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Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase

Molecules(2021)10.3390/molecules26020270Source: DataRank Database

Dynamic Preference for NADP/H Cofactor Binding/Release in E. coli YqhD Oxidoreductase is a research paper published in Molecules (2021). On theSindex it has a DataRank of 0. It has been cited 10 times.

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Open Access10 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (7 grants)OA: goldTopics (55)IDs (PubMed)SDGs (1)

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Accessible (1/2)

Open Access

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Reusable (0/3)

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Authors (3)

Jonathan M. Ellis ORCID,Katie R. Mitchell‐Koch ORCID,Rajni Verma ORCID

Live enrichment

PubMed:33430436

National Institutes of Health

Grant: P20 GM103418

National Science Foundation

Grant: EPS-0903806

National Science Foundation

Grant: 0216178

MRI: Acquisition of High Performance Computer For Wichita State University

National Science Foundation

Grant: 0903806

Phase VI: Climate Change and Energy: Basic Science, Impacts, and Mitigation

National Institutes of Health

Grant: 5P20GM103418-22

Kansas IDeA Network of Biomedical Research Excellence (K-INBRE)

National Science Foundation

Grant: 0236913

Phase IV: Improvement of the Academic Research Infrastructure

NIGMS NIH HHS

Grant: T32 GM008349

goldLicense: cc-by

publisherhttps://www.mdpi.com/1420-3049/26/2/270/pdf?version=1610095545

publisherhttps://www.mdpi.com/1420-3049/26/2/270/pdf

repositoryhttps://doaj.org/article/b9d3e25dae904da88f42c4193f7a30b6

repositoryhttp://europepmc.org/pmc/articles/PMC7826944

repositoryhttps://dx.doi.org/10.3390/molecules26020270

Fields of Study

0301 basic medicine03 medical and health sciences0303 health sciencesAldehyde ReductaseBinding SitesCoenzymesEscherichia coliEscherichia coli ProteinsHydrogen BondingMolecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationNADPProtein BindingProtein Interaction Domains and MotifsStructure-Activity RelationshipSubstrate Specificity

MeSH Terms

Aldehyde ReductaseBinding SitesCoenzymesEscherichia coliEscherichia coli ProteinsHydrogen BondingMolecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationNADPProtein BindingProtein Interaction Domains and MotifsStructure-Activity RelationshipSubstrate Specificity

Keywords

570CoenzymesMolecular ConformationOrganic chemistrycofactor binding and releaseMolecular Dynamics SimulationArticleinterdomain cleft dynamicsSubstrate SpecificityStructure-Activity RelationshipQD241-441Aldehyde ReductaseEscherichia coliProtein Interaction Domains and MotifsNAD(P)H-dependent oxidoreductaseBinding SitesEscherichia coli ProteinsHydrogen Bondingmolecular dynamics simulations540Molecular Docking Simulationzinc-containing alcohol dehydrogenaseNADPProtein Binding

Sustainable Development Goals

SDG 7: 7. Clean energy