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1 cytosolic bypass around the block of stromal triose phosphate isomerase.
2 dehyde-3-phosphate dehydrogenase (GAPDH) and triose-phosphate isomerase.
3 s central carbon metabolism by inhibition of triose-phosphate isomerase.
5 We have predicted mutations that introduce triose phosphate isomerase activity into ribose-binding
6 , we showed that it is possible to introduce triose phosphate isomerase activity into the ribose-bind
8 osphoglycolate is a competitive inhibitor of triose phosphate isomerase, an enzyme in the Calvin-Bens
9 diseased mice reduced 3-nitrotyrosination of triose-phosphate isomerase, an enzyme involved in the fo
10 und that TpiA2 and RpiB, distant homologs of triose phosphate isomerase and ribose 5-phosphate isomer
11 mobile loop, analogous to those observed in triose phosphate isomerase and tryptophan synthetase.
12 y inhibiting the Calvin-Benson cycle enzymes triose-phosphate isomerase and sedoheptulose 1,7-bisphos
13 A, glyceraldehyde 3-phosphate dehydrogenase, triose phosphate isomerase, and enolase 1, are targeted
15 phosphate dehydrogenase (G3PDH), annexin A2, triose phosphate isomerase, and ubiquitin B precursor.
16 s involved in triose phosphate reduction and triose phosphate isomerase are primarily located in the
17 s, we identified the yeast glycolytic enzyme triose phosphate isomerase as being aggregation-prone in
19 re of YKL-39 comprises a major (beta/alpha)8 triose-phosphate isomerase barrel domain and a small alp
22 m Clostridium perfringens reveals a modified triose-phosphate isomerase (beta/alpha)8 barrel in which
23 olase reaction and incomplete equilibrium by triose phosphate isomerase cannot break a (13)C-(13)C bo
24 is exported to the cytosol, where cytosolic triose phosphate isomerase could convert it to dihydroxy
25 her targets, whereas a single AS ODN against triose-phosphate isomerase did not differ significantly
26 ition of His-6 to another expressed protein (triose phosphate isomerase) did not result in stimulatio
28 minoaspartate and (ii) the DHAP analogue and triose-phosphate isomerase inhibitor phosphoglycolohydro
31 taalpha) barrel structure, first observed in triose-phosphate isomerase, occurs ubiquitously in natur
32 le or the PPP but not an influence of either triose phosphate isomerase or the transaldolase reaction
33 tric acid cycle, incomplete equilibration by triose phosphate isomerase, or the transaldolase reactio
35 omerase, heat shock protein 27, cathepsin D, triose-phosphate isomerase, peroxiredoxin 6, and electro
36 ighly conserved with close similarity to the triose-phosphate isomerase protein sequence from Dermato
38 stem, the gene encoding the metabolic enzyme triose phosphate isomerase (tim) was sequenced from a nu
39 architectural elements: a Rossman fold and a triose phosphate isomerase (TIM)-barrel domain for bindi
42 c glucoside hydrolase 1 family (alpha/beta)8 triose-phosphate isomerase (TIM) barrel structure with a
43 -fold dimer in head-to-tail arrangement of a triose-phosphate isomerase (TIM) barrel-like alpha/beta