The Meloidogyne incognita Nuclear Effector MiEFF1 Interacts With Arabidopsis Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenases to Promote Parasitism [PDF]
Frontiers in Plant Science, 2021 Root-knot nematodes are obligate endoparasites that maintain a biotrophic relationship with their hosts over a period of several weeks. They induce the differentiation of root cells into specialized multinucleate hypertrophied feeding cells known as ...
Nhat My Truong +12 more
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The Role of Glyceraldehyde-3-Phosphate Dehydrogenases in NADPH Supply in the Oleaginous Filamentous Fungus Mortierella alpina [PDF]
Frontiers in Microbiology, 2020 Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a highly conserved enzyme within the glycolytic pathway. GAPDH catalyzes the transformation of glyceraldehyde 3-phosphate to glycerate-1, 3-biphosphate, a process accompanied by the production of NADH ...
Shunxian Wang +20 more
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Coat protein of rice stripe virus enhances autophagy activity through interaction with cytosolic glyceraldehyde-3-phosphate dehydrogenases, a negative regulator of plant autophagy [PDF]
Stress Biology, 2023 Viral infection commonly induces autophagy, leading to antiviral responses or conversely, promoting viral infection or replication. In this study, using the experimental plant Nicotiana benthamiana, we demonstrated that the rice stripe virus (RSV) coat ...
Wanying Zhao +8 more
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Functional divergence and convergent evolution in the plastid-targeted glyceraldehyde-3-phosphate dehydrogenases of diverse eukaryotic algae. [PDF]
PLoS ONE, 2013 Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme of the glycolytic pathway, reversibly catalyzing the sixth step of glycolysis and concurrently reducing the coenzyme NAD(+) to NADH.
Daniel Gaston, Andrew J Roger
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Genome-wide identification of GAPDH gene family and functional analysis of CaGAPC2-mediated autophagy during BWYV infection in pepper [PDF]
BMC GenomicsBackground Glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) are glycolytic enzymes involved in plant metabolism, growth, signal transduction and stress responses.
Wenqing Yang +7 more
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Glyceraldehyde-3-phosphate dehydrogenase [PDF]
Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1981 Conflicting experimental evidence of the pathway of catalysis for the enzyme from rabbit, pig and lobster muscle tissues is reviewed. Transient kinetic studies with the enzyme from rabbit muscle are presented. The results are shown to be consistent with the double-displacement mechanism of catalysis originally proposed by Segal & Boyer
K, Dalziel, N V, McFerran, A J, Wonacott
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Redox Biology, 2021 The bacterial cytosol is generally a reducing environment with protein cysteine residues maintained in their thiol form. The low molecular weight thiol bacillithiol (BSH) serves as a general thiol reductant, analogous to glutathione, in a wide range of ...
Ahmed Gaballa +2 more
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Multi-level kinetic model explaining diverse roles of isozymes in prokaryotes. [PDF]
PLoS ONE, 2014 Current standard methods for kinetic and genomic modeling cannot provide deep insight into metabolic regulation. Here, we developed and evaluated a multi-scale kinetic modeling approach applicable to any prokaryote. Specifically, we highlight the primary
Jiri Jablonsky +2 more
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Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis
Molecules, 2021 Lactobacillus sp. have long been studied for their great potential in probiotic applications. Recently, proteomics analysis has become a useful tool for studies on potential lactobacilli probiotics.
Bernadette B. Bagon +4 more
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Glyceraldehyde‐3‐phosphate activates auto‐ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase [PDF]
FEBS Letters, 1993 Nitric oxide was recently demonstrated to stimulate ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH). Our studies on the effect of glyceraldehyde‐3‐phosphate (GA3P), the natural substrate of dehydrogenase activity of GAPDH, indicated GA3P to be another very potent activator of ADP‐ribosylation of the enzyme.
Kots, Alexander Ya. +3 more
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