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1 ase (PMK) from S. pneumoniae in complex with phosphomevalonate and AMPPNP.Mg(2+).
2  = 12 microm, where pmev and ppmev represent phosphomevalonate and diphosphomevalonate, respectively.
3 e superfamily (galacto-homoserine-mevalonate-phosphomevalonate), but duplication to form a compact do
4                                 This enzyme, phosphomevalonate decarboxylase (PMD), exhibits strong i
5 tal demonstration in H. volcanii of both the phosphomevalonate decarboxylase and isopentenyl phosphat
6                             The inhibitor of phosphomevalonate decarboxylase, sodium phenylacetate, a
7 t identification and characterization of any phosphomevalonate decarboxylase.
8 e, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase (GHMP) family were compared to
9 erine kinase (H), mevalonate kinase (M), and phosphomevalonate kinase (P).
10                                              Phosphomevalonate kinase (PMK) catalyzes a key step in i
11                                              Phosphomevalonate kinase (PMK) catalyzes phosphoryl tran
12                                              Phosphomevalonate kinase (PMK) catalyzes the cation-depe
13 ve determined the 1.9 A crystal structure of phosphomevalonate kinase (PMK) from S. pneumoniae in com
14 o overlapping cDNAs which encode human liver phosphomevalonate kinase (PMKase) were isolated.
15    The MJ0044-derived protein was tested for phosphomevalonate kinase activity and was found not to c
16 also demonstrate structure-linked latency of phosphomevalonate kinase and mevalonate diphosphate deca
17 actokinase superfamily, between the metazoan phosphomevalonate kinase and the nucleoside monophosphat
18 sidues corresponding to Ser291 and Ala293 in phosphomevalonate kinase are linked to mevalonic acid de
19                                              Phosphomevalonate kinase catalyzes an essential step in
20 verse class of metabolites, the mechanism of phosphomevalonate kinase from any organism is not yet we
21                     The first structure of a phosphomevalonate kinase from Streptococcus pneumoniae w
22 esentative member of the GHMP kinase family, phosphomevalonate kinase from Streptococcus pneumoniae.
23 ense variation c.412C > T (p.Arg138*) in the phosphomevalonate kinase gene (PMVK), which encodes a cy
24 okinase/homoserine kinase/ mevalonate kinase/phosphomevalonate kinase protein family.
25 e, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase) family members, 14 PduX varian
26 ee members of the family (mevalonate kinase, phosphomevalonate kinase, and diphosphomevalonate decarb
27 hosphate from mevalonate (mevalonate kinase, phosphomevalonate kinase, and MDD) share the same fold,
28 thase, HMG-CoA reductase, mevalonate kinase, phosphomevalonate kinase, and mevalonate diphosphate dec
29 ow that the activities of mevalonate kinase, phosphomevalonate kinase, and mevalonate diphosphate dec
30  between mevalonate kinase and FPP synthase (phosphomevalonate kinase, mevalonate diphosphate decarbo
31 e, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase, with homologues in plants and
32 rchaea and was predicted to be the "missing" phosphomevalonate kinase.
33 active Mev.pp forms by the endogenous MK and phosphomevalonate kinase.
34      The galacto-, homoserine-, mevalonate-, phosphomevalonate-kinase (GHMP) superfamily encompases a
35 fy genes for the enzymes required to convert phosphomevalonate (PM) to IPP in eukaryotes.
36 east proteins, accounting for the route from phosphomevalonate to geranyl pyrophosphate, are missing,

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