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Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies

Structure(2021)10.1016/j.str.2021.05.014Source: DataRank Database

Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies is a research paper published in Structure (2021). On theSindex it has a DataRank of 0. It has been cited 61 times.

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0DataRank · unranked

Scored on demand from live citation data

Open Access61 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (5 grants)Impact (FWCI 3.53)OA: bronzeTopics (66)IDs (PubMed, PMC, OpenAlex)Annotations (4)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)

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Authors (14)

Micah Rapp ORCID,Yicheng Guo ORCID,Fabiana Bahna,Jude Bimela,Eswar R. Reddem ORCID

Live enrichment

PubMed:34111408 PMC:PMC8188728 OpenAlex:https://openalex.org/W3166510353

NIH HHS

Grant: DP5 OD023118

NIAID NIH HHS

Grant: R21 AI143407

NIAID NIH HHS

Grant: R21 AI144408

NIGMS NIH HHS

Grant: T32 GM008224

NIGMS NIH HHS

Grant: U24 GM129539

FWCI

3.53

Citation Percentile

0.9%

Citation Trend

2021

2022

2023

2024

2025

2026

bronzeLicense: http://www.elsevier.com/open-access/userlicense/1.0/

journalhttp://www.cell.com/article/S0969212621001726/pdf

publisherhttp://www.cell.com/article/S0969212621001726/pdf

publisherhttps://api.elsevier.com/content/article/PII:S0969212621001726?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0969212621001726?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.str.2021.05.014

Fields of Study

SARS-CoV-2 and COVID-19 ResearchSARS-CoV-2 detection and testingBacillus and Francisella bacterial researchAngiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralBinding SitesCloning, MolecularCryoelectron MicroscopyEpitopesGene ExpressionHEK293 CellsHumansModels, MolecularMutationProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsReceptors, VirusRecombinant ProteinsSARS-CoV-2Spike Glycoprotein, Coronavirus

MeSH Terms

Protein Conformation, alpha-HelicalProtein Conformation, beta-StrandAngiotensin-Converting Enzyme 2SARS-CoV-2Antibodies, MonoclonalAntibodies, ViralEpitopesBinding SitesCloning, MolecularHumansModels, MolecularMutationProtein BindingReceptors, VirusRecombinant ProteinsGene ExpressionCryoelectron MicroscopyProtein Interaction Domains and MotifsAntibodies, NeutralizingHEK293 CellsSpike Glycoprotein, Coronavirus

Keywords

NeutralizationEpitopeAntibodyMonoclonal antibodyVirologyNeutralizing antibodySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)BiologyImmune escapeImmune systemCoronavirus disease 2019 (COVID-19)ImmunologyMedicineInfectious disease (medical specialty)DiseaseReceptor-binding domainCryo-emCovid-19Sars-cov-2B.1.351 And B.1.1.7 VariantsLow-frequency Immune Response

Sustainable Development Goals

SDG 0: Good health and well-being

Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies

FAIR Checklist

Authors (14)

Funding (5 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)