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1 rly zebrafish melanoblast marker, dopachrome tautomerase.
2 gulatory protein as well as a phenylpyruvate tautomerase.
3 an inhibitor of the enzyme 4-oxalocrotonate tautomerase.
4 DH) and Rpa1177, a putative 4-oxalocrotonate tautomerase.
5 h two bacterial isomerases, 4-oxalocrotonate tautomerase (4-OT) and 5-(carboxymethyl)-2-hydroxymucona
6 us to the bacterial enzymes 4-oxalocrotonate tautomerase (4-OT) and 5-carboxymethyl-2-hydroxymuconate
8 nhibitors of three enzymes: 4-oxalocrotonate tautomerase (4-OT) and vinylpyruvate hydratase (VPH) fro
10 e reaction catalyzed by the 4-oxalocrotonate tautomerase (4-OT) enzyme has been studied using a quant
11 62 amino acid member of the 4-oxalocrotonate tautomerase (4-OT) family, was pro-immunogenic in mice w
13 e amino-terminal proline of 4-oxalocrotonate tautomerase (4-OT) functions as the general base catalys
14 lyst Pro-1 (pK(a) = 6.4) in 4-oxalocrotonate tautomerase (4-OT) has been ascribed to both a low diele
15 r the kinetic parameters of 4-oxalocrotonate tautomerase (4-OT) have been measured using 2-hydroxy-2,
17 The crystal structure of 4-oxalocrotonate tautomerase (4-OT) inactivated by the active site-direct
21 jor families represented by 4-oxalocrotonate tautomerase (4-OT), 5-(carboxymethyl)-2-hydroxymuconate
22 tion secondary structure of 4-oxalocrotonate tautomerase (4-OT), a 41 kDa homohexamer with 62 residue
24 lecular weight 47,547), and 4-oxalocrotonate tautomerase (4-OT), an (alpha)(6) homohexamer, distingui
25 nd the bacterial isomerase, 4-oxalocrotonate tautomerase (4-OT), thereby distinguishing CaaD from a n
26 cluding carbonic anhydrase, 4-oxalocrotonate tautomerase (4OT) analogue, and SecB, a chaperone from E
27 de backbone interactions in 4-oxalocrotonate tautomerase (4OT) catalysis has been investigated using
29 , Tyr, Tyr-related protein 1, and dopachrome tautomerase accumulated in enlarged granules distributed
32 ian MIFs, it has critical differences in the tautomerase active site that account for the different i
34 l-molecular-weight inhibitor targeting MIF's tautomerase activity (SCD-19) significantly reduces the
36 een described recently to exhibit dopachrome tautomerase activity and to be structurally homologous t
37 For instance, the IC(50) inhibition of MIF tautomerase activity by aromatic amino acid Schiff base
39 ine oxidation drop rapidly, while DOPAchrome tautomerase activity increases and dihydroxyindole carbo
41 ted for biaryltriazoles as inhibitors of the tautomerase activity of human macrophage migration inhib
42 ibitors of the p-hydroxyphenylpyruvate (HPP) tautomerase activity of MIF and an allosteric binding si
46 To identify small-molecule inhibitors of the tautomerase activity of PfMIF, virtual screening has bee
47 MIF inhibitors has focused on monitoring the tautomerase activity using l-dopachrome methyl ester or
50 t lacks oxidoreductase activity but exhibits tautomerase activity with a specific activity of 19.3 mu
51 rongly correlated with the inhibition of MIF tautomerase activity, a connection not made previously t
52 oxycinnamate, a competitive inhibitor of the tautomerase activity, has been determined to 1.8 A resol
54 The effect of a specific inhibitor of MIF-tautomerase activity, ISO-1, was investigated in PBMCs.
55 teins were compared using in vitro assays of tautomerase activity, macrophage migration, and binding
56 er (ISO-1), an inhibitor of MIF d-dopachrome tautomerase activity, reveals that ISO-1 binds to the sa
58 elatively nonspecific 1,3- and 1,5-keto-enol tautomerase activity, with the former activity prevailin
65 We designed small molecules to inhibit this tautomerase activity; a lead molecule, "ISO-1 ((S,R)-3-(
67 hancer required for expression of dopachrome tautomerase, an enzyme that functions in melanin synthes
68 ve site similar to those of 4-oxalocrotonate tautomerase and 5-carboxymethyl-2-hydroxymuconate isomer
69 t of two microbial enzymes (4-oxalocrotonate tautomerase and 5-carboxymethyl-2-hydroxymuconate isomer
70 inhibitory factor (MIF) is both a keto-enol tautomerase and a cytokine associated with numerous infl
72 d mechanism of action, the protein is also a tautomerase and has a catalytically active N-terminal pr
73 and tyrosinase-related protein 2/dopachrome tautomerase and increased protection from a lethal chall
74 als that, unusually for a cytokine, exhibits tautomerase and oxidoreductase enzymatic activities.
76 se, tyrosinase-related protein-1, dopachrome tautomerase, and Pmel17, are known, the function of MART
77 -associated transcription factor, dopachrome tautomerase, and tyrosinase promoters, leading to an inc
79 itory factor (MIF), its homolog D-dopachrome tautomerase (D-DT), and their common receptor CD74 may c
80 IF) and its functional homolog, d-dopachrome tautomerase (d-DT), have protumorigenic functions in non
81 d its only known family member, D-dopachrome tautomerase (D-DT), promote the expression of proangioge
82 tory activity for extracellular d-dopachrome tautomerase (D-DT), the recruitment of neutrophils to th
83 TRP1) and 3,4-dihydroxyphenylalanine-chrome tautomerase (Dct or TRP2) encoded at the Tyrp1/brown and
89 sinase-related protein-1 (Tyrp1), dopachrome tautomerase (Dct), and LAMP1 and 3 localization in HPS-3
90 al precursor cells (line Ntva) or dopachrome tautomerase (DCT)-expressing melanoblasts (line DCTtva)
91 elated protein-1 (TYRP1/gp75) and dopachrome tautomerase (DCT/TYRP2) belong to a family of melanocyte
92 nt work by others has described D-dopachrome tautomerase (DDT) as a functional homologue of MIF with
94 identify the function of TenI as a thiazole tautomerase, describe the structure of the enzyme comple
95 (olfactory receptors, OR) and phenylpyruvate tautomerase/dopachrome isomerase activity (MIF and DDT g
97 the quaternary structure of 4-oxalocrotonate tautomerase (EC 5.3.2; 4OT), and four analogues prepared
98 tophilus, and M. aeruginosa RLPs function as tautomerases/enolases in a methionine salvage pathway (M
100 F) is a proinflammatory mediator with unique tautomerase enzymatic activity; the precise function has
103 base, Pro-1, of the enzyme 4-oxalocrotonate tautomerase has been mutated to Gly, Ala, Val, and Leu,
105 found at the active site of 4-oxalocrotonate tautomerase in the X-ray structure of the affinity-label
107 mpounds are likely the most potent known MIF tautomerase inhibitors; the most active ones are more th
110 y have evolved from a short 4-oxalocrotonate tautomerase-like ancestor followed by gene duplication a
113 used in MIF wild-type mice (mif(+/+)) and in tautomerase-null, MIF gene knockin mice (mif (P1G/P1G)).
114 be activated by MITF, including dautochrome tautomerase, pMel 17/Silver and tyrosinase-related prote
121 ecules that bind at the catalytically active tautomerase site of MIF and tested the complex for MIF b
122 olecule MIF inhibitors typically bind in the tautomerase site of the MIF trimer, often covalently mod
123 homology with significant differences in the tautomerase sites of the human and hookworm proteins.
126 at the evolution of new functions within the tautomerase superfamily could be quite facile, requiring
127 This is the first reported observation of a tautomerase superfamily member functioning by covalent c
128 d trans-3-chloroacrylic acid dehalogenase, a tautomerase superfamily member preceding MSAD in the tra
129 (MSAD) from Pseudomonas pavonaceae 170 is a tautomerase superfamily member that converts malonate se
130 ot exhibit the low-level activity of another tautomerase superfamily member, the heterohexamer trans-
131 d for Pro1 and the conserved arginine in all tautomerase superfamily members characterized thus far,
132 ino-terminal proline, conserved in all known tautomerase superfamily members, functioning as a genera
133 characterized member of a new family in the tautomerase superfamily that probably resulted from an i
134 acid dehalogenase (CaaD) are members of the tautomerase superfamily, a group of structurally homolog
139 t irreversible inhibitor of 4-oxalocrotonate tautomerase than is 2-OP suggest that Arg-39" and the or
140 f the functions assigned to MIF is that of a tautomerase that interconverts the enol and keto forms o
141 H from dopachrome is catalyzed by dopachrome tautomerase, that the melanogenic protein tyrosinase-rel
143 tyrosinase-related protein-1 and dopachrome tautomerase/tyrosinase-related protein-2 and transactiva
145 One of those enzymes is 4-oxalocrotonate tautomerase, with which CaaD seems to share a common evo
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