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1 thesis as an l-threonine:uridine-5'-aldehyde transaldolase.
2 ate, changing the chemistry from aldolase to transaldolase.
3 atients with predetermined autoreactivity to transaldolase.
4 s further gene clusters encoding L-threonine transaldolases.
5 e moiety was scrambled via transketolase and transaldolase activities of the pentose phosphate pathwa
7 m (Glyceraldehyde 3-phosphate dehydrogenase, transaldolase, alcohol dehydrogenase, and phosphoenolpyr
11 one structure of the mechanistically similar transaldolase and KDPG aldolase allows the identificatio
12 e in basal and tissue-specific expression of transaldolase and regulation of the metabolic network co
13 an be used to calculate the three individual transaldolase and transketolase extents of reversibility
14 in kinases; (2) metabolic enzymes, including transaldolase and transketolase of the nonoxidative pent
15 fructose-1,6-(bis)phosphate (FBP) aldolase, transaldolase, and 2-keto-3-deoxy-6-phosphogluconate ald
16 ls the importance of glutathione peroxidase, transaldolase, and the concentration of total glutathion
17 of the human transaldolase gene, thus termed transaldolase-associated repetitive elements, TARE, were
20 enase, 6-phosphogluconate dehydrogenase, and transaldolase, elevated intracellular glutathione levels
22 acterium leprae, similarity to the conserved transaldolase enzymes from humans, E. coli and Saccharom
23 tibodies binding to the most prominent human transaldolase epitope, between residues 271 and 285, sho
25 C5-to-C3 glucose ratio is <1 indicates that transaldolase exchange, selective retention of deuterium
27 Nase I footprinting with nuclear extracts of transaldolase-expressing cell lines unveiled protection
30 cifically isocitrate lyase, malate synthase, transaldolase, fructose bisphosphatase and phosphoenolpy
31 otide biosynthesis, and the PPP, including a transaldolase gene that is the most prevalent PPP gene i
32 ements flanked by exons 2 and 3 of the human transaldolase gene, thus termed transaldolase-associated
38 preliminary data suggesting that L-threonine transaldolases might be useful for the preparation of L-
40 om various potato tissues indicated that the transaldolase mRNA accumulation to higher levels in the
42 of ZNF143 enhanced, maintained, or abolished transaldolase promoter activity, respectively, in HepG2
45 ration by triose phosphate isomerase, or the transaldolase reaction all interact to produce complex (
47 the M. jannaschii MJ0400 gene catalyzes the transaldolase reaction and the protein product of the MJ
48 th unlabeled three-carbon precursors via the transaldolase reaction and/or selective retention of the
49 es a "hydroxyacetone" fragment, which, via a transaldolase reaction, undergoes an aldol condensation
51 t the reversibility of the transketolase and transaldolase reactions in the nonoxidative pathway.
52 4, raised against enzymatically active human transaldolase, recognized antigenic determinants corresp
54 and an L-threonine:4-nitrophenylacetaldehyde transaldolase responsible for (2S,3R)-2-amino-3-hydroxy-
57 also encodes fructose bisphosphatase (fbp), transaldolase (tal) and a gene product termed OpcA, whic
58 e responses to oligodendroglial autoantigens transaldolase (TAL) and myelin basic protein (MBP) were
59 ate the evolution of the land plant TAL-type transaldolase (TAL) gene and its potential function in r
65 ntose phosphate pathway (PPP), the effect of transaldolase (TAL), a key enzyme of PPP, was investigat
66 hate pathway (PPP), we studied the impact of transaldolase (TAL), a key enzyme of the PPP, on Fas sig
67 n the pentose phosphate pathway (PPP) enzyme transaldolase (TAL; encoded by TALDO1) and liver failure
68 ogue to the pentose phosphate pathway enzyme transaldolase (TAL1), and the transcription factor vitam
69 (psbA), high-light inducible protein (hli), transaldolase (talC) and ribonucleotide reductase (nrd)-
70 h of the pentose phosphate pathway involving transaldolase that places this (13)C-enriched 3-carbon u
71 ite reductase, and metabolic enzymes such as transaldolase, transketolase, malate dehydrogenase, aspa
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