ArticleActa crystallographica. Section F, Structural biology communications2020
Characterization and structure of glyceraldehyde-3-phosphate dehydrogenase type 1 from Escherichia coli.
Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Exploring the Molecular Mechanism of Cinnamaldehyde Intervening in Ochratoxin A-Induced Type 2 Diabetes Mellitus and Non-Alcoholic Fatty Liver Disease Comorbidity: An Integrated Approach Based on Network Pharmacology, Network Toxicology and Molecular Docking.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Optimization of Fermentation and Transcriptomic Analysis of a High-Protein-ProducingFoods (Basel, Switzerland) · 2026Article
- Molecular Insights Into the Interaction of Tryptophan Metabolites With Tryptophan and Indoleamine 2,3-Dioxygenases: Nitric Oxide a New Effector of Tryptophan 2,3-Dioxygenase and Their Roles in Infection.International journal of tryptophan research : IJTR · 2025Article
- Biological Function of Prophage-Related Gene Cluster ΔInternational journal of molecular sciences · 2024Article
- Self assembling nanoparticle enzyme clusters provide access to substrate channeling in multienzymatic cascades.Nature communications · 2023Article
- Novel Structures of Type 1 Glyceraldehyde-3-phosphate Dehydrogenase fromBiomolecules · 2021Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Here, the full-length GAPDH type 1 from Escherichia coli (EcGAPDH1) was cloned and overexpressed, and the protein was purified. Biochemical analyses found that the optimum reaction temperature and pH of EcGAPDH1 were 55°C and 10.0, respectively. The protein has a certain amount of thermostability. Crystals of EcGAPDH1 were obtained using the sitting-drop vapor-diffusion technique and X-ray diffraction data were collected to 1.88 Å resolution. Characterization of the crystals showed that they belonged to space group P4
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