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Structure and function of an effector domain in antiviral factors and tumor suppressors SAMD9 and SAMD9L

Proceedings of the National Academy of Sciences(2022)10.1073/pnas.2116550119Source: DataRank Database

Structure and function of an effector domain in antiviral factors and tumor suppressors SAMD9 and SAMD9L is a research paper published in Proceedings of the National Academy of Sciences (2022). On theSindex it has a DataRank of 0. It has been cited 49 times.

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0DataRank · unranked

Scored on demand from live citation data

Open Access49 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (12 grants)Impact (FWCI 3.02)OA: hybridTopics (58)IDs (PubMed, PMC, OpenAlex)Annotations (1)SDGs (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 (11)

Xiangzhi Meng ORCID,Fushun Zhang ORCID,Prabhat Kumar Pathak ORCID,Juhi Chaturvedi ORCID,Jaime Coronado ORCID

Live enrichment

PubMed:35046037 PMC:PMC8795524 OpenAlex:https://openalex.org/W4206710640

HHS | NIH | National Institute of Allergy and Infectious Diseases

Grant: AI151638

OSU | Oklahoma Agricultural Experiment Station

Grant: OKL03060

NIAID NIH HHS

Grant: R21 AI149295

NCI NIH HHS

Grant: P30 CA054174

NIAID NIH HHS

Grant: R01 AI151638

NIAID NIH HHS

Grant: R21 AI153948

NIH HHS

Grant: S10 OD021805

NCATS NIH HHS

Grant: UL1 TR002645

National Institutes of Health

Grant: 1UL1TR002645-01

Institute for Integration of Medicine & Science: A Partnership to Improve Health

National Institutes of Health

Grant: 1S10OD021805-01

High Throughput DNA Sequencer: Illumina HiSeq 3000 Sequencer

National Institutes of Health

Grant: 5P30CA054174-16

SAN ANTONIO CANCER INSTITUTE

National Institutes of Health

Grant: 1R01AI151638-01A1

Novel Translational Control Mechanisms in Host Range Restriction of Poxvirus

FWCI

3.02

Citation Percentile

0.9%

Citation Trend

2022

2023

2024

2025

2026

hybridLicense: cc-by-nc-nd

journalhttps://doi.org/10.1073/pnas.2116550119

publisherhttps://doi.org/10.1073/pnas.2116550119

publisherhttp://www.pnas.org/syndication/doi/10.1073/pnas.2116550119

publisherhttps://pnas.org/doi/pdf/10.1073/pnas.2116550119

repositoryhttps://pubmed.ncbi.nlm.nih.gov/35046037

Fields of Study

interferon and immune responsesRNA Research and SplicingRNA and protein synthesis mechanisms0301 basic medicine0303 health sciences03 medical and health sciencesBinding SitesDNA-Binding ProteinsHumansIntracellular Signaling Peptides and ProteinsModels, MolecularMutationProtein BindingProtein ConformationProtein Interaction Domains and MotifsStress, PhysiologicalStructure-Activity RelationshipTumor Suppressor Proteins

MeSH Terms

Binding SitesDNA-Binding ProteinsHumansModels, MolecularMutationProtein BindingProtein ConformationStress, PhysiologicalStructure-Activity RelationshipTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsProtein Interaction Domains and Motifs

Keywords

SuppressorEffectorFunction (biology)Domain (mathematical analysis)BiologyCancer researchCell biologyCancerGeneticsMathematicsPoxvirusNODinnate immunityMyeloid MalignanciesMyelodysplasia SyndromeModels, MolecularBinding SitesProtein ConformationTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsBiological SciencesDNA-Binding ProteinsStructure-Activity RelationshipStress, PhysiologicalMutationHumansProtein Interaction Domains and MotifsProtein Binding

Sustainable Development Goals

SDG 3: 3. Good healthSDG 0: Good health and well-being