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1 ave been prepared as potential inhibitors of IMP dehydrogenase.
2 the most potent cofactor type inhibitors of IMP dehydrogenase.
3 nthosine 5'-monophosphate (XMP) catalyzed by IMP dehydrogenase.
4 d as inhibitors of the two isoforms of human IMP-dehydrogenase.
8 nery render yeast sensitive to inhibitors of IMP dehydrogenase and defective in inducing transcriptio
13 osyltransferase (DRTase, encoded by bb0426), IMP dehydrogenase (GuaB) and GMP synthase (GuaA) catalys
14 o key enzymes in purine salvage pathways are IMP dehydrogenase (GuaB) and GMP synthase (GuaA), encode
16 n cells unable to convert IMP to XMP or AMP (IMP dehydrogenase, guaB; adenylosuccinate synthetase, pu
17 ve-site sequence of At IMPDH conforms to the IMP dehydrogenase/guanosine monophosphate reductase moti
18 e conformation of IMP bound to human type II IMP dehydrogenase has been determined by two-dimensional
19 of ribavirin, suggesting that inhibition of IMP dehydrogenase (IMPDH) and reduction of intracellular
35 Mycophenolic acid (MPA), an inhibitor of IMP-dehydrogenase (IMPDH), is used worldwide in transpla
37 stemin protein degradation in tumor cells by IMP dehydrogenase inhibition or by other small molecules
38 ld temperature, nutrient limitation, and the IMP dehydrogenase inhibitor mycophenolic acid (MPA).
39 tive secretory vacuoles, we hypothesize that IMP dehydrogenase inhibitors induce androgen-independent
41 itor of the de novo purine synthetic enzyme, IMP dehydrogenase, leads to the rapid disappearance of n
43 ds with extensive sequence similarity to the IMP dehydrogenases of Saccharomyces cerevisiae and vario
45 phenolic acid (MPA), a specific inhibitor of IMP dehydrogenases, per ml, whereas transformants hostin
46 ar motor switch protein and the guaB-encoded IMP dehydrogenase) were noninfectious, whereas four clon
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