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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-
4                                            D-Alanyl-ACP in the presence of LTA was not hydrolyzed.
5 catalyzed the hydrolysis of the mischarged D-alanyl-ACP.
6 d has thioesterase activity for mischarged D-alanyl-acyl carrier proteins (ACPs).
7 elevated acylation velocities with seryl and alanyl-adenylates.
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
10 l endopeptidase as well as N-acetylmuramyl-L-alanyl amidase activity.
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
17                Protocols that use microsomal alanyl aminopeptidase as a discovery-enabling agent are
18                  Seven crystal structures of alanyl aminopeptidase from Neisseria meningitides (the e
19   Here, enzymatic digestion using microsomal alanyl aminopeptidase is combined with MS characterizati
20               The midgut-specific anopheline alanyl aminopeptidase N (AnAPN1) is highly conserved acr
21                    Here we identify membrane alanyl aminopeptidase N (APN) as a receptor for pea enat
22 mycin-sensitive aminopeptidase (PSA, cytosol alanyl aminopeptidase).
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
25         It also acted at lower rates on beta-alanyl-arginine and gamma-aminobutyryl-arginine but virt
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
32          Several possibilities exist for the alanyl beta-cation equivalent, including direct activati
33 ine involve the reaction of cysteine with an alanyl beta-cation equivalent.
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
38 -D-alanyl carrier protein ligase (Dcl) and D-alanyl carrier protein (Dcp), respectively.
39 carrier protein ligase (AMP) (Dcl) and the D-alanyl carrier protein (Dcp).
40 rrier protein ligase (Dcl) and the 8.9-kDa D-alanyl carrier protein (Dcp).
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
43         dltA and dltC encode the D-alanine-D-alanyl carrier protein ligase (Dcl) and D-alanyl carrier
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
46                 This DNA encoded D-alanine-D-alanyl carrier protein ligase that was expressed in Esch
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
50                      The VanX protein is a D-alanyl-D-alanine (D-Ala-D-Ala) dipeptidase essential for
51                        The zinc-containing D-alanyl-D-alanine (D-Ala-D-Ala) dipeptidase VanX has been
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
56 c hedgehog and the Zn(2+)-dependent N-acyl-D-alanyl-D-alanine carboxypeptidase of S. albus G.
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
60                   VanX is a zinc-dependent D-alanyl-D-alanine dipeptidase that is a critical componen
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
68 eptidases, because of their resemblance to D-alanyl-D-alanine peptides.
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
71 iently catalyze acyl transfer reactions of D-alanyl-D-alanine terminating peptides.
72                              The bacterial D-alanyl-D-alanine transpeptidases (DD-peptidases) are the
73 ntibiotics act through their inhibition of D-alanyl-D-alanine transpeptidases (DD-peptidases) that ca
74                Nevertheless, the bacterial D-alanyl-D-alanine transpeptidases (DD-peptidases), the ki
75 the final step of biosynthesis by specific D-alanyl-D-alanine(DD)-peptidases/transpeptidases.
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
81                                        The D-alanyl-D-alanine-adding enzyme encoded by the murF gene
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
85 valent complex vancomycin/diacetyl-L-lysyl-D-alanyl-D-alanine.
86 rate, glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine.
87 cryloyl-D-alanyl-D-alanine or haloalkanoyl-D-alanyl-D-alanines.
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
92       Mycobacterial peptidoglycan contains L-alanyl-D-iso-glutaminyl-meso-diaminopimelyl-D-alanyl-D-a
93 ding protein for apoptotic N-acetylmuramyl-L-alanyl-D-isoglutamine (L,D-MDP) or peptidoglycan in RK(1
94 eoisomeric configuration of the dipeptide (L-alanyl-D-isoglutamine) moiety.
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
97 s and is distinct from previous models for d-alanyl-d-lactate ligase mechanistic studies.
98                           The structure of d-alanyl-d-lactate ligase provides a revised interpretatio
99              The peptides N-(phenylacetyl)-D-alanyl-D-phenylalanine and N-(phenylacetyl)glycyl-D-phen
100 strate, 3-(N-glycyl-l-cysteinyl)-propanoyl-d-alanyl-d-thiolactate, that the enzyme hydrolyzes and ami
101                                            d-Alanyl:d-lactate (d-Ala:d-Lac) and d-alanyl:d-serine lig
102       d-Alanyl:d-lactate (d-Ala:d-Lac) and d-alanyl:d-serine ligases are key enzymes in vancomycin re
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
107       It was discovered that incubation of D-alanyl-Dcp in the presence of LTA resulted in the time-d
108  Dcp with D-alanine and that the resulting D-alanyl-Dcp is translocated to the primary site of D-alan
109 e and concentration-dependent formation of D-alanyl-Dcp was found.
110                            The recombinant D-alanyl-Dcp was functionally identical to native D-alanyl
111 lanyl-Dcp and stimulated the hydrolysis of D-alanyl-Dcp.
112 ard the palladated pincer complexes with the alanyl derivative being the strongest overall, demonstra
113 tion of Ala-PG and a novel alanylated lipid, Alanyl-diacylglycerol (Ala-DAG).
114       Mass spectrometry analysis of aspartyl-alanyl diketopiperazine (DA-DKP) content of HSA and perc
115  disclose their cooperative activity in beta-alanyl-dopamine formation.
116  a mechanism for the transacylation of the D-alanyl ester residues between LTA and wall teichoic acid
117 ovir alafenamide (TAF) with a docosyl phenyl alanyl ester, now referred to as M1TFV.
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
121                      Using N-acetylmuramyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl
122 es, i.e., recycles, its murein tripeptide, L-alanyl-gamma-D-glutamyl-meso-diaminopimelate, to form ne
123  uptake of the cell wall murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate.
124 pimelic acid bond in the murein tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelic acid, was de
125 placed by the cell wall murein tripeptide, L-alanyl-gamma-D-glutamyl-mesodiaminopimelate.
126 he GLN group (n = 75) received PN containing alanyl-GLN dipeptide (0.5 g/kg/d), proportionally replac
127 ng a perioperative supplement of intravenous alanyl-glutamine (0.5 g . kg(-1) . d(-1)).
128 g/ml) in medium with or without glutamine or alanyl-glutamine (3 to 100 mM).
129 -competence of PD fluid supplementation with alanyl-glutamine (AlaGln) in 6 patients in an open-label
130                                              Alanyl-glutamine (AQ) is a highly soluble dipeptide deri
131 taining unmethylated CpG motif (CpG-ODN) and alanyl-glutamine in vivo and in vitro.
132                                  Addition of alanyl-glutamine increased O-GlcNAcylation and partly co
133                                Glutamine and alanyl-glutamine inhibited the apoptosis of T84 cells by
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
136                           Both glutamine and alanyl-glutamine reduced TxA-induced ileal mucosal disru
137                                              Alanyl-glutamine showed similar benefits.
138                                 Glutamine or alanyl-glutamine significantly reduced TxA-induced apopt
139 and its stable and highly soluble derivative alanyl-glutamine, have been beneficial in models of inte
140 ated the protective effects of glutamine and alanyl-glutamine.
141  an N-acetylmuramoyl-L-alanine amidase and D-alanyl-glycine endopeptidase.
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
146                             The N-terminal L-alanyl group is needed for cellular import but not for i
147 ates beta-alanine to histamine, forming beta-alanyl-histamine or carcinine.
148                              Carcinine (beta-alanyl-histamine) is a natural imidazole-containing pept
149 ndent ligase responsible for carnosine (beta-alanyl-histidine) and homocarnosine (gamma-aminobutyryl-
150 g lost its amino terminal dipeptide aspartyl alanyl (HSA-DA) were correlated.
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
153                                     Acetyl-L-alanyl-L-alanine exhibits a structure which is very simi
154                                       That d-alanyl-l-alanine shows little activity as an acceptor su
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
161                              Carnosine (beta-alanyl-l-histidine) and anserine (beta-alanyl-3-methyl-l
162  unable to use the dipeptide carnosine (beta-alanyl-L-histidine) as a sole carbon or nitrogen source
163 g precursor of the dipeptide carnosine (beta-alanyl-l-histidine) in muscle.
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
166 +) and the natural dipeptide carnosine (beta-alanyl-L-histidine).
167 ted peptide prodrugs such as N-succinyl-beta-alanyl-L-isoleucyl-L-alanyl-L-leucyl-Dox (sAIAL-Dox).
168 nzoxy-L-isoleucyl-gamma-t-butyl-L-glutamyl-L-alanyl-L-leucinal (PSI), to rodents.
169 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
175 n the D-alanylation of membrane-associated D-alanyl-lipoteichoic acid.
176              Thus, it is hypothesized that D-alanyl LTA may provide binding sites for the putative 10
177 Dcp was incubated with membrane-associated D-alanyl LTA, a time and concentration-dependent formation
178 ates on some "classic dipeptides" like alpha-alanyl-lysine and alpha-lysyl-lysine.
179 lotting showed coelution of PM20D2 with beta-alanyl-lysine dipeptidase activity.
180  heart, and brain contained a cytosolic beta-alanyl-lysine dipeptidase activity.
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.
185         Molecular modeling showed that the D-alanyl methyl group fits snugly into the space originall
186           Accommodation of the penultimate D-alanyl methyl group is therefore necessary for efficient
187  of a H-bonding interaction between the 2'-O-alanyl moiety and the N-3 atom of the adenine nucleobase
188 f the glycyl-l-alpha-amino-epsilon-pimelyl-d-alanyl moiety to amines.
189                               Anserine (beta-alanyl-N(Pi)-methyl-L-histidine), a methylated derivativ
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
194                        The ester 4-((tosyl-l-alanyl)oxy)phenyl tosyl-l-alaninate (TAPTA) was synthesi
195 apable of hydrolyzing the substrate N-acetyl-alanyl-p-nitroanilide.
196 O-[N-(2,7-difluoro-4'-fluoresceincarbonyl)-L-alanyl]paclitaxel, a fluorescent paclitaxel derivative,
197 rcuit for the appropriate tuning of cellular alanyl-PG concentrations.
198              Consequently, PA0919 was termed alanyl-PG hydrolase.
199 say in the presence of radioactively labeled alanyl-PG then revealed hydrolysis of the aminoacyl link
200 9 indicated significantly enlarged levels of alanyl-PG.
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
203               The phenylalanyl-glycyl-glycyl-alanyl-prolyl (FG-GAP) domain plays an important role in
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
207           PacB catalyzes the transfer of the alanyl residue from alanyl-tRNA to the N terminus of the
208  ATP-dependent addition of D-glutamate to an alanyl residue of the UDP-N-acetylmuramyl-L-alanine prec
209 rium leprae, in which glycine replaces the L-alanyl residue.
210 e of covalent FAD attachment (Cys-406) to an alanyl residue.
211             In addition, both the glycyl and alanyl residues of the GXXXG or GXXXA motifs form van de
212 aration of lysyl charges by intercalation of alanyl residues reduced assembly promoting potency for h
213                                         When alanyl residues replaced all TMD residues except Ser(16)
214 0)-O(eq)-glycyl-ryanodine < C(10)-O(eq)-beta-alanyl-ryanodol, implying an inverse relationship with t
215 0)-O(eq)-glycyl-ryanodine > C(10)-O(eq)-beta-alanyl-ryanodol.
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
238                                              Alanyl-substituted and N-terminal truncated analogues id
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
243 cysteinyl-sulfamoyl-, prolyl-sulfamoyl-, and alanyl-sulfamoyl-adenylates.
244  the presence of thiol probably proceeds via alanyl thioester, which is produced by rearrangement of
245 d in the time-dependent hydrolysis of this D-alanyl thioester.
246                                 A complex of alanyl-tmRNA (which functions as a tRNA and mRNA), SmpB
247                   Biallelic mutations in the alanyl-transfer (t)RNA synthetase 2 (AARS2) gene were fo
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
251 e relatively easily altered to be charged by alanyl tRNA synthetase.
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
254 ntly recognized by A. gossypii mitochondrial alanyl-tRNA synthetase (AgAlaRS).
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
257               Here we show that the class II alanyl-tRNA synthetase (AlaRS) has a specialized interna
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
260  machinery provides MurM, quality control by alanyl-tRNA synthetase (AlaRS) was investigated.
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
263  major determinants for recognition by Dm mt alanyl-tRNA synthetase (AlaRS).
264 n AARS2 (NM_020745.2) encoding mitochondrial alanyl-tRNA synthetase (mt-AlaRS) were first described i
265                      Paradoxically, although alanyl-tRNA synthetase activates glycine as well as alan
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
269                                              Alanyl-tRNA synthetase efficiently aminoacylates tRNAAla
270                                      Data on alanyl-tRNA synthetase from an early eukaryote and other
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
275         Here we identify a two-helix pair in alanyl-tRNA synthetase that is required for RNA microhel
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.
279        Here we show that the editing site of alanyl-tRNA synthetase, as an artificial recombinant fra
280 te that prevents aminoacylation by the dicot alanyl-tRNA synthetase, indicating that features identif
281             When applied to Escherichia coli alanyl-tRNA synthetase, the assay allowed accurate measu
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
285                        Similarly, autonomous alanyl-tRNA synthetase-editing domain homologues (AlaX p
286  (G3.U70) marks a tRNA for aminoacylation by alanyl-tRNA synthetase.
287 for clearance of errors of aminoacylation by alanyl-tRNA synthetase.
288       We report that CDC64 encodes Ala1p, an alanyl-tRNA synthetase.
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
292 rative aminoacylation and editing domains of alanyl-tRNA synthetases (AlaRSs).
293 n bacterial and eukaryotic threonyl- and all alanyl-tRNA synthetases is missing from archaebacterial
294       G. lamblia's archaeal-type prolyl- and alanyl-tRNA synthetases refine our understanding of the
295 ome-encoded homolog of the editing domain of alanyl-tRNA synthetases.
296 nine, is activated by both human prolyl- and alanyl-tRNA synthetases.
297 yzes the transfer of the alanyl residue from alanyl-tRNA to the N terminus of the tetrapeptide interm
298 on in mutants forming substantial amounts of alanyl-tRNAAla.
299 ate quality of the molecule for formation of alanyl-tRNAAla.
300 ay that could significantly amplify cellular alanyl-tRNAAla.
301 uent cross coupling of the aryl iodide to an alanyl zinc reagent (in the presence of a Pd(0) catalyst

 
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