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1 s central carbon metabolism by inhibition of triose-phosphate isomerase.
2 dehyde-3-phosphate dehydrogenase (GAPDH) and triose-phosphate isomerase.
4 We have predicted mutations that introduce triose phosphate isomerase activity into ribose-binding
5 , we showed that it is possible to introduce triose phosphate isomerase activity into the ribose-bind
6 und that TpiA2 and RpiB, distant homologs of triose phosphate isomerase and ribose 5-phosphate isomer
8 y inhibiting the Calvin-Benson cycle enzymes triose-phosphate isomerase and sedoheptulose 1,7-bisphos
9 A, glyceraldehyde 3-phosphate dehydrogenase, triose phosphate isomerase, and enolase 1, are targeted
11 phosphate dehydrogenase (G3PDH), annexin A2, triose phosphate isomerase, and ubiquitin B precursor.
12 s involved in triose phosphate reduction and triose phosphate isomerase are primarily located in the
13 re of YKL-39 comprises a major (beta/alpha)8 triose-phosphate isomerase barrel domain and a small alp
16 m Clostridium perfringens reveals a modified triose-phosphate isomerase (beta/alpha)8 barrel in which
17 olase reaction and incomplete equilibrium by triose phosphate isomerase cannot break a (13)C-(13)C bo
18 her targets, whereas a single AS ODN against triose-phosphate isomerase did not differ significantly
19 ition of His-6 to another expressed protein (triose phosphate isomerase) did not result in stimulatio
21 minoaspartate and (ii) the DHAP analogue and triose-phosphate isomerase inhibitor phosphoglycolohydro
24 taalpha) barrel structure, first observed in triose-phosphate isomerase, occurs ubiquitously in natur
25 le or the PPP but not an influence of either triose phosphate isomerase or the transaldolase reaction
26 tric acid cycle, incomplete equilibration by triose phosphate isomerase, or the transaldolase reactio
28 omerase, heat shock protein 27, cathepsin D, triose-phosphate isomerase, peroxiredoxin 6, and electro
30 stem, the gene encoding the metabolic enzyme triose phosphate isomerase (tim) was sequenced from a nu
31 architectural elements: a Rossman fold and a triose phosphate isomerase (TIM)-barrel domain for bindi
34 c glucoside hydrolase 1 family (alpha/beta)8 triose-phosphate isomerase (TIM) barrel structure with a
35 -fold dimer in head-to-tail arrangement of a triose-phosphate isomerase (TIM) barrel-like alpha/beta
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