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A synergy of activity, stability, and inhibitor‐interaction of HIV‐1 protease mutants evolved under drug‐pressure

Protein Science(2020)10.1002/pro.4013Source: DataRank Database

A synergy of activity, stability, and inhibitor‐interaction of HIV‐1 protease mutants evolved under drug‐pressure is a research paper published in Protein Science (2020). On theSindex it has a DataRank of 0. It has been cited 1 time.

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0DataRank · unranked

Scored on demand from live citation data

Open Access1 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 0.02)OA: bronzeTopics (40)IDs (PubMed, PMC, OpenAlex)Annotations (1)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 (6)

John D. Persons ORCID,Michel Guerrero,Tatiana V. Ilina ORCID,Masayuki Oda ORCID,Rieko Ishima ORCID

Live enrichment

PubMed:33314454 PMC:PMC7888579 OpenAlex:https://openalex.org/W3110655035

National Institute of General Medical Sciences

Grant: GM135919

National Institute of General Medical Sciences

Grant: GM109767

National Institutes of Health

Grant: S10OD023481

NIGMS NIH HHS

Grant: P01 GM109767

NIGMS NIH HHS

Grant: R01 GM135919

FWCI

0.02

Citation Percentile

0.4%

Citation Trend

2020

bronzeLicense: http://onlinelibrary.wiley.com/termsAndConditions#vor

journalhttps://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/pro.4013

publisherhttps://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/pro.4013

publisherhttps://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4013

publisherhttps://onlinelibrary.wiley.com/doi/full-xml/10.1002/pro.4013

journalhttps://doi.org/10.1002/pro.4013

Fields of Study

HIV/AIDS drug development and treatmentHIV Research and TreatmentAdvanced biosensing and bioanalysis techniquesCalorimetryDrug Resistance, ViralHIV ProteaseHIV Protease InhibitorsModels, MolecularMutationNuclear Magnetic Resonance, BiomolecularPepstatinsProtein BindingThermodynamics

MeSH Terms

CalorimetryModels, MolecularMutationPepstatinsProtein BindingThermodynamicsHIV ProteaseHIV Protease InhibitorsNuclear Magnetic Resonance, BiomolecularDrug Resistance, Viral

Keywords

Isothermal titration calorimetryMutantHIV-1 proteaseChemistryProteaseStereochemistryResidue (chemistry)BiophysicsEnzymeBiochemistryBiologyGeneHIV-1InhibitorNMRCalorimetrythermodynamics

Sustainable Development Goals

SDG 0: Good health and well-being