ArticlePeerJ2022
Investigating effect of mutation on structure and function of G6PD enzyme: a comparative molecular dynamics simulation study.
Article in PeerJ, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 7 citations in OpenAlex.
- Improving the thermostability of Pseudoalteromonas Porphyrae κ-carrageenase by rational design and MD simulation.AMB Express · 2024Article
- Molecular heterogeneity of glucose-6-phosphate dehydrogenase deficiency in neonates in Wuhan: Description of four novel variants.Frontiers in genetics · 2022Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
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Abstract
Several natural mutants of the human G6PD enzyme exist and have been reported. Because the enzymatic activities of many mutants are different from that of the wildtype, the genetic polymorphism of G6PD plays an important role in the synthesis of nucleic acids via ribulose-5-phosphate and formation of reduced NADP in response to oxidative stress. G6PD mutations leading to its deficiency result in the neonatal jaundice and acute hemolytic anemia in human. Herein, we demonstrate the molecular dynamics simulations of the wildtype G6PD and its three mutants to monitor the effect of mutations on dynamics and stability of the protein. These mutants are Chatham (A335T), Nashville (R393H), Alhambra (V394L), among which R393H and V394L lie closer to binding site of structural NADP
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