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1 Ile-Pro-Ile-Gln-Tyr, Tyr-Pro-Tyr-Tyr and Leu-Pro-Tyr-Pro
3 e arrestin pathway-selective agonist [Sar(1)-Ile(4)-Ile(8)]AngII (SII), is blocked by shRNA silencing
4 f TM3 to extracellular loop 2, ECL2 (Thr-141/Ile-142) and ECL2 (Asn-148/Asp-149, Leu-150/Thr-151, Arg
5 e N-Cap amphipathic helix identified Leu-15, Ile-18, and Ile-19 as residues critical for the stabiliz
6 mogens, pro-uPA (at consensus sites Lys(158)-Ile(159) and Lys(135)-Lys(136)) and plasminogen, yieldin
7 d 2 were well-tolerated, with Val(1)-Val(2), Ile(1)-Ala(2), and Leu(1)-Val(2) variants exhibiting Pro
11 Specifically, Candida intermedia gxs1 Phe(38)Ile(39)Met(40), Scheffersomyces stipitis rgt2 Phe(38) an
12 tin pathway-selective agonist [Sar(1)-Ile(4)-Ile(8)]AngII (SII), is blocked by shRNA silencing of bet
13 four amino acid positions, Val-750, Ile-552, Ile-839, and Trp-500, located within a previously propos
16 Mutating SM residues Phe-35/Ser-37/Leu-65/Ile-69 into alanine, based on the key residues in Deg1,
18 1 (Phe-40), helix 3 (Leu-63, Arg-68, Gln-69, Ile-72, Tyr-76), and C-terminal segment (Leu-81, Glu-84)
19 idues at gp120 positions 23, 45, 47, and 70 (Ile-Ala-Lys-Asn [I-A-K-N]) emerged as signatures of muco
20 revealed also a key role of residues Lys-74/Ile-76 at the N-terminal of FGF14 in the FGF14.Nav1.6 co
21 ncluding four amino acid positions, Val-750, Ile-552, Ile-839, and Trp-500, located within a previous
23 ned in this study harbored the single Thr-86-Ile mutation in GyrA, FQ(R) C. jejuni isolates had other
24 ds Gly and Glu, and the essential amino acid Ile were more abundant in the scalp hair of diabetic pat
25 nel-based homology models predict amino acid Ile-1575 in domain IV segment 6 to be in close proximity
26 es whereas those of hydrophobic amino acids (Ile, Phe) deviate positively from the isotropic trend li
27 protein (65-74) fragment (H-Val-Gln-Ala-Ala-Ile-Asp-Tyr-Ile-Asn-Gly-OH), following the solid-phase p
28 nt (with a C-terminal Gly, H-Asn-Phe-Gly-Ala-Ile-Leu-Gly-NH2) and acyl carrier protein (65-74) fragme
31 Ile and Thr residues, i.e. containing d-allo-Ile and d-allo-Thr along with d-amino acids and glycine.
35 esaturase homologs which contained either an Ile or a Gly at this location and showed that only the G
38 ipathic helix identified Leu-15, Ile-18, and Ile-19 as residues critical for the stabilization of ful
40 th the scaffold proteins beta-arrestin 2 and Ile Gln motif containing GTPase Activating Protein 1, a
41 g the idea, mutations in residues Ile-24 and Ile-25 of the MinD-interacting domain affect fibril form
46 ), Ala(16), Met(17), Gly(475), Val(477), and Ile(485) are more important for kinase domain closure an
48 gest that an interaction between Val(48) and Ile(328) stabilizes the closed channel and that this is
51 iously identified two residues (Gln(596) and Ile(597)) in the helical domain of the catalytic subunit
52 ral side chains, such as Phe-57, Tyr-60, and Ile-77, that change their orientations to accommodate th
53 Additional mutations in residues Ile-72 and Ile-74 suggest a role of the C-terminal domain of MinE i
54 obic patch of ubiquitin comprising Leu-8 and Ile-44 is important for E6AP-mediated ubiquitination, wh
55 idA proteins can preempt damage to BCAT3 and Ile biosynthesis by hydrolyzing the Ser-derived enamine/
56 ith the APC/C through their common C-box and Ile-Arg tail motifs, the mechanism underlying this diffe
58 ntally verified contact of Ser-281 (ECD) and Ile-486 (TMD) was subsequently utilized in docking homol
59 fied to homogeneity functional Asn, Glu, and Ile tRNAs from the native E. coli tRNA mixture, and by c
60 exception of isoacceptors for Asn, Glu, and Ile, the majority of 48 synthetic Escherichia coli tRNAs
61 vealed that BCAT6 transaminates Val, Leu and Ile as well as the corresponding 2-oxo acids but also tr
62 (MS) for de novo protein sequencing, Leu and Ile have been generally considered to be indistinguishab
64 cid sequences, including identity of Leu and Ile residues, can be accurately obtained solely by means
65 by supplementation of LNAAs, such as Leu and Ile, with a strong affinity for the LNAA transporter typ
66 tion patches of ubiquitin (Ile(44) patch and Ile(36) patch, respectively, including Leu(8), which is
68 eu, Tyr-Pro-Tyr-Tyr, Leu-Pro-Tyr-Pro-Tyr and Ile-Pro-Ile) and a casein (CasH), whey (WPH) and lactofe
71 f 7 and NOP ligands (e.g., H-Arg-Tyr-Tyr-Arg-Ile-Lys-NH2) led to binding affinities in the low nanomo
72 3a (H-Dmt-d-Arg-Aba-beta-Ala-Arg-Tyr-Tyr-Arg-Ile-Lys-NH2) to mice resulted in potent and long lasting
73 hat tryptophan-containing dipeptides such as Ile-Trp or Val-Trp, which were recently found in food pr
76 e hydrogen-bonded coassemblies formed by BTA Ile and the intrinsically achiral catalytic rhodium cata
77 BTA(PPh2) and the enantiopure comonomer BTA Ile as confirmed by various spectroscopic and scattering
82 e quantum coherence (HMQC) spectrum of (13)C-Ile-labeled enzyme resembles the glucose-bound state.
84 inge enables conserved nonpolar side chains (Ile(A2), Val(A3), Val(B12), Phe(B24), and Phe(B25)) to e
85 variant positions, and a triplet ATT codon (Ile) insertion within ATP synthase subunit 8, were uniqu
86 ctures of dimers of unliganded CodY and CodY-Ile derived from the tetramers showed a splaying of the
88 Our analysis highlighted highly conserved Ile and Phe residues at the RfaH interdomain interface.
90 siological conditions and that the conserved Ile-Met motif is mainly used to recover mistargeted rece
92 he pentapeptides Cys-Ile-His-Asn-Pro and Cys-Ile-Gln-Pro-Val while low response was achieved for the
93 peptides (cysteinylglycine, glutathione, Cys-Ile-His-Asn-Pro, Cys-Ile-Gln-Pro-Val, Cys-Arg-Gln-Val-Ph
94 ponse was obtained for the pentapeptides Cys-Ile-His-Asn-Pro and Cys-Ile-Gln-Pro-Val while low respon
95 ycine, glutathione, Cys-Ile-His-Asn-Pro, Cys-Ile-Gln-Pro-Val, Cys-Arg-Gln-Val-Phe) vs. 14 volatile co
96 n target of rapamycin signaling and decrease Ile Gln motif containing GTPase Activating Protein 1 pho
97 s ProT by inserting its N-terminal dipeptide Ile(1)-Val(2) into the ProT Ile(16) pocket, forming a sa
98 ids possessing two chiral centers such as dl-Ile or dl-Thr, only the epimerization of isomers with di
99 s show that Met(73) and, to a lesser extent, Ile(75) suppress excision activity when TAMs are present
100 By comparison, substitutions of Asn for Ile-136 (I136N) and Thr for Ile-142 (I142T) in a subdoma
104 tions of Asn for Ile-136 (I136N) and Thr for Ile-142 (I142T) in a subdomain previously named the heli
105 her generation of a signature 69 Da ion from Ile or formation of unique w-ions employing MS(3) (ETD-H
107 peptides of the sequence EGAAXAASS (X = Gly, Ile, Tyr, Trp) through comparison of molecular dynamics
108 acetyltransferase uses a similar Gly-Asp-Gly-Ile motif to form the "cysteine synthase" complex with C
109 ositive bacteria lack C-terminal Gly-Tyr-Gly-Ile motifs, suggesting that they do not interact with Cy
110 CT(EC536) inserts its C-terminal Gly-Tyr-Gly-Ile peptide tail into the active-site cleft of CysK to a
111 h asthma at 18 years for children with GSTP1 Ile/Ile (odds ratio, 1.66; 95% CI, 1.07 to 2.57), but no
112 ing to AA was: Trp > norleucine > Phe, Leu > Ile > His >3,4-dihydroxyphenylalanine, Arg > Val > Lys,
114 ate, thereby establishing the alpha-70(Val-->Ile) intermediate as a reliable guide to mechanism.
115 e-trapped intermediate of the alpha-70(Val-->Ile) MoFe protein as the Janus intermediate that stores
117 s containing amino acids Ala, Asn, Gln, His, Ile, and Lys at positions equivalent to 782 and/or 786 i
118 Leu-Leu-Ala-Pro and Met-Ala-Gly-Val-Asp-His-Ile, with IC50 values in the range 43-159 muM were ident
119 UT1), reveal that Ile-335 (or the homologous Ile-296 in hSLC2A5) is a key component for protein confo
120 similarly to the wild type hSLC2A9; however, Ile-335 is necessary for urate/fructose trans-accelerati
126 28~Gln653, named CP), but with an innovative Ile-Asp-Leu tail (IDL) that dramatically increased the i
127 affolding protein, KIBRA, has an isoleucine (Ile-81) rather than a second conserved tryptophan and is
129 ain amino acids (BCAAs) leucine, isoleucine (Ile), and valine (Val) in the mitochondria efficiently a
131 Asp, as well as racemization of isoleucine (Ile) and phenylalanine (Phe) after 100 s of irradiation
132 f growth regulators includes the isoleucine (Ile) conjugate of jasmonic acid (JA-Ile) and its biosynt
135 coronatine (COR), we demonstrate that (1) JA-Ile/COR-based signaling regulates corolla limb opening a
136 leucine (Ile) conjugate of jasmonic acid (JA-Ile) and its biosynthetic precursor 12-oxophytodienoic a
138 ed accumulation of jasmonic acid (JA) and JA-Ile, elevated expression of over 2,200 different transcr
140 ugh COI1; and (3) limb expansion involves JA-Ile-induced changes in limb fresh mass and carbohydrate
141 t recognizes both jasmonoyl-l-isoleucine (JA-Ile) and the bacterial-produced phytotoxin coronatine (C
142 nd that the COR and jasmonate isoleucine (JA-Ile) co-receptor JAZ2 is constitutively expressed in gua
145 The binding of jasmonoyl-L-isoleucine (JA-Ile) to the F-box of CORONATINE INSENSITIVE1 (COI1) is r
149 To assess the relative contribution of JA/JA-Ile and OPDA to insect resistance in tomato (Solanum lyc
151 we found that OPDA can substitute for JA/JA-Ile in the local induction of defense gene expression, b
154 g the signaling activities of OPDA and JA/JA-Ile, we found that OPDA can substitute for JA/JA-Ile in
155 were complemented with methyl jasmonate, JA-Ile, and its functional homolog, coronatine (COR), we de
159 Flower opening, by contrast, requires JA-Ile signaling-dependent changes in primary metabolism, w
160 ons of benzylacetone) and nectar requires JA-Ile/COR perception through COI1; and (3) limb expansion
161 trate a master regulatory function of the JA-Ile/COI1 duet for the main function of a sympetalous cor
162 es showed that jasmonic acid (JA), jasmonoyl-Ile, salicylic acid, abscisic acid, and indole-3-acetic
163 Mozamide A contains l-Val, d-Lys, and l-Ile (instead of d-Val, l-Lys, and l-allo-Ile) and is a h
164 iron and 2-oxoglutarate dependent enzymes, l-Ile 4-hydroxylase, l-Leu 5-hydroxylase and polyoxin dihy
165 hods of Marfey and Mosher indicated l-Glu, l-Ile, l-Phe and 1S-configurations, respectively; ROESY co
167 e conjugating jasmonic acid (JA) to at least Ile, Leu, Met, Phe, Trp and Val and both osjar1 alleles
168 Branched-chained amino acids (BCAAs) (Leu, Ile, and Val) and their catabolites, propionylcarnitine
169 The branched-chain amino acids (BCAAs) Leu, Ile, and Val are among nine essential amino acids that m
170 of Spo7, we identified a hydrophobic Leu-Leu-Ile (LLI) sequence comprising residues 54-56 as being re
175 elines we unambiguously identified every Leu/Ile residue in peptides containing up to five Leu/Ile re
176 nstrated, for the first time, that every Leu/Ile residue in the variable regions of a monoclonal anti
178 is integrated, online LC-MS approach for Leu/Ile assignment can be applied to de novo sequencing of a
183 55 where Lys23 to Phe39 encompassing the Leu/Ile/Phe-rich domain forms an amphipathic alpha-helix.
187 5)N-labeled Ras as well as [(13)C]methyl-Met,Ile-labeled Sos for observing site-specific details of R
191 3), as well as the hydrocarbon side chain of Ile(310) Our results suggest that placing methionine pro
192 de, whereas the strong positive deviation of Ile leads to prediction or fibril formation for the NINI
194 e same extent as ZnTerp upon Ala mutation of Ile-116(III:16/3.40), a residue that constrains the Trp-
195 revertants of K377C reveals that mutation of Ile-22 (in helix I) preserves Na(+) binding, whereas tha
196 for external QX-222 created by mutations of Ile-1575 was abolished by the additional mutation K1237E
198 mprehensive (13)C-methyl relaxation study of Ile, Leu, and Val (ILV) residues of PTP1B, which, becaus
199 from the 4-fold channel axis and twisting of Ile-4937 at the channel constriction site out of the cha
202 n this model, OMR1 exerts primary control on Ile accumulation and functions independently of AHAS and
204 ta-ketosulfonamides derived from Val, Leu or Ile gave the expected beta-keto-alpha,alpha-difluorosulf
205 obic character; (3) ISDs tend to have Leu or Ile residues at their core; (4) ISDs are approximately e
206 X is any amino acid and Phi is Val, Leu, or Ile) endocytic motif that, when transferred to CD4, resu
209 For steric reasons, epoxyketones with Val or Ile at the P1 position are weak inhibitors of all active
212 Five casein-derived synthetic peptides (Ile-Pro-Ile-Gln-Tyr, Leu-Pro-Leu-Pro-Leu, Tyr-Pro-Tyr-Ty
213 interaction between milk bioactive peptides, Ile-Asn-Tyr-Trp, Leu-Asp-Gln-Trp, and Leu-Gln-Lys-Trp, a
214 Three novel DPP-IV inhibitory peptides, Ile-Leu-Ala-Pro, Leu-Leu-Ala-Pro and Met-Ala-Gly-Val-Asp
215 of TCam-2 cells with the peptide Leu-Asp-Phe-Ile (LDFI), a full leptin-receptor antagonist, completel
216 residues with Ile, one by one, and prepared Ile-1-(13)C amyloid of each mutant, seeding with amyloid
217 variation surrounding the C-terminal Glu-Pro-Ile-Tyr-Ala (EPIYA) motifs as well as the number of EPIY
218 Pro-Tyr-Tyr, Leu-Pro-Tyr-Pro-Tyr and Ile-Pro-Ile) and a casein (CasH), whey (WPH) and lactoferrin hyd
219 e casein-derived synthetic peptides (Ile-Pro-Ile-Gln-Tyr, Leu-Pro-Leu-Pro-Leu, Tyr-Pro-Tyr-Tyr, Leu-P
221 rminal dipeptide Ile(1)-Val(2) into the ProT Ile(16) pocket, forming a salt bridge with ProT's Asp(19
223 ed non-Hispanic white patients with the rare Ile 164 allele compared with non-Hispanic white patients
224 rimary and replication cohorts with the rare Ile 164 allele were more than twice as likely as Thr 164
225 anic white patients with or without the rare Ile 164 allele, 2.6 [SD 3.5] vs 1.1 [2.1] visits, p<0.00
226 Glutamate substitution of the A55 residue Ile-48, adjacent to the canonical phiX(D/E) Cul3-binding
227 e binding, although the MinD-binding residue Ile-25 is critical for this conformational transition.
229 xpected that the substitution of the residue Ile(105) for a serine, located within hydrogen-bonding d
233 g hydrophobic contacts between FtsZ residues Ile-374, Pro-375, and Leu-378 with ZapD residues Leu-74,
234 Supporting the idea, mutations in residues Ile-24 and Ile-25 of the MinD-interacting domain affect
236 and binding studies indicated that residues Ile-701, Phe-705, and Trp-708 of the MyoB IQ motif are c
237 nce of three relay loop amino acid residues (Ile(508), Asn(509), and Asp(511)) in communicating with
238 2 peptides which possess two extra residues (Ile 41 &Ala 42) that the non-pathological strain (Abeta4
239 onal roles of two form II-specific residues (Ile(165) and Met(331)) near the active site were examine
242 Both peptides contain a putative 'SIP' (Ser-Ile-Pro) domain that is important for interactions with
245 g involves the hydrophobic patch surrounding Ile-44 in the parkin Ubl, a region that is highly conser
248 A positions are, in general, more rigid than Ile, Leu, and Val methyl probes in protein side chains.
249 C-terminal domain of primase, we found that Ile-85 is located at the interface in the NTD of DnaB th
250 al structure of hSLC2A1 (GLUT1), reveal that Ile-335 (or the homologous Ile-296 in hSLC2A5) is a key
251 tutions at positions 80 and 83 revealed that Ile(80) and Arg(83) within the Bw4 motif constrain the c
253 However, mutagenesis studies suggest that Ile-A10, Ser-A12, Leu-A13, and Glu-A17 also belong to in
256 ), and the association was reinforced in the Ile-de-France region when this indicator was combined wi
257 onserved hydrophobic residues, including the Ile at position 181 which was highly correlated with vac
258 eochemistry of the chiral side chains of the Ile and Thr residues, i.e. containing d-allo-Ile and d-a
260 ion measurements of the methyl groups of the Ile, Leu, and Val residues at two static magnetic fields
262 olymorphism is functional in vitro, with the Ile allele leading to increased monoamine transport into
264 actions revealed that mutation of Val-434 to Ile significantly reduces inhibition by meloxicam due to
266 fect can almost exclusively be attributed to Ile-Trp, the ACE inhibition by plant protein hydrolysate
269 mutant of Bacillus subtilis that allows tRNA(Ile) mischarging while retaining wild-type Ile-tRNA(Ile)
271 ic binding to the cognate tRNA(Ile) and tRNA(Ile)-dependent structural rearrangements consistent with
272 r C(32) in the Saccharomyces cerevisiae tRNA(Ile)(IAU) anticodon stem and loop domain (ASL) negates w
273 strated specific binding to the cognate tRNA(Ile) and tRNA(Ile)-dependent structural rearrangements c
275 ed in which the essential gene encoding tRNA(Ile)-lysidine synthetase was deleted for the first time.
279 l-tRNA synthetases, IleRS can mischarge tRNA(Ile) and correct this misacylation through a separate po
280 A(Leu(UUR)) or with mutations in the mt-tRNA(Ile), both of which are aminoacylated by Class I mt-amin
286 ever, the molecular mechanisms by which tRNA(Ile) organizes the synthetic site to enhance pre-transfe
288 strain, C34 at the wobble position of tRNA2(Ile) is expected to remain unmodified and cells depend o
289 agmatidine) at the wobble position of tRNA2(Ile) to base pair specifically with the A of the AUA cod
291 -74) fragment (H-Val-Gln-Ala-Ala-Ile-Asp-Tyr-Ile-Asn-Gly-OH), following the solid-phase peptide synth
292 secondary recognition patches of ubiquitin (Ile(44) patch and Ile(36) patch, respectively, including
294 The most potent inhibitory peptides were Ile-Gln-Ala (beta-CN f187-189) and Val-Glu-Pro (beta-CN
295 s showed a splaying of the wHTH domains when Ile was bound; splaying is likely to account for the inc
298 eu and then replaced 16 single residues with Ile, one by one, and prepared Ile-1-(13)C amyloid of eac
299 sults suggest that SC variants other than WT Ile(1)-Val(2)-Thr(3) might emerge with similar ProT-acti
300 Ca(2+) -dependent complex with EB3 via Ser-x-Ile-Pro aminoacid motif and that disruption of STIM2-EB3