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Switching an active site helix in dihydrofolate reductase reveals limits to subdomain modularity

Biophysical Journal(2021)10.1016/j.bpj.2021.09.032Source: DataRank Database

Switching an active site helix in dihydrofolate reductase reveals limits to subdomain modularity is a research paper published in Biophysical Journal (2021). On theSindex it has a DataRank of 0. It has been cited 2 times.

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Open Access2 citations

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (8 grants)Impact (FWCI 0.07)OA: greenTopics (31)IDs (PubMed, PMC, OpenAlex)Annotations (2)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (5)

João V. Rodrigues ORCID,Elena R. Lozovsky,Daniel L. Hartl ORCID,Eugene I. Shakhnovich ORCID,Victor Y. Zhao ORCID

Live enrichment

PubMed:34571014 PMC:PMC8595743 OpenAlex:https://openalex.org/W3203343719

National Science Foundation

Grant: ACI-1548562 ( 82

National Science Foundation

Grant: DGE1745303

National Institutes of Health

Grant: R35GM139571

Harvard University

Grant: BIO200028

NIGMS NIH HHS

Grant: R01 GM068670

National Science Foundation

Grant: 1745303

Graduate Research Fellowship Program (GRFP)

National Institutes of Health

Grant: 5R35GM139571-02

Biophysical foundations of evolutionary dynamics

National Institute of General Medical Sciences

FWCI

0.07

Citation Percentile

0.4%

Citation Trend

2022

2026

greenLicense: CC BY

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/8595743

publisherhttps://api.elsevier.com/content/article/PII:S0006349521007943?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0006349521007943?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.bpj.2021.09.032

Fields of Study

RNA and protein synthesis mechanismsGenomics and Phylogenetic StudiesProtein Structure and Dynamics0301 basic medicine0303 health sciences03 medical and health sciencesCatalytic DomainEscherichia coliKineticsProtein ConformationTetrahydrofolate Dehydrogenase

MeSH Terms

Escherichia coliKineticsProtein ConformationTetrahydrofolate DehydrogenaseCatalytic Domain

Keywords

Dihydrofolate reductaseBiologyActive siteProtein structureProtein designStereochemistryBiochemistryEnzymeBiophysicsChemistryKineticsTetrahydrofolate DehydrogenaseProtein ConformationCatalytic DomainEscherichia coli

Switching an active site helix in dihydrofolate reductase reveals limits to subdomain modularity

FAIR Checklist

Authors (5)

Funding (8 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)