Results 51 to 60 of about 170,695 (197)
Resistance to the tyrosine kinase inhibitor Sorafenib, which is the standard treatment for advanced hepatocellular carcinoma, is a major clinical challenge.
Lai Wei +11 more
doaj +1 more source
The phosphorylated pathway of serine biosynthesis represents an important pathway in plants. The pathway consist of three reactions catalyzed by the phosphoglycerate dehydrogenase, the phosphoserine aminotransferase and the phosphoserine phosphatase, and
Sabine Wulfert, Stephan Krueger
doaj +1 more source
Phosphoglycerate dehydrogenase diverts glycolytic flux and contributes to oncogenesis [PDF]
Most tumors exhibit increased glucose metabolism to lactate, however, the extent to which glucose-derived metabolic fluxes are used for alternative processes is poorly understood. Using a metabolomics approach with isotope labeling, we found that in some cancer cells a relatively large amount of glycolytic carbon is diverted into serine and glycine ...
Locasale, Jason W. +25 more
openaire +4 more sources
Proteomics analysis of antimalarial targets of Garcinia mangostana Linn.
Objective: To investigate possible protein targets for antimalarial activity of Garcinia mangostana Linn. (G. mangostana) (pericarp) in 3D7 Plasmodium falciparum clone using 2-dimensional electrophoresis and liquid chromatography mass-spectrometry (LC/MS/
Wanna Chaijaroenkul +4 more
doaj +1 more source
Inhibition of 3-phosphoglycerate dehydrogenase by
1. l-Serine was shown to be a highly specific inhibitor of 3-phosphoglycerate dehydrogenase. 2. 3-Phosphoglycerate dehydrogenase is cold-labile with respect to its catalytic activity and to sensitivity to serine. 3. l-Serine protects the catalytic site as well as the inhibitor site. 4. Glycerol protects the catalytic site as well as the inhibitor site.
J C, Slaughter, D D, Davies
openaire +2 more sources
The malate-aspartate shuttle is important for de novo serine biosynthesis
Summary: The malate-aspartate shuttle (MAS) is a redox shuttle that transports reducing equivalents across the inner mitochondrial membrane while recycling cytosolic NADH to NAD+.
Melissa H. Broeks +11 more
doaj +1 more source
Probing Subunit Interactions in 3‐Phosphoglycerate Dehydrogenase
3‐Phosphoglycerate Dehydrogenase is a homotetramer with three types of subunit interfaces; between adjacent regulatory domains, cofactor domains, and across the central cavity of the tetramer. A single tryptophan per subunit lies at the cofactor interface and crosses over between adjacent subunits.
Falk, Bradley, Bell, Ellis
openaire +1 more source
The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas [PDF]
1. 3-Phosphoglycerate dehydrogenase was purified 400-fold from crude extracts of etiolated pea epicotyls. 2. Michaelis constants were determined for all four substrates. 3. Loss of sensitivity to inhibition by l-serine occurs on purification. 4. The purified enzyme is inhibited by thiol-group reagents and, with N-ethyl-maleimide, protection is afforded
J C, Slaughter, D D, Davies
openaire +2 more sources
Glycerol dehydrogenase: Structure, specificity, and mechanism of a family III polyol dehydrogenase [PDF]
Background: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD+ to NADH.
Baker PJ +26 more
core +1 more source
The present study was performed to unravel the mechanisms of systemic acquired resistance (SAR) establishment and resistance signaling pathways against the canker-rot fungus (Inonotus obliquus strain IO-U1) infection in Japanese birch plantlet No.8 ...
Hiromu Suzuki +4 more
doaj +1 more source

