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1 S*,R*)-N-[[2-[N-(2-amino-3-mercaptopropyl)-L-valyl]-1,2,3,4- tetrahydro-3-isoquinolinyl]carbonyl]-L-m
2 trahydro-2-[N-[2-(1H-imidazol-4-yl)ethyl] -L-valyl]-3-isoquinolinyl]carbonyl]-L-methionine ([imidazol
3 A synthetase misactivates valine (to produce valyl adenylate or Val-tRNA(Ile)) at its active site.
5 d 7 because benzyloxycarbonyl-valyl-aspartyl-valyl-alanyl-aspartic acid fluoromethyl ketone (Z-VDVAD-
6 the potent antiapoptotic agent carbobenzoxy-valyl-alanyl-aspartyl(beta-methyl ester)-fluoromethyl ke
7 with the pancaspase inhibitor carbobenzoxyl-valyl-alanyl-aspartyl-[O-methyl]-fluoromethylketone befo
8 nd SuVP reagents are the same except for the valyl and aspartyl groups which provide a distinctive ch
10 spase inhibitor) or acetyl-aspartyl-glutamyl-valyl-aspart-1-aldehyde (a relatively selective caspase-
11 aspase 2, 3, and 7 because benzyloxycarbonyl-valyl-aspartyl-valyl-alanyl-aspartic acid fluoromethyl k
12 the 5'-glycyl ester of acyclovir, and the 5'-valyl ester of zidovudine (AZT), was purified from Caco-
14 by treatment with N-benzyloxycarbonyl-leucyl-valyl-glycine diazomethyl ketone lacked the 66-kDa gelat
15 with the subsequent mole fractions of [14C] valyl groups that could be covalently transferred to the
17 e substrates, acetyl-L-aspartic-L-glutamic-L-valyl-L-aspartic acid 4-methyl-7-aminocoumarin or acetyl
19 l cleavage of acetyl-L-aspartic-L-glutamic-L-valyl-L-aspartic acid 4-methyl-7-aminocoumarin within 6
21 d FMOC-l-valine, and a dipeptide, N-acetyl-l-valyl-l-leucine (N-Ac-VL), were studied via one- and two
22 scent peptide N-succinyl-L-leucyl-L-leucyl-L-valyl-L-tyrosine-7-amido-4- methylcoumarin or the microt
23 ent substrate N-succinyl-L-leucyl-L-leucyl-L-valyl-L-tyrosine-7-amido-4-methylcouma rin, as well as t
24 phenylalanyl-lysine-fluorescein and N-formyl-valyl-leucyl-phenylalanyl-lysine-fluorescein to the N-fo
26 fied tRNA transcripts of four specificities (valyl, methionyl, alanyl, and phenylalanyl) from higher
27 t of the hydrolysis of P5, N,N-dimethylvalyl-valyl-N-methylvalyl-proline (P4), had little activity as
28 lularly, with formation of N,N-dimethylvalyl-valyl-N-methylvalyl-prolyl-proline (P5), a pentapeptide
29 s shows that this use of a chirally resolved valyl phosphonate results in selection of much more pote
30 experiment, a single-enantiomer form of the valyl phosphonate was used rather than a racemic mixture
32 lecular weight MyD88 mimic, hydrocinnamoyl-l-valyl pyrrolidine (compound 4a), modeled on a tripeptide
34 ransient overexpression of editing-defective valyl-tRNA synthetase (ValRS(ED)) activated DNA break-re
35 actions between Escherichia coli tRNAVal and valyl-tRNA synthetase (ValRS) by enzymatic footprinting
36 mologs isoleucyl-tRNA synthetase (IleRS) and valyl-tRNA synthetase (ValRS) deacylate Val-tRNA(Ile) an
39 uRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) have evolved a discrete ed
40 uRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) share a common insertion,
41 n Escherichia coli tRNAValfor recognition by valyl-tRNA synthetase (ValRS), nucleotides in the accept
44 NMR also shows that formation of the tRNAVal-valyl-tRNA synthetase complex does not disrupt the first
46 the homologous isoleucyl-tRNA synthetase and valyl-tRNA synthetase editing active sites, play a centr
48 tive peptide 1; CP1 domain), LeuRS resembles valyl-tRNA synthetase in its reliance on post-transfer e
53 hing the identity of the human mitochondrial valyl-tRNA synthetase then inducing its overexpression i
55 tic analyses of beta-tubulin, chaperonin 60, valyl-tRNA synthetase, and EF-1alpha, suggests a sister-
56 or analyses of isoleucyl-tRNA synthetase and valyl-tRNA synthetase, these experiments provide the bas
59 mportant for proper recognition of tRNAValby valyl-tRNA synthetase.19F NMR also shows that formation
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