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1 c acid] and its subsequent transformation to LTA4 5-LOX is thought to receive arachidonic acid from t
3 rted by cyclooxygenases into leukotriene A4 (LTA4) and subsequently into the chemotaxin LTB4, which h
4 ximately 40% (P<0.05) to a similar extent as LTA4 ( approximately 50%, P<0.05) but was not converted
5 such as arachidonic acid or the leukotriene LTA4, are further processed by endothelial enzymes via t
7 y of S36E increased linearly with increasing LTA4 concentrations during the steady-state kinetics ana
8 ic pocket that accommodates the omega-end of LTA4, distant from the aminopeptidase active site, thus
10 sulting structural alterations indicate that LTA4 entrance into the active site is a dynamic process
11 ants in the leukotriene pathway (ALOX5AP and LTA4) have emerged as susceptibility factors for myocard
13 h enantiomers as substrates, and recombinant LTA4 hydrolase (LTA4H) converted chiral 5S(6)-epoxide-co
16 hibit proinflammatory mediator production by LTA4 hydrolase and to block arachidonate conversion by h
18 ts of Pro-Gly-Pro, it could be inferred that LTA4 hydrolase cleaves at the N terminus of the palindro
21 Here, we determined the crystal structure of LTA4 hydrolase in complex with a Pro-Gly-Pro analog at 1
23 plausible that the widespread occurrence of LTA4 hydrolase in various tissues may correspond more wi
24 g and analysis of genomic sequences of mouse LTA4 hydrolase indicated that it is a single-copy gene s
35 no apparent effect of the glucocorticoid on LTA4-hydrolase-immunoreactive protein levels or specific
39 of approximately 0.5 muM) and conversion of LTA4 into LTB4 by purified LTA4H with a Ki of 2.3 muM.
40 rts the highly unstable epoxide intermediate LTA4 into LTB4, a potent leukocyte activating agent, whi
41 Hence, ARM1 selectively blocks conversion of LTA4 into LTB4, although sparing the enzyme's anti-infla
45 n crystal structures of LTA4H complexed with LTA4, providing the structural underpinnings of the enzy
47 ential for the conversion of leukotriene A4 (LTA4) to leukotriene B4 (LTB4) and also possesses an ami
49 (LTC4) synthase catalyzes the conjugation of LTA4 with reduced GSH to form LTC4, the parent of the re
50 catalyzes the conjugation of the fatty acid LTA4 with the tripeptide GSH to produce LTC4, the parent
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