ArticleParasitology research2007
Molecular cloning and characterization of a phosphoglycerate mutase gene from Clonorchis sinensis.
Article in Parasitology research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Liver Flukes: Clonorchis and Opisthorchis.Advances in experimental medicine and biology · 2024Review
- Schistosoma mansoni phosphoglycerate mutase: a glycolytic ectoenzyme with thrombolytic potential.Parasite (Paris, France) · 2022Article
- Molecular cloning and characterization of a novel ras-related protein (rap2) from Clonorchis sinensis.Parasitology research · 2011Article
- Cloning, characterization, and expression of a novel secretory lipase-like gene from Clonorchis sinensis.Parasitology research · 2009Article
- Functional genes and proteins of Clonorchis sinensis.The Korean journal of parasitology · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoglycerate mutase (PGM) is a widely distributed glycolytic enzyme. Two known distinct classes of PGM enzymes were identified, a cofactor-dependent one (dPGM) and a cofactor-independent one (iPGM). A complementary DNA (cDNA) encoding a PGM was cloned from a Clonorchis sinensis cDNA library by large-scale sequencing. This new cDNA contains 955 bp with a putative open reading frame of 256 amino acids, which has a high homology with dPGMs from a number of species. The putative peptide was produced in E. coli and was purified to electrophoretic homogeneity. Enzymatic assays showed that the product of this gene could catalyze the conversion of 3-phosphoglycerate to 2-phosphoglycerate when the cofactor was present and the enzyme activities could be inhibited by vanadate.
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Registered trials
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