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1 evis oocytes conferred a 48-fold increase in alanyl-[14C]phenylalanine uptake relative to water injec
2 (beta-alanyl-l-histidine) and anserine (beta-alanyl-3-methyl-l-histidine) are abundant peptides in th
3 idehydro-N-methylalanyl-L-alanyl-N-methyl-L-alanyl-(3R)-3-[[(2S,3R)-3-hydroxy-4- methyl-1-oxo-2-[(1-
8 hed peptides that most frequently carried an alanyl-alanine substituent on the epsilon amino group of
9 vity and can cleave the substrate N-succinyl-alanyl-alanyl-prolyl-phenylalanine-p-nitroanilide (SAAPF
11 l morphology and putative N-acetylmuramoyl-L-alanyl amidase AmiA were both involved in the coccoid tr
12 sequence homology to known N-acetylmuramyl-L-alanyl amidases; however, their precise cleavage sites o
13 A series of water-soluble L-lysyl- and L-alanyl-amide prodrugs of the lipophilic antitumor 2-(4-a
14 proposed DPO precursor, a linear molecule, N-alanyl-aminoacetone (Ala-AA), also bound and activated V
15 d evaluated for their ability to detect beta-alanyl aminopeptidase activity in bacteria known to hydr
16 gh overall yield and were selective for beta-alanyl aminopeptidase activity in bacteria, producing a
19 Here, enzymatic digestion using microsomal alanyl aminopeptidase is combined with MS characterizati
23 t such hydrogen bonding may explain both the alanyl and amide I/III markers of PH75 capsid subunits a
24 pts of four specificities (valyl, methionyl, alanyl, and phenylalanyl) from higher plants or Escheric
26 es to histidyl-tRNA synthetase (HisRS) or to alanyl-, asparaginyl-, glycyl-, isoleucyl-, or threonyl-
27 cause benzyloxycarbonyl-valyl-aspartyl-valyl-alanyl-aspartic acid fluoromethyl ketone (Z-VDVAD-FMK) t
28 RGD in the pro-toxin was changed to arginyl-alanyl-aspartic or to arginyl-glycyl-glutamic, were expr
29 otent antiapoptotic agent carbobenzoxy-valyl-alanyl-aspartyl(beta-methyl ester)-fluoromethyl ketone (
30 the pancaspase inhibitor carbobenzoxyl-valyl-alanyl-aspartyl-[O-methyl]-fluoromethylketone before the
31 to other cell wall subunits, in which the D-alanyl at position four was amide linked to the pentagly
34 city in glial expression of ebony, an N-beta-alanyl-biogenic amine synthase, and show that Ebony acti
35 circadian rhythm in Drosophila Ebony (N-beta-alanyl-biogenic amine synthetase) abundance can be visua
36 odification of the beta-position of the beta-alanyl carboxylate group of 29 had only a modest effect
37 dification at the alpha-position of the beta-alanyl carboxylate group resulted in the identification
41 -positive organisms requires the D-alanine-D-alanyl carrier protein ligase (AMP) (Dcl) and the D-alan
42 D-alanine into LTA requires the D-alanine:D-alanyl carrier protein ligase (AMP-forming) (Dcl) and th
44 cillus casei requires the 56-kDa D-alanine-D-alanyl carrier protein ligase (Dcl) and the 8.9-kDa D-al
45 cement of the dltA gene encoding d-alanine-d-alanyl carrier protein ligase in an invasive serotype M1
47 incorporated into acyl carrier protein and D-alanyl carrier protein, the prosthetic groups of which a
48 s 7 with N-trifluoroacetyl-protected D- or L-alanyl chloride, followed by ketone reduction and N-depr
49 l-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alan ine as substrate, mutation of Asp155, Phe1
52 tion of peptidoglycan precursors ending in D-alanyl-D-alanine (D-Ala-D-Ala) in glycopeptide-resistant
53 to encode amino acid racemases however, a D-alanyl-D-alanine (D-Ala-D-Ala) ligase homologue (Ddl) is
54 bacterial cell wall through binding to the D-alanyl-D-alanine (D-Ala-D-Ala) terminal peptide of the p
55 ctam antibiotics, are believed to catalyze d-alanyl-d-alanine carboxypeptidase and transpeptidase rea
57 ctive site of the bifunctional serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase (EC ) f
58 exchange was detected over temperature for D-alanyl-D-alanine carboxypeptidases (dac1 and dac2), DEAD
59 The crystal structures of VanX, the VanX:D-alanyl-D-alanine complex, the VanX:D-alanine complex, an
61 , catalyzes ATP-dependent formation of the d-alanyl-d-alanine dipeptide essential for bacterial cell
62 bination of this motif with the C-terminal D-alanyl-D-alanine moiety required of a DD-peptidase subst
63 hibit DD-peptidases because they mimic the D-alanyl-D-alanine motif of the peptidoglycan substrate of
64 tages of peptidoglycan synthesis, that the d-alanyl-d-alanine of the stem peptide and the lipid II N-
65 e thiols were reacted with either acryloyl-D-alanyl-D-alanine or haloalkanoyl-D-alanyl-D-alanines.
66 hibit this reaction because they mimic the D-alanyl-D-alanine peptide precursors of cell-wall structu
67 lanyl-D-iso-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine peptides, with the exception of the pep
69 in peptidoglycan synthesis) by binding to D-alanyl-D-alanine stem termini in Gram-positive bacteria.
70 atalyze hydrolysis and aminolysis of small D-alanyl-D-alanine terminating peptides, especially those
73 ntibiotics act through their inhibition of D-alanyl-D-alanine transpeptidases (DD-peptidases) that ca
76 ch as glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine, 1, contain the glycyl-L-alpha-amino-ep
77 tide, glycyl-l-alpha-amino-epsilon-pimelyl-d-alanyl-d-alanine, 1, is a very specific and reactive car
78 rate, glycyl-l-alpha-amino-epsilon-pimelyl-d-alanyl-d-alanine, has been described that is much more s
79 alent complex, vancomycin/diacetyl-L-lysyl-D-alanyl-D-alanine, obtained from ESI and from nanoelectro
80 anine-D-glutamate-meso-diaminopimelic acid-D-alanyl-D-alanine, whereas those isolated from lipid II f
82 gh site-directed mutagenesis of the murein D-alanyl-D-alanine-adding enzyme from Escherichia coli (mu
83 ormed on three virulent PAI proteins (Fic; D-alanyl-D-alanine-carboxypeptidase; transposase) dated th
84 catalyzes the hydrolysis and aminolysis of d-alanyl-d-alanine-terminating peptides by specific amines
88 sotropic, and anisotropic Raman spectra of L-alanyl-D-alanyl-L-alanine, acetyl-L-alanyl-L-alanine, L-
89 a holin-like protein (ChiW) and a putative l-alanyl-d-glutamate endopeptidase (ChiX), and subsequent
90 ylococcus aureus MurE UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase (MurE
91 inal domain resembles UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase (MurE), y
93 ding protein for apoptotic N-acetylmuramyl-L-alanyl-D-isoglutamine (L,D-MDP) or peptidoglycan in RK(1
95 nist, N-acetylglucosaminyl-N-acetylmuramyl-l-alanyl-d-isoglutamyl-meso-diaminopimelic acid (GM-triDAP
96 tidoglycan chain precursors terminating in D-alanyl-D-lactate (D-Ala-D-lactate) rather than D-Ala-D-A
100 strate, 3-(N-glycyl-l-cysteinyl)-propanoyl-d-alanyl-d-thiolactate, that the enzyme hydrolyzes and ami
103 o this reaction inhibited the formation of D-alanyl-Dcp and stimulated the hydrolysis of D-alanyl-Dcp
104 In previous results it was shown that D-alanyl-Dcp donates its ester residue to membrane-associa
105 us, may determine the donor specificity of D-alanyl-Dcp in the D-alanylation of membrane-associated D
106 l-Dcp was functionally identical to native D-alanyl-Dcp in the incorporation of D-alanine into lipote
108 Dcp with D-alanine and that the resulting D-alanyl-Dcp is translocated to the primary site of D-alan
112 ard the palladated pincer complexes with the alanyl derivative being the strongest overall, demonstra
116 a mechanism for the transacylation of the D-alanyl ester residues between LTA and wall teichoic acid
118 ngle insertion in dltA exhibited a loss of D-alanyl esters in lipoteichoic acid (LTA) and a loss of i
119 - 1,6 - anhydro - N - acetylmuramyl - (L) - alanyl - gamma - (D) - glutamyl - meso - diaminopimelyl
120 A cephalosporin analogue, 7beta-[N-Acetyl-L-alanyl-gamma-D-glutamyl-L-lysine]-3-acetoxymethyl-3-ceph
122 es, i.e., recycles, its murein tripeptide, L-alanyl-gamma-D-glutamyl-meso-diaminopimelate, to form ne
124 pimelic acid bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, was de
126 he GLN group (n = 75) received PN containing alanyl-GLN dipeptide (0.5 g/kg/d), proportionally replac
129 -competence of PD fluid supplementation with alanyl-glutamine (AlaGln) in 6 patients in an open-label
134 ast, increasing O-GlcNAc levels by PUGNAc or alanyl-glutamine led to significantly improved cell surv
135 ls and evaluate the effects of glutamine and alanyl-glutamine on TxA-induced apoptosis in vitro and d
139 and its stable and highly soluble derivative alanyl-glutamine, have been beneficial in models of inte
142 onic model dipeptides, L-alanyl-L-alanine, L-alanyl-glycine, glycyl-L-alanine, and glycyl-glycine, in
143 e and mechanisms of LTA modifications with D-alanyl, glycosyl, and phosphocholine residues will be di
144 ce, phi11(Delta181-381), revealed that the D-alanyl-glycyl endopeptidase activity is contained within
145 Our results show that the phi11 enzyme has D-alanyl-glycyl endopeptidase as well as N-acetylmuramyl-L
149 ndent ligase responsible for carnosine (beta-alanyl-histidine) and homocarnosine (gamma-aminobutyryl-
151 ydrophobic ProTide was made by replacing the alanyl isopropyl ester present in tenofovir alafenamide
152 methyl]-4-methylpentanoyl)-L-3-(tert-bu tyl)-alanyl-l -alanine, 2-aminoethyl amide), which has previo
155 )- methyl]-4-methylpentano)-L-3-(tert-butyl)-alanyl-L-alanine, 2-aminoethyl amide, which blocks leuko
156 and anisotropic Raman spectra of L-alanyl-D-alanyl-L-alanine, acetyl-L-alanyl-L-alanine, L-vanyl-L-v
157 ies of four zwitterionic model dipeptides, L-alanyl-L-alanine, L-alanyl-glycine, glycyl-L-alanine, an
158 tra of L-alanyl-D-alanyl-L-alanine, acetyl-L-alanyl-L-alanine, L-vanyl-L-vanyl-L-valine, L-seryl-L-se
159 e synthetic substrate N-t-butyloxycarbonyl-L-alanyl-L-alanyl-L-aspartyl (Boc-Ala-Ala-Asp) thiobenzyl
160 ic substrate N-t-butyloxycarbonyl-L-alanyl-L-alanyl-L-aspartyl (Boc-Ala-Ala-Asp) thiobenzyl ester wit
162 unable to use the dipeptide carnosine (beta-alanyl-L-histidine) as a sole carbon or nitrogen source
164 The endogenous dipeptide carnosine (beta-alanyl-L-histidine), at 0.1-10 mM, provokes sustained co
165 , a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of verte
167 ted peptide prodrugs such as N-succinyl-beta-alanyl-L-isoleucyl-L-alanyl-L-leucyl-Dox (sAIAL-Dox).
170 PI-0004Na [N-succinyl-beta-alanyl-L-leucyl-L-alanyl-L-leucyl-Dox (sALAL-Dox)] has been shown to have
171 xorubicin (Dox), CPI-0004Na [N-succinyl-beta-alanyl-L-leucyl-L-alanyl-L-leucyl-Dox (sALAL-Dox)] has b
172 l --> gas exchange of Xe in self-assembled L-alanyl-L-valine (AV) nanotubes was facilitated by contin
173 oxycarbonyl-isoleucyl-glutamyl(O-tert-butyl)-alanyl-leucinal (PSI), could be a source of Ag-specific
174 tion of D-alanine into membrane-associated D-alanyl-lipoteichoic acid in Lactobacillus casei requires
177 Dcp was incubated with membrane-associated D-alanyl LTA, a time and concentration-dependent formation
181 Recombinant mouse PM20D2 hydrolyzed beta-alanyl-lysine, beta-alanyl-ornithine, gamma-aminobutyryl
182 he accumulation of abnormal dipeptides (beta-alanyl-lysine, beta-alanyl-ornithine, gamma-aminobutyryl
183 2 (MMP2), interleukin (IL)-6, insulin (INS), alanyl (membrane) aminopeptidase (ANPEP), and IL-10 were
184 GC1 enzyme, also has space available for a D-alanyl methyl group because of an extended omega loop.
187 of a H-bonding interaction between the 2'-O-alanyl moiety and the N-3 atom of the adenine nucleobase
190 phenylcarbamoyl-(S)-prolyl-(S)-3-(2-naphthyl)alanyl-N-benz yl- N-methylamide, SDZ NKT 343), a highly
191 zenepropanoyl-2,3- idehydro-N-methylalanyl-L-alanyl-N-methyl-L-alanyl-(3R)-3-[[(2S,3R)-3-hydroxy-4- m
192 bnormal dipeptides (beta-alanyl-lysine, beta-alanyl-ornithine, gamma-aminobutyryl-lysine), thus favor
193 e PM20D2 hydrolyzed beta-alanyl-lysine, beta-alanyl-ornithine, gamma-aminobutyryl-lysine, and gamma-a
196 O-[N-(2,7-difluoro-4'-fluoresceincarbonyl)-L-alanyl]paclitaxel, a fluorescent paclitaxel derivative,
199 say in the presence of radioactively labeled alanyl-PG then revealed hydrolysis of the aminoacyl link
201 ol (PG) catalyzed by Ala-tRNA(Ala)-dependent alanyl-phosphatidylglycerol synthase (A-PGS) or by Lys-t
202 s, such as histidyl (Jo-1), threonyl (PL-7), alanyl (PL-12), glycyl (EJ), and isoleucyl (OJ), are clo
204 , which provides a general method to prepare alanyl proteins from their cysteinyl forms, can be used
205 f HPr is replaced with an unphosphorylatable alanyl residue are resistant to carbon catabolite repres
206 either a central pyridyl glycyl or a pyridyl alanyl residue between two terminally protected glycines
208 ATP-dependent addition of D-glutamate to an alanyl residue of the UDP-N-acetylmuramyl-L-alanine prec
212 aration of lysyl charges by intercalation of alanyl residues reduced assembly promoting potency for h
214 0)-O(eq)-glycyl-ryanodine < C(10)-O(eq)-beta-alanyl-ryanodol, implying an inverse relationship with t
216 se inhibitor N-(N-[3,5-difluorophenacetyl]-l-alanyl)-S-phenylglycine t-butyl ester (DAPT) or followin
217 se inhibitor N-(N-(3,5-difluorophenacetyl)-l-alanyl)-S-phenylglycine t-butyl ester, supporting the co
218 ase inhibitor N-[N-(3,5-Difluorophenacetyl-L-alanyl)-S-phenylglycine]-t-butyl ester, which blocks Not
219 se inhibitors N-[N-(3,5-difluorophenacetyl-L-alanyl)]-S-phenylglycine t-butyl ester and L-685,458.
220 ibitor, DAPT (N-[N-(3,5-difluorophenacetyl-l-alanyl)]-S-phenylglycine t-butyl ester), reduces the sur
221 ted whether N-[N-(3,5-difluorophenylacetyl-l-alanyl)]-S-phenylglycine t-butylester (DAPT), a specific
222 mma-secretase inhibitor difluorophenacetyl-l-alanyl-S-phenylglycine t-butyl ester (DAPT) or dimethyl
223 ibitor DAPT (N-[N-(3,5-Difluorophenacetyl)-l-alanyl]-S-phenyl glycine t-butylester) abrogates GH-indu
224 treated with N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglucine t-butyl ester (DAPT), a gamma-se
225 ng inhibitor N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester (DAPT) significant
226 Similarly N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester (DAPT), a chemical
227 istration of N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester (DAPT), a gamma-se
228 e inhibitor, N-[N-(3,5-difluorophenacetyl)-1-alanyl]-S-phenylglycine t-butyl ester (DAPT), or Notch1
229 e inhibitor, N-[N-(3,5-Difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester (DAPT), which sign
230 se inhibitor N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester failed to promote
231 ibitor DAPT (N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester) diminished these
232 ibitor (GSI) N-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycine-t-butylester (DAPT), at a dose t
233 ase inhibitorN-[N-(3,5-difluorophenacetyl)-l-alanyl]-S-phenylglycinet-butyl ester negated the up-regu
234 ch inhibitor N-[N-(3,5-difluorophenacetyl)-L-alanyl]-(S)-phenylglycine t-butyl ester (DAPT) preferent
235 we show that N-[N-(3,5-difluorophenacetyl)-L-alanyl]-(S)-phenylglycine t-butyl ester, a potent gamma-
236 h inhibitor (N-[N-(3,5-difluorophenacetyl)-L-alanyl]-(S)-phenylglycine t-butyl ester; DAPT) was admin
237 hat different rotameric states of the indole alanyl side-chain are responsible for the observed fluor
239 tures, none of the single, double, or triple alanyl substitutions at arginyl residues significantly d
240 readily hydrolyzes and aminolyzes acyclic D-alanyl substrates than glycyl analogues, in contrast to
241 owever, no enhancement of activity against D-alanyl substrates with respect to glycyl was observed.
242 lycyl substrates but not for more specific d-alanyl substrates; hydroxy acids actually behave, more g
244 the presence of thiol probably proceeds via alanyl thioester, which is produced by rearrangement of
248 tase autoantibody (anti-Jo-1) and 1 had anti-alanyl-transfer RNA synthetase autoantibody (anti-PL-12)
249 Ps in the coding regions of two human mRNAs: alanyl tRNA synthetase and replication protein A, 70-kDa
250 s that bacterial GlyRS is closely related to alanyl tRNA synthetase, which led us to define a new sub
252 al neuropathy, demonstrating that defects of alanyl-tRNA charging can result in a wide spectrum of di
253 identified mutations in the nuclear-encoded alanyl-tRNA synthetase (AARS) in these two unrelated fam
255 observed that BMAA is a substrate for human alanyl-tRNA synthetase (AlaRS) and can form BMAA-tRNA(Al
256 tion of alanine-specific tRNA (tRNA(Ala)) by alanyl-tRNA synthetase (AlaRS) gave rise to the concept
258 Throughout evolution, tRNA(Ala) selection by alanyl-tRNA synthetase (AlaRS) has depended predominantl
259 Transfer of alanine from Escherichia coli alanyl-tRNA synthetase (AlaRS) to RNA minihelices that m
261 ) that are associated with aminoacylation by alanyl-tRNA synthetase (AlaRS) were investigated in vivo
262 ypomorphic mutation in the editing domain of alanyl-tRNA synthetase (AlaRS), resulted in accumulation
264 n AARS2 (NM_020745.2) encoding mitochondrial alanyl-tRNA synthetase (mt-AlaRS) were first described i
266 es of an active fragment of Aquifex aeolicus alanyl-tRNA synthetase complexed, separately, with Mg2+-
267 activator of hsp90 ATPase protein 1 (Aha1), alanyl-tRNA synthetase domain containing 1 (Aarsd1), cel
268 minihelix) lacked determinants for editing, alanyl-tRNA synthetase effectively cleared a mischarged
271 ssense mutation in the editing domain of the alanyl-tRNA synthetase gene that compromises the proofre
272 d, a small defect in the editing activity of alanyl-tRNA synthetase is causally linked to neurodegene
273 he AlaXp redundancy of the editing domain of alanyl-tRNA synthetase is thought to reflect an unusual
274 y was within 1-2 kcal.mol(-1) of a truncated alanyl-tRNA synthetase that has aminoacylation activity
276 he transfer of alanine from Escherichia coli alanyl-tRNA synthetase to a cognate RNA minihelix involv
277 e contacts between tRNA and Escherichia coli alanyl-tRNA synthetase, an enzyme previously shown to in
278 ponents, such as the alpha-subunit of phenyl-alanyl-tRNA synthetase, and several metabolic enzymes.
280 te that prevents aminoacylation by the dicot alanyl-tRNA synthetase, indicating that features identif
282 d by a strain harboring an editing-defective alanyl-tRNA synthetase, was rescued by an AlaXp-encoding
283 agenesis of the homologous editing pocket of alanyl-tRNA synthetase, where even a mild defect in edit
284 , we examined a fragment of Escherichia coli alanyl-tRNA synthetase, which catalyzes aminoacyl adenyl
289 not to be a substrate for (re)activation by alanyl-tRNA synthetase.Application of the optimized syst
290 sing from confusion of serine for alanine by alanyl-tRNA synthetases (AlaRSs) has profound functional
291 evented in part by the editing activities of alanyl-tRNA synthetases (AlaRSs), which remove serine fr
293 n bacterial and eukaryotic threonyl- and all alanyl-tRNA synthetases is missing from archaebacterial
297 yzes the transfer of the alanyl residue from alanyl-tRNA to the N terminus of the tetrapeptide interm
301 uent cross coupling of the aryl iodide to an alanyl zinc reagent (in the presence of a Pd(0) catalyst