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

Trapping a cross-linked lysine–tryptophan radical in the catalytic cycle of the radical SAM enzyme SuiB

Proceedings of the National Academy of Sciences(2021)10.1073/pnas.2101571118Source: DataRank Database

Trapping a cross-linked lysine–tryptophan radical in the catalytic cycle of the radical SAM enzyme SuiB is a research paper published in Proceedings of the National Academy of Sciences (2021). On theSindex it has a DataRank of 0. It has been cited 46 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access46 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 (4 grants)Impact (FWCI 1.75)OA: bronzeTopics (105)IDs (PubMed, OpenAlex)SDGs (1)

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 (6)

Alessio Caruso ORCID,Lizhi Tao ORCID,Dean J. Tantillo ORCID,Mohammad R. Seyedsayamdost ORCID,R. David Britt ORCID

Live enrichment

PubMed:34001621 OpenAlex:https://openalex.org/W3160089421

HHS | National Institutes of Health

Grant: 1R35GM126961-01

Spectroscopy Investigations of Metalloenzyme Mechanisms

National Science Foundation

Grant: 1847932

CAREER: New Metalloenzyme-Catalyzed Transformations in Natural Product Biosynthesis

National Science Foundation

Grant: CHE-030089

Natural Sciences and Engineering Research Council of Canada

Grant: unidentified

unidentified

FWCI

1.75

Citation Percentile

0.8%

Citation Trend

2021

2022

2023

2024

2025

2026

bronzeLicense: https://www.pnas.org/site/aboutpnas/licenses.xhtml

journalhttps://www.pnas.org/content/pnas/118/21/e2101571118.full.pdf

publisherhttps://www.pnas.org/content/pnas/118/21/e2101571118.full.pdf

publisherhttp://www.pnas.org/syndication/doi/10.1073/pnas.2101571118

publisherhttps://pnas.org/doi/pdf/10.1073/pnas.2101571118

journalhttps://doi.org/10.1073/pnas.2101571118

Fields of Study

Metalloenzymes and iron-sulfur proteinsCO2 Reduction Techniques and CatalystsMetal-Catalyzed Oxygenation Mechanisms0301 basic medicine01 natural sciences03 medical and health sciences0104 chemical sciences

MeSH Terms

Protein Conformation, alpha-HelicalProtein Conformation, beta-StrandBacterial ProteinsBinding SitesCatalysisCloning, MolecularElectron Spin Resonance SpectroscopyEscherichia coliGenetic VectorsIron-Sulfur ProteinsKineticsLysineModels, MolecularOxidation-ReductionProtein BindingRecombinant ProteinsRibosomal ProteinsS-AdenosylmethionineStreptococcusSubstrate SpecificityThermodynamicsTryptophanGene ExpressionProtein Interaction Domains and Motifs

Keywords

ChemistryElectron paramagnetic resonanceRedoxCatalysisStereochemistryTryptophanCatalytic cycleLysineElectrophilePhotochemistryCombinatorial chemistryAmino acidOrganic chemistryBiochemistryIron-Sulfur ProteinsModels, MolecularProtein Conformation, alpha-HelicalS-AdenosylmethionineBacterial Proteins (mesh)Protein ConformationGene ExpressionGene Expression (mesh)Substrate Specificitybioinorganic chemistryModels3402 Inorganic Chemistry (for-2020)Protein Binding (mesh)Cloning, MolecularLysine (mesh)Iron-Sulfur Proteins (mesh)S-Adenosylmethionine (mesh)Protein Interaction Domains and Motifs (mesh)Recombinant ProteinsMolecular (mesh)Substrate Specificity (mesh)ThermodynamicsKinetics (mesh)Oxidation-ReductionEPR spectroscopyProtein BindingStreptococcus (mesh)Thermodynamics (mesh)Ribosomal ProteinsRibosomal Proteins (mesh)enzymologyGenetic Vectors34 Chemical Sciences (for-2020)chemical biologyBinding Sites (mesh)Oxidation-Reduction (mesh)Electron Spin Resonance Spectroscopy (mesh)Inorganic Chemistrybeta-Strand (mesh)Bacterial ProteinsRecombinant Proteins (mesh)Escherichia coliProtein Interaction Domains and MotifsCatalysis (mesh)alpha-Helical (mesh)Binding Sitesalpha-HelicalTryptophan (mesh)Electron Spin Resonance SpectroscopyMolecularStreptococcus500Genetic Vectors (mesh)540KineticsChemical Sciencesbeta-StrandEscherichia coli (mesh)Protein Conformation, beta-StrandCloning

Sustainable Development Goals

SDG 0: Clean water and sanitation