cadmium-induced stress in seedlings roots induces nitric oxide accumulation, cytosolic oxidation, activation of the GAPC1 promoter, GAPC1 protein accumulation in enzymatically inactive form, and strong relocalization of GAPC1 to the nucleus. All the effects are detected in the same zone of the root tip. In vitro, GAPC1 is inactivated by either nitric oxide donors or hydrogen peroxide, but no inhibition is directly provided by cadmium
GAPDH is a multi-functional protein that is used as a control marker for basal function, it is known to undergo cysteine oxidation under different types of cellular stress
proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
molecular evolution or metabolic engineering protocols can exploit substrate channeling of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and L-lactate dehydrogenase (LDH) for metabolic flux control by fine-tuning substrate-binding affinity for the key enzymes in the competing reaction paths
lung-stage schistosomula immunofluorescence reactivity is diminished following antiserum absorption with reconbinant glyceraldehyde 3-phosphate dehydrogenase. Discussion of glyceraldehyde 3-phosphate dehydrogenase as a candidate vaccine antigen
Gapdh can be an effective target for anti-malarial chemotherapeutics. Enzyme PfGapdh shows an extra ligand binding capacity in the vicinity of the NAD+ binding region of the active site that may offer an opportunity to design and develop novel antimalarials
the conformation of FgGAPDH in this region is similar to the human enzyme. Therefore, GAPDH may not be a suitable target for drug discovery against fascioliasis caused by Fasciola gigantica
among 256 ovarian and fallopian tube cancer specimens, GAPDH is regulated, with almost 50% of specimens having no GAPDH staining.Low GAPDH staining is associated with a low macrophage colony stimulating factor CSF-1 score
glyceraldehyde 3-phosphate dehydrogenase may be involved in the postranscriptional regulation of hepatitis B virus. Recombinant glyceraldehyde 3-phosphate dehydrogenase binds to hepatitis B virus regulatory element RNA in vitro and inhibits hepatitis B virus regulatory element function. Overexpression of glyceraldehyde 3-phosphate dehydrogenase depresses the expression of hepatitis B virus antigen
in diabetic rats, modification of GAPDH by S-(2-succinyl)cysteine is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme
in experimental autoimmune encephalomyelitis, the proportion of S-nitrosylated neurofilament proteins, NMDA receptors, alpha/beta-tubulin, beta-actin, and GAPDH is increased. Neuronal specific enolase is the major S-nitrosylated protein in acute experimental autoimmune encephalomyelitis
the Porphyromonas gingivalis client proteins tonB-dependent receptor protein RagA4, 4-hydroxybutyryl-coenzyme A dehydratase AbfD, GAPDH, NAD-dependent glutamate dehydrogenase GDH, and malate dehydrogenase MDH function as regulators in Porphyromonas gingivalis biofilm formation with oral streptococci
generation of a de novo NADPH generation pathway by altering the coenzyme specificity of native NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) to NADP, to produce additional NADPH in the glycolytic pathway. Increasing the catalytic efficiency of GAPDH towards NADP enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (60%) is achieved with the mutant showing similar preference towards both NAD and NADP. There is no significant change of flux towards the pentose phosphate pathway and the increased lysine yield is mainly attributed to the NADPH generated by the mutated GAPDH
engineering the coenzyme specificity of (GAPDH) as a promising NADPH source is of interest for the metabolic engineering of NADPH-dependent bioproduction systems, e.g. for lysine production
engineering the coenzyme specificity of (GAPDH) as a promising NADPH source is of interest for the metabolic engineering of NADPH-dependent bioproduction systems, e.g. for lysine production
engineering the coenzyme specificity of (GAPDH) as a promising NADPH source is of interest for the metabolic engineering of NADPH-dependent bioproduction systems, e.g. for lysine production
generation of a de novo NADPH generation pathway by altering the coenzyme specificity of native NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) to NADP, to produce additional NADPH in the glycolytic pathway. Increasing the catalytic efficiency of GAPDH towards NADP enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (60%) is achieved with the mutant showing similar preference towards both NAD and NADP. There is no significant change of flux towards the pentose phosphate pathway and the increased lysine yield is mainly attributed to the NADPH generated by the mutated GAPDH
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development