ライフサイエンスコーパス: phenylalanine residue

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 first selective chemical modification of the phenylalanine residue.

7 pore that is gated by an extremely conserved phenylalanine residue.

8 edge-to-face" orientation with a neighboring phenylalanine residue.

9 T189 in the ion selectivity filter, and all phenylalanine residues.

10 of mutating two conserved F(-)-coordinating phenylalanine residues.

11 gh the intercalation of two sets of adjacent phenylalanine residues.

12 n comparison to a control complex containing phenylalanine residues.

13 analog that stably modifies tyrosine but not phenylalanine residues.

14 when hydroxyl radical oxidizes protein-bound phenylalanine residues.

15 L150; and almost undetectable with L179 and phenylalanine residues.

16 le Arg-Gly-(Gly) sequences interspersed with phenylalanine residues.

17 three critical and evolutionarily invariant phenylalanine residues.

18 t the C-terminus promoted by the presence of phenylalanine residues.

19 for lysine, arginine, leucine, tyrosine, and phenylalanine residues.

20 ion modules that have two flanking conserved phenylalanine residues.

21 on-pi solvation by tryptophan, tyrosine, and phenylalanine residues.

22 ormation, particularly in peptides that lack phenylalanine residues.

23 Our results indicate that the elimination of phenylalanine residue 211 or 213 abolishes the UQ-depend

24 core domain demonstrated that replacement of phenylalanine residues 413, 425, and 429 with alanine re

25 At the active site of CheA, phenylalanine residues 455 and 459 occupy positions near

26 Deletion of phenylalanine residue 508 (DeltaF508) in the cystic fibr

27 0% of CF chromosomes carry a deletion of the phenylalanine residue 508 (deltaF508) of CFTR, roughly 5

28 ies of injected tRNA charged with the native phenylalanine residue, a fluorescent NBD-alanine, or nit

29 , but mutating two tyrosine residues and one phenylalanine residue abolished the inhibitory action.

30 Its core contains a conserved phenylalanine residue adjoining three architectural elem

31 mechanisms of nonradiative deactivation of a phenylalanine residue after near-UV photoexcitation have

32 xyl terminus of CFTR; however, mutation to a phenylalanine residue (an amino acid found at position 1

33 amily Enterobacteriaceae, such as a terminal phenylalanine residue and a region in the amino portion

34 68 and Phe93 are broader than those of other phenylalanine residues and can be deconvoluted into two

35 etween the high beta-sheet propensity of the phenylalanine residues and charge-charge interactions th

36 ophobic and rich in alanine, glycine, and/or phenylalanine residues and contain a canonical fusion tr

37 of an extended cleft lined with hydrophobic phenylalanine residues and flanked by basic amino acids.

38 ils postulate that Tyr-37 is near one of the phenylalanine residues, and it is known that Tyr-37 inte

39 ydrophobic groups other than the traditional phenylalanine residues as important for efficacy and aff

40 (iii) substitution of the nonpolar alpha-381-phenylalanine residue, as well as substitution of either

41 t inhibitors with side-chains smaller than a phenylalanine residue at P3 and P3', preferably medium-s

42 tant juxtaposition of an upwardly projecting phenylalanine residue at peptide position 6 that likely

43 We show that the phenylalanine residue at position 126 of mouse MD-2 is i

44 A phenylalanine residue at position 37 intercalates into a

45 ce, resulting in a change from a serine to a phenylalanine residue at position 37.

46 avocytochrome P450 BM3, there is a conserved phenylalanine residue at position 393 (Phe393), close to

47 The phenylalanine residue at position 48 is likely to be of

48 e most common mutation, DeltaF508, omits the phenylalanine residue at position 508 in the first nucle

49 we demonstrate that substitution of a single phenylalanine residue at position 983 (F983) with alanin

50 cture reveals an extended CDR H3 loop with a phenylalanine residue at the apex and shows a striking p

51 However, nonconservative substitutions to a phenylalanine residue at the apex of the H3 loop also ma

52 Second, a phenylalanine residue at the center of the ATP pocket st

53 PfEMP1 protein family to bind to a conserved phenylalanine residue at the membrane distal tip of CD36

54 37 suggests a function of the camel-specific phenylalanine residue at this position in the hydrophobi

55 Although a phenylalanine residue at this position within M2 is cons

56 ophilic groups, aromatic amino acids, or a D-phenylalanine residue at this position.

57 Deletion of a phenylalanine residue at Yor1p position 670 led to a mut

58 en heptad "Phe-zipper" protein (Phe-14) with phenylalanine residues at all 14 hydrophobic a and d pos

59 Of particular interest are invariant phenylalanine residues at consecutive positions in the B

60 Additional mutagenesis revealed that two phenylalanine residues at positions 334 and 335 mediated

61 91 while manganese peroxidase (MnP) contains phenylalanine residues at the corresponding positions.

62 In this work, six conserved phenylalanine residues at this proposed active site were

63 ned by replacing the appropriate tyrosine or phenylalanine residue by leucine in the wild-type crysta

64 ntaining the singly charged p-(carboxymethyl)phenylalanine residue (cmF) as a phosphotyrosine (Tyr(P)

65 We find that the removal of any phenylalanine residue completely abrogates assembly abil

66 re in the N-terminal helix (helix 1) and the phenylalanine residues constituting the hydrophobic core

67 N and 19S activators, a penultimate tyrosine/phenylalanine residue contacts the proteasome Gly-19 car

68 Specific, overlapping sets of phenylalanine residues contribute selectively to DAT rec

69 th specific tryptophan residues converted to phenylalanine residues demonstrates that the main intera

70 it is demonstrated that mutation of the H11 phenylalanine residues diminishes the ability of RXR to

71 en, implicate a cluster of three active site phenylalanine residues (F100, F114, F476) in ligand bind

72 rating a series of chimeras, we identified a phenylalanine residue, F137, in the pore region of GIRK1

73 Substitution of a phenylalanine residue (F328) by alanine reduced binding

74 ed mutants of the phylogenetically conserved phenylalanine residue F393 were constructed in flavocyto

75 rt of an unusual set of three closely packed phenylalanine residues, F47, F51, and F58 (denoted using

76 residues (E678 and E686) in this motif and a phenylalanine residue (F680) that resides between the tw

77 Further, substituting these phenylalanine residues for either isoleucine or tyrosine

78 Three phenylalanine residues form the walls of the guanine-bin

79 Two phenylalanine residues found exclusively in isoprene syn

80 critically contains two of three consecutive phenylalanine residues found in helix 11 (H11) of the re

81 n showed that substitution of valine for the phenylalanine residue four residues downstream of the ph

82 PapD contains six phenylalanine residues, four in the N-terminal domain an

83 At each site, phenylalanine residues from Nup1p are buried in hydropho

84 region of Sis1, composed of a region rich in phenylalanine residues (G/F) and another rich in methion

85 ular protein, HPr, in which each of the four phenylalanine residues has in turn been replaced by a tr

86 ion loop tyrosine residues Tyr(1007/1008) to phenylalanine residues impaired, but did not abolish, th

87 Most striking were mutations that altered a phenylalanine residue in block 4 of the domain severely

88 Comparison of mutations of the homologous phenylalanine residue in brain and heart channels showed

89 retin receptor through a photolabile benzoyl-phenylalanine residue in position 13.

90 Substitutions at the lysine or either phenylalanine residue in the central KYNFSF sequence had

91 iogenesis of ABC transporters; deletion of a phenylalanine residue in the first nucleotide-binding do

92 ed that 2,6-DTBP interacted with a conserved phenylalanine residue in the membrane-associated stretch

93 gues incorporating a photolabile p-benzoyl-l-phenylalanine residue in the mid-region and carboxyl-ter

94 Mutation of Tyr-255 to a phenylalanine residue in the Na,K-ATPase alpha1-subunit

95 Deletion of a phenylalanine residue in Yor1p, equivalent to the major

96 ortant controversy regarding the role of two phenylalanine residues in Ago2 activity.

97 vates 15-fold cleavage after leucine but not phenylalanine residues in model synthetic substrates.

98 corresponding residues in the beta(2) to the phenylalanine residues in the alpha(1a).

99 cy of sites I and II in the N-domain because phenylalanine residues in the C-domain are nonemissive.

100 ine and was further facilitated by a pair of phenylalanine residues in the cytoplasmic tail.

101 Mutation of phenylalanine residues in the cytosolic tail of Arn1p al

102 ligand amino group and the carbonyls of two phenylalanine residues in the ligand binding pocket.

103 WIP is dependent on the two highly conserved phenylalanine residues in the motif.

104 In addition, mutating the two phenylalanine residues in the PIP-box to alanine or aspa

105 of Mxr1 to residues 246-280, and showed that phenylalanine residues in this region are critical for i

106 We now report the identification of two phenylalanine residues in transmembrane domain 7 of the

107 (e.g. serine, alanine) or hydrophobic (e.g. phenylalanine) residues in the P1 and P1' sites, and pro

108 genesis to engineer rhodopsin with p-azido-l-phenylalanine residues incorporated at selected sites, a

109 no acid substitution at serine, tyrosine, or phenylalanine residues inhibited hemagglutination of ame

110 ture revealed by the structure is the single phenylalanine residue insertion on the tip of the flap,

111 We introduced phenylalanine residues into nonconserved positions of ea

112 This phenylalanine residue is conserved in all but one subfam

113 Unfortunately this phenylalanine residue is not conserved in the ARF family

114 lectrocatalyst containing either tyrosine or phenylalanine residues is reported.

115 Mutations of two phenylalanine residues known to be critical for autoinhi

116 ls are mushroom shaped, with a ring of seven phenylalanine residues (known as the phenylalanine clamp

117 icted pi-pi stacking interaction between two phenylalanine residues leading to a destabilized uS12 th

118 A phenylalanine residue located at the heart of the ubiqui

119 required for the last step of this cycle, a phenylalanine residue located four amino acids from the

120 Two phenylalanine residues located adjacent to the substitut

121 is of interleukin-1beta indicates that three phenylalanine residues located at positions 42, 101, and

122 domain," critically contains two consecutive phenylalanine residues located at the C-terminal region

123 utL binding site is composed of two adjacent phenylalanine residues located laterally in an exposed l

124 hat 'aromatic clamps' formed by tyrosine and phenylalanine residues located within the substrate bind

125 ences of alanine substitution for each of 29 phenylalanine residues lying in or near a putative DAT T

126 We hypothesized that phenylalanine residues lying in putative DAT transmembra

127 e, aspartic acid, beta-alanine, leucine, and phenylalanine residues, maximum activity was displayed b

128 esented here suggests that the carboxymethyl-phenylalanine residue may be a viable Tyr(P) replacement

129 creating a deep pocket that accommodates the phenylalanine residue of the trailing collagen chain ("P

130 This phenylalanine residue of TyrOH is found to be hydroxylat

131 The C-terminal phenylalanine residues of PKCdelta (Phe(660), Phe(663),

132 Two sets of data indicate that the phenylalanine residues of the MARCKS-ED are positioned w

133 ratospongamides, which each consist of two L-phenylalanine residues, one (L-isoleucine)-L-methyloxazo

134 fraction of our simulations, the C-terminal phenylalanine residue packs improperly with the rest of

135 ith acidic lipids and that the 5 hydrophobic phenylalanine residues penetrate the polar head group re

136 The importance of phenylalanine residues Phe-116, Phe-119, Phe-120, Phe-12

137 asticity, in a ligand-dependent manner, to a phenylalanine residue (Phe-126) at the cavity mouth prev

138 magnitude by mutation of a nearby conserved phenylalanine residue (Phe-283) to leucine.

139 s in Orai1 gating to a strategically exposed phenylalanine residue (Phe-394) in SOAR1, which in SOAR2

140 Overhauser effect, the distance between two phenylalanine residues (Phe(68) and Phe(93)) located in

141 ive-like collapse in regions involving three phenylalanine residues (Phe-62, Phe-68, and Phe-93) with

142 binding at beta(2)-adrenergic receptors, two phenylalanine residues, Phe-163 and Phe-187, of the alph

143 selectivity filter (Lys1237) and an adjacent phenylalanine residue (Phe1236).

144 Of the eight phenylalanine residues, Phe2, Phe47, Phe62, Phe68, and P

145 e reductase by mutation of a surface-exposed phenylalanine residue (Phe306), located 12 A away from t

146 e function of the GABAA receptor, requires a phenylalanine residue (Phe77) in the gamma2 subunit.

147 equires the Q domain of Grg5 and a conserved phenylalanine residue present in an eh1-like motif locat

148 tif, amino acids 249-256, which contains two phenylalanine residues required for binding.

149 catalysis, were substituted with alanine and phenylalanine residues, respectively.

150 Structural modeling showed that up to three phenylalanine residues restrict the size of the active s

151 r-wise combination with the more hydrophobic phenylalanine residue(s).

152 suggest that double mutations eliminating 2 phenylalanine residues strongly destabilize the enzyme.

153 ion of multiple TM4, -5, and -6 tyrosine and phenylalanine residues suggests that aromatic-aromatic l

154 Module-A contributes a phenylalanine residue that functions as an essential par

155 ossesses the characteristic packing of three phenylalanine residues that constitute the main part of

156 nhibitor of the enzyme barnase, contains two phenylalanine residues, three tryptophan residues, and t

157 Conversely, mutation of a conserved I domain phenylalanine residue to a tryptophan (F205W) increased

158 d into the protein by mutation of a specific phenylalanine residue to a tyrosine.

159 ed were functionalized with a perfluorinated phenylalanine residue to promote anion-pi interactions w

160 lB and BcmB toward CMP, and mutation of this phenylalanine residue to tyrosine results in a 1000-fold

161 the ER due to mutation of two COOH-terminal phenylalanine residues to alanines.

162 he highly reactive hydroxyl radical oxidizes phenylalanine residues to o-tyrosine and m-tyrosine.

163 We show that placing a phenylalanine residue two or three positions before a gl

164 A phenylalanine residue was intercalated into the "weak" C

165 utagenesis of individual tyrosines in LAT to phenylalanine residues, we demonstrate that Y(171) and p

166 To address these questions native phenylalanine residues were replaced, at each face of th

167 Within the IST1 MIM sequence, two phenylalanine residues were shown to be important in dis

168 Trp-72 could only tolerate mutation to a phenylalanine residue, which allowed only limited fusion

169 e tags were appended with a hydrophobic p-Cl-phenylalanine residue, which conferred enhanced retentio

170 FabH structure, this channel is blocked by a phenylalanine residue, which constrains specificity to a

171 on of oxoG by Fpg and its mutants with a key phenylalanine residue, which intercalates next to the da

172 utations involve the replacement of specific phenylalanine residues, which circumscribe the cavity, w

173 rediction that replacement of the C-terminal phenylalanine residue with alanine will increase the fol

174 luorescent probes were obtained by replacing phenylalanine residues with tryptophan at position 442 o

175 Phenylalanine residues within it may coordinate permeati

176 Collectively, these studies show that phenylalanine residues within the carboxyl terminus of U

177 In this study, we investigated the role of phenylalanine residues within the carboxyl terminus of U

178 Conserved phenylalanine residues within the DNA-binding domain wer

179 In particular, the two phenylalanine residues within the FYXWF motif of S519C16