine residues crucial for binding and unwinding
75 th specific tryptophan residues converted to phenylalanine residues demonstrates that the main intera
76  it is demonstrated that mutation of the H11 phenylalanine residues diminishes the ability of RXR to
77 en, implicate a cluster of three active site phenylalanine residues (F100, F114, F476) in ligand bind
78 rating a series of chimeras, we identified a phenylalanine residue, F137, in the pore region of GIRK1
79                            Substitution of a phenylalanine residue (F328) by alanine reduced binding
80                                The conserved phenylalanine residue F329 closing the transport pore of
81 ed mutants of the phylogenetically conserved phenylalanine residue F393 were constructed in flavocyto
82 rt of an unusual set of three closely packed phenylalanine residues, F47, F51, and F58 (denoted using
83 residues (E678 and E686) in this motif and a phenylalanine residue (F680) that resides between the tw
84 ectively, confirmed the accessibility of the phenylalanine residue for antibody recognition.
85                  Further, substituting these phenylalanine residues for either isoleucine or tyrosine
86                                        Three phenylalanine residues form the walls of the guanine-bin
87 d more extensive pai-CH interactions between phenylalanine residues forming the roof of the active-si
88                                          Two phenylalanine residues found exclusively in isoprene syn
89 critically contains two of three consecutive phenylalanine residues found in helix 11 (H11) of the re
90 n showed that substitution of valine for the phenylalanine residue four residues downstream of the ph
91                            PapD contains six phenylalanine residues, four in the N-terminal domain an
92                                At each site, phenylalanine residues from Nup1p are buried in hydropho
93 region of Sis1, composed of a region rich in phenylalanine residues (G/F) and another rich in methion
94                              Specifically, a phenylalanine residue (GcoA-F169) interferes with the bi
95 ular protein, HPr, in which each of the four phenylalanine residues has in turn been replaced by a tr
96 ion loop tyrosine residues Tyr(1007/1008) to phenylalanine residues impaired, but did not abolish, th
97  Most striking were mutations that altered a phenylalanine residue in block 4 of the domain severely
98    Comparison of mutations of the homologous phenylalanine residue in brain and heart channels showed
99 retin receptor through a photolabile benzoyl-phenylalanine residue in position 13.
100            By replacing the highly conserved phenylalanine residue in the active site of KDM4 members
101        Substitutions at the lysine or either phenylalanine residue in the central KYNFSF sequence had
102 iogenesis of ABC transporters; deletion of a phenylalanine residue in the first nucleotide-binding do
103 ed that 2,6-DTBP interacted with a conserved phenylalanine residue in the membrane-associated stretch
104 gues incorporating a photolabile p-benzoyl-l-phenylalanine residue in the mid-region and carboxyl-ter
105                     Mutation of Tyr-255 to a phenylalanine residue in the Na,K-ATPase alpha1-subunit
106                                Mutation of a phenylalanine residue in the VCP C-terminal tail that ca
107                                Deletion of a phenylalanine residue in Yor1p, equivalent to the major
108 nes are positively charged and interact with phenylalanine residues in a hydrophobic cleft between ad
109 ortant controversy regarding the role of two phenylalanine residues in Ago2 activity.
110 vates 15-fold cleavage after leucine but not phenylalanine residues in model synthetic substrates.
111                            Specifically, two phenylalanine residues in RD3 make crucial contacts with
112                              Moreover, three phenylalanine residues in the AAA+ domain induce a steri
113 corresponding residues in the beta(2) to the phenylalanine residues in the alpha(1a).
114 udy, we determined that two highly conserved phenylalanine residues in the alphavirus E1 glycoprotein
115 cy of sites I and II in the N-domain because phenylalanine residues in the C-domain are nonemissive.
116 catalyzes ortho-hydroxylation of each of the phenylalanine residues in the conserved FRF motif, the a
117 /trans-isomerase B following mutation of two phenylalanine residues in the core of the protein to SF(
118                              Substitution of phenylalanine residues in the CsgF N-terminus both reduc
119 ine and was further facilitated by a pair of phenylalanine residues in the cytoplasmic tail.
120                                  Mutation of phenylalanine residues in the cytosolic tail of Arn1p al
121  ligand amino group and the carbonyls of two phenylalanine residues in the ligand binding pocket.
122 WIP is dependent on the two highly conserved phenylalanine residues in the motif.
123                In addition, mutating the two phenylalanine residues in the PIP-box to alanine or aspa
124 rane-facing leucine, isoleucine, valine, and phenylalanine residues in the transmembrane alpha-helice
125 of Mxr1 to residues 246-280, and showed that phenylalanine residues in this region are critical for i
126      We now report the identification of two phenylalanine residues in transmembrane domain 7 of the
127  (e.g. serine, alanine) or hydrophobic (e.g. phenylalanine) residues in the P1 and P1' sites, and pro
128 genesis to engineer rhodopsin with p-azido-l-phenylalanine residues incorporated at selected sites, a
129 no acid substitution at serine, tyrosine, or phenylalanine residues inhibited hemagglutination of ame
130 ture revealed by the structure is the single phenylalanine residue insertion on the tip of the flap,
131                                We introduced phenylalanine residues into nonconserved positions of ea
132                                         This phenylalanine residue is conserved in all but one subfam
133                           Unfortunately this phenylalanine residue is not conserved in the ARF family
134 lectrocatalyst containing either tyrosine or phenylalanine residues is reported.
135                             Mutations of two phenylalanine residues known to be critical for autoinhi
136 ls are mushroom shaped, with a ring of seven phenylalanine residues (known as the phenylalanine clamp
137 icted pi-pi stacking interaction between two phenylalanine residues leading to a destabilized uS12 th
138                                            A phenylalanine residue located at the heart of the ubiqui
139  required for the last step of this cycle, a phenylalanine residue located four amino acids from the
140 dy characterized that a missense mutation on phenylalanine residue located in CRD2 (TNFR1(F60V) ) cau
141                                          Two phenylalanine residues located adjacent to the substitut
142 is of interleukin-1beta indicates that three phenylalanine residues located at positions 42, 101, and
143 domain," critically contains two consecutive phenylalanine residues located at the C-terminal region
144 utL binding site is composed of two adjacent phenylalanine residues located laterally in an exposed l
145 hat 'aromatic clamps' formed by tyrosine and phenylalanine residues located within the substrate bind
146 ences of alanine substitution for each of 29 phenylalanine residues lying in or near a putative DAT T
147                         We hypothesized that phenylalanine residues lying in putative DAT transmembra
148 e, aspartic acid, beta-alanine, leucine, and phenylalanine residues, maximum activity was displayed b
149 esented here suggests that the carboxymethyl-phenylalanine residue may be a viable Tyr(P) replacement
150 hat contribute to acceptor RNA binding and a phenylalanine residue near the RT active site that media
151 creating a deep pocket that accommodates the phenylalanine residue of the trailing collagen chain ("P
152                                         This phenylalanine residue of TyrOH is found to be hydroxylat
153                               The C-terminal phenylalanine residues of PKCdelta (Phe(660), Phe(663),
154           Two sets of data indicate that the phenylalanine residues of the MARCKS-ED are positioned w
155 ratospongamides, which each consist of two L-phenylalanine residues, one (L-isoleucine)-L-methyloxazo
156  fraction of our simulations, the C-terminal phenylalanine residue packs improperly with the rest of
157 ith acidic lipids and that the 5 hydrophobic phenylalanine residues penetrate the polar head group re
158                            The importance of phenylalanine residues Phe-116, Phe-119, Phe-120, Phe-12
159 asticity, in a ligand-dependent manner, to a phenylalanine residue (Phe-126) at the cavity mouth prev
160  magnitude by mutation of a nearby conserved phenylalanine residue (Phe-283) to leucine.
161 s in Orai1 gating to a strategically exposed phenylalanine residue (Phe-394) in SOAR1, which in SOAR2
162  Overhauser effect, the distance between two phenylalanine residues (Phe(68) and Phe(93)) located in
163 ive-like collapse in regions involving three phenylalanine residues (Phe-62, Phe-68, and Phe-93) with
164 binding at beta(2)-adrenergic receptors, two phenylalanine residues, Phe-163 and Phe-187, of the alph
165 he ART motif, we have identified a conserved phenylalanine residue, Phe116, that is critical for the
166 selectivity filter (Lys1237) and an adjacent phenylalanine residue (Phe1236).
167                                 Of the eight phenylalanine residues, Phe2, Phe47, Phe62, Phe68, and P
168 e reductase by mutation of a surface-exposed phenylalanine residue (Phe306), located 12 A away from t
169 e function of the GABAA receptor, requires a phenylalanine residue (Phe77) in the gamma2 subunit.
170           Histidine, arginine, tyrosine, and phenylalanine residues preferentially take oxygen from H
171 equires the Q domain of Grg5 and a conserved phenylalanine residue present in an eh1-like motif locat
172                      In place of tyrosine or phenylalanine residues prototypically used for phase sep
173 thogenesis, the impact of the isoleucine and phenylalanine residues remains unknown.
174                                    A ring of phenylalanine residues repositions to expose previously
175 tif, amino acids 249-256, which contains two phenylalanine residues required for binding.
176 catalysis, were substituted with alanine and phenylalanine residues, respectively.
177  Structural modeling showed that up to three phenylalanine residues restrict the size of the active s
178 r-wise combination with the more hydrophobic phenylalanine residue(s).
179  suggest that double mutations eliminating 2 phenylalanine residues strongly destabilize the enzyme.
180 ion of multiple TM4, -5, and -6 tyrosine and phenylalanine residues suggests that aromatic-aromatic l
181                       Module-A contributes a phenylalanine residue that functions as an essential par
182 Furthermore, the B-subunit contains a unique phenylalanine residue that resides within the pore and d
183 ossesses the characteristic packing of three phenylalanine residues that constitute the main part of
184 gical measurements to identify two conserved phenylalanine residues that form an aromatic pathway who
185 nhibitor of the enzyme barnase, contains two phenylalanine residues, three tryptophan residues, and t
186 Conversely, mutation of a conserved I domain phenylalanine residue to a tryptophan (F205W) increased
187 d into the protein by mutation of a specific phenylalanine residue to a tyrosine.
188 ed were functionalized with a perfluorinated phenylalanine residue to promote anion-pi interactions w
189 lB and BcmB toward CMP, and mutation of this phenylalanine residue to tyrosine results in a 1000-fold
190  the ER due to mutation of two COOH-terminal phenylalanine residues to alanines.
191 ally cleaves translocated polypeptides after phenylalanine residues to generate peptides that range f
192 he highly reactive hydroxyl radical oxidizes phenylalanine residues to o-tyrosine and m-tyrosine.
193                       We show that placing a phenylalanine residue two or three positions before a gl
194                                            A phenylalanine residue was intercalated into the "weak" C
195 utagenesis of individual tyrosines in LAT to phenylalanine residues, we demonstrate that Y(171) and p
196 pact CoV replication, the isoleucine and the phenylalanine residues were mutated to alanine (I-A/F-A)
197            To address these questions native phenylalanine residues were replaced, at each face of th
198            Within the IST1 MIM sequence, two phenylalanine residues were shown to be important in dis
199     Trp-72 could only tolerate mutation to a phenylalanine residue, which allowed only limited fusion
200 e tags were appended with a hydrophobic p-Cl-phenylalanine residue, which conferred enhanced retentio
201 FabH structure, this channel is blocked by a phenylalanine residue, which constrains specificity to a
202 on of oxoG by Fpg and its mutants with a key phenylalanine residue, which intercalates next to the da
203 utations involve the replacement of specific phenylalanine residues, which circumscribe the cavity, w
204 he ideal alpha-helical geometry due to three phenylalanine residues, which stack within each helix an
205 rediction that replacement of the C-terminal phenylalanine residue with alanine will increase the fol
206 luorescent probes were obtained by replacing phenylalanine residues with tryptophan at position 442 o
207                                              Phenylalanine residues within it may coordinate permeati
208        Collectively, these studies show that phenylalanine residues within the carboxyl terminus of U
209   In this study, we investigated the role of phenylalanine residues within the carboxyl terminus of U
210                                    Conserved phenylalanine residues within the DNA-binding domain wer
211                       In particular, the two phenylalanine residues within the FYXWF motif of S519C16
212    Importantly, this mechanism relies on two phenylalanine residues within the separase-interacting s

 
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