Pilot corpus: NIH-funded biomedical datasets. Any DOI can be scored on demand — network effects sharpen as coverage grows.

Ternary complexes of isopentenyl phosphate kinase from Thermococcus paralvinellae reveal molecular determinants of non‐natural substrate specificity

Proteins Structure Function and Bioinformatics(2024)10.1002/prot.26674Source: DataRank Database

Ternary complexes of isopentenyl phosphate kinase from Thermococcus paralvinellae reveal molecular determinants of non‐natural substrate specificity is a research paper published in Proteins Structure Function and Bioinformatics (2024). On theSindex it has a DataRank of 0. It has been cited 1 time.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access1 citations

Download PDF

Cite:

DataRank reads this dataset's downstream impact straight off the citation graph — no black box, no proprietary weighting. How is this computed?

›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (3 grants)Impact (FWCI 0.16)OA: greenTopics (35)IDs (PubMed, OpenAlex)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

FAIR checklist signals are shown for context only and do not affect DataRank scoring.

Run a calibrated FAIR evaluation for this paper →

We only score data papers we can read in full — never from an abstract alone.

Authors (5)

Prashant S. Mandal ORCID,Sara M. Brown,Leonard M. Thomas,Shanteri Singh ORCID,Bryce P. Johnson ORCID

Live enrichment

PubMed:38333996 OpenAlex:https://openalex.org/W4391683522

National Institute of General Medical Sciences

Grant: P20GM103640

National Science Foundation

Grant: 0922269

National Institute of General Medical Sciences

Grant: R01GM138800

FWCI

0.16

Citation Percentile

0.5%

Citation Trend

2025

greenLicense: http://onlinelibrary.wiley.com/termsAndConditions#am

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC11147733/pdf/nihms-1962246.pdf

publisherhttps://onlinelibrary.wiley.com/doi/am-pdf/10.1002/prot.26674

publisherhttps://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.26674

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/11147733

Fields of Study

Plant biochemistry and biosynthesisEnzyme Structure and FunctionMicrobial Natural Products and Biosynthesis

MeSH Terms

Protein Conformation, alpha-HelicalProtein Conformation, beta-StrandAdenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceCloning, MolecularEscherichia coliKineticsModels, MolecularProtein BindingProtein KinasesRecombinant ProteinsSubstrate SpecificityGene ExpressionCrystallography, X-RayThermococcusArchaeal ProteinsCatalytic DomainHemiterpenesProtein Interaction Domains and Motifs

Keywords

ChemistrySubstrate (aquarium)AlkylStereochemistryTernary complexActive siteEnzymeThermococcusBiochemistryBiologyArchaeaOrganic chemistry