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

The Shigella kinase effector OspG modulates host ubiquitin signaling to escape septin-cage entrapment

Nature Communications(2024)10.1038/s41467-024-48205-4Source: DataRank Database

The Shigella kinase effector OspG modulates host ubiquitin signaling to escape septin-cage entrapment is a research paper published in Nature Communications (2024). On theSindex it has a DataRank of 0. It has been cited 15 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access15 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 (6 grants)Impact (FWCI 2.49)OA: goldTopics (62)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 (14)

Jiaqi Fu ORCID,Qinxin Zhang ORCID,Chuang Li ORCID,Yan‐Bo Zhao ORCID,Zhiheng Tang ORCID

Live enrichment

PubMed:38719850 OpenAlex:https://openalex.org/W4396748140

National Natural Science Foundation of China

Grant: 22174003

National Natural Science Foundation of China

Grant: 21974002

Foundation for the National Institutes of Health

Grant: R01AI127465

Foundation for the National Institutes of Health

Grant: R01GM126296

National Institutes of Health

Grant: 5R01AI127465-07

Effector-mediated ubiquitin manipulation in Legionella pneumophila pathogenesis

National Institutes of Health

Grant: 5R01GM126296-06

Mechanism of atypical ubiquitination and deubiquitination by bacterial effectors

FWCI

2.49

Citation Percentile

0.9%

Citation Trend

2024

2025

2026

goldLicense: cc-by

journalhttps://doi.org/10.1038/s41467-024-48205-4

publisherhttps://doi.org/10.1038/s41467-024-48205-4

publisherhttps://www.nature.com/articles/s41467-024-48205-4.pdf

publisherhttps://www.nature.com/articles/s41467-024-48205-4

repositoryhttps://pubmed.ncbi.nlm.nih.gov/38719850

Fields of Study

Ubiquitin and proteasome pathwaysGlycosylation and Glycoproteins ResearchGenomics and Phylogenetic Studies0301 basic medicine0303 health sciences03 medical and health sciencesShigella flexneriSeptinsHumansUbiquitinBacterial ProteinsSignal TransductionUbiquitinationPhosphorylationHost-Pathogen InteractionsHeLa CellsCullin ProteinsUbiquitin-Protein LigasesHEK293 CellsDysentery, Bacillary

MeSH Terms

Bacterial ProteinsDysentery, BacillaryHeLa CellsHumansPhosphorylationShigella flexneriSignal TransductionUbiquitinUbiquitin-Protein LigasesCullin ProteinsUbiquitinationHost-Pathogen InteractionsHEK293 CellsSeptins

Keywords

UbiquitinEffectorCell biologySeptinBiologyShigella flexneriUbiquitin ligaseKinasePhosphorylationCytokinesisBiochemistryGeneCellEscherichia coliScienceUbiquitin-Protein LigasesQUbiquitinationCullin ProteinsArticleHEK293 CellsBacterial ProteinsHost-Pathogen InteractionsHumansSeptinsSignal TransductionHeLa CellsDysentery, Bacillary