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1 ct against proteasomal inhibition induced by dopachrome.
2 and (p-hydroxyphenyl)pyruvate and converts D-dopachrome, a stereoisomer of naturally occurring L-dopa
4 rwent tyrosinase-catalyzed oxidation to form dopachrome, and similar to aminochrome, proteasomal inhi
5 en shown that formation of (HO)2IndCOOH from dopachrome is catalyzed by dopachrome tautomerase, that
7 oxidase, phenol oxidase, and interleukin 1, dopachrome isomerase and other, as of yet unidentified,
8 note, molecular modeling of the substrate L-dopachrome methyl ester into the active site of MIF sugg
9 monitoring the tautomerase activity using l-dopachrome methyl ester or 4-hydroxyphenyl pyruvic acid
10 n of the non-naturally occurring D-isomer of dopachrome, phenylpyruvate, and certain catecholamines,
12 ation inhibitory factor (MIF), its homolog D-dopachrome tautomerase (D-DT), and their common receptor
13 y factor (MIF) and its functional homolog, d-dopachrome tautomerase (d-DT), have protumorigenic funct
14 rine MIF and its only known family member, D-dopachrome tautomerase (D-DT), promote the expression of
15 ew inflammatory activity for extracellular d-dopachrome tautomerase (D-DT), the recruitment of neutro
21 inase, tyrosinase-related protein-1 (Tyrp1), dopachrome tautomerase (Dct), and LAMP1 and 3 localizati
22 essing neural precursor cells (line Ntva) or dopachrome tautomerase (DCT)-expressing melanoblasts (li
23 yrosinase-related protein-1 (TYRP1/gp75) and dopachrome tautomerase (DCT/TYRP2) belong to a family of
28 melanocytes, Tyr, Tyr-related protein 1, and dopachrome tautomerase accumulated in enlarged granules
29 also has been described recently to exhibit dopachrome tautomerase activity and to be structurally h
30 yphenylalanine oxidation drop rapidly, while DOPAchrome tautomerase activity increases and dihydroxyi
32 methyl ester (ISO-1), an inhibitor of MIF d-dopachrome tautomerase activity, reveals that ISO-1 bind
33 igens gp100 and tyrosinase-related protein 2/dopachrome tautomerase and increased protection from a l
40 nd of the melanogenic enzymes tyrosinase and dopachrome tautomerase, all major players in melanogenes
41 cy of an enhancer required for expression of dopachrome tautomerase, an enzyme that functions in mela
42 as tyrosinase, tyrosinase-related protein-1, dopachrome tautomerase, and Pmel17, are known, the funct
43 rophthalmia-associated transcription factor, dopachrome tautomerase, and tyrosinase promoters, leadin
44 osinase or on the mRNA levels of tyrosinase, dopachrome tautomerase, Pmel17, or MITF mRNA levels.
45 (HO)2IndCOOH from dopachrome is catalyzed by dopachrome tautomerase, that the melanogenic protein tyr
47 tyrosinase, tyrosinase-related protein-1 and dopachrome tautomerase/tyrosinase-related protein-2 and
49 of eumelanin by catalyzing the conversion of dopachrome to 5,5-dihydroxyindole-2-carboxylic acid (DHI
50 ome, a stereoisomer of naturally occurring L-dopachrome, to 5,6-dihydroxyindole-2-carboxylic acid.
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