2019
The Polar Region of the HIV-1 Envelope Protein Determines Viral Fusion and Infectivity by Stabilizing the gp120-gp41 Association
Lu W, Chen S, Yu J, Behrens R, Wiggins J, Sherer N, Liu S, Xiong Y, Xiang S, Wu L. The Polar Region of the HIV-1 Envelope Protein Determines Viral Fusion and Infectivity by Stabilizing the gp120-gp41 Association. Journal Of Virology 2019, 93: 10.1128/jvi.02128-18. PMID: 30651369, PMCID: PMC6430531, DOI: 10.1128/jvi.02128-18.Peer-Reviewed Original ResearchConceptsHIV-1 fusionHIV-1 infectivityPR mutationsHIV-1 membrane fusionViral entryHIV-1 Env precursorEnv trimersMembrane fusionHIV-1 envelope proteinHIV-1 isolatesViral fusionHIV-1 Env trimersHIV-1 EnvGp120-gp41 associationTransmembrane unitViral envelope glycoproteinsHIV-1Cell-cell fusionViral fusogenicityPolar amino acidsEnv expressionVirus bindingEnvelope glycoproteinFusion inhibitorsTarget cells
2014
Predicting the side‐chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models
Zhou AQ, O'Hern CS, Regan L. Predicting the side‐chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models. Proteins Structure Function And Bioinformatics 2014, 82: 2574-2584. PMID: 24912976, DOI: 10.1002/prot.24621.Peer-Reviewed Original Research
2013
Insights on the Facet Specific Adsorption of Amino Acids and Peptides toward Platinum
Ramakrishnan SK, Martin M, Cloitre T, Firlej L, Cuisinier F, Gergely C. Insights on the Facet Specific Adsorption of Amino Acids and Peptides toward Platinum. Journal Of Chemical Information And Modeling 2013, 53: 3273-3279. PMID: 24289530, DOI: 10.1021/ci400630d.Peer-Reviewed Original ResearchConceptsMolecular dynamics simulationsInorganic surfacesPt facetsSpecific adsorptionPredictable conformationsNovel nanomaterialsInorganic materialsDifferential adsorptionAdhesion peptidesMolecular architectureDynamics simulationsAdsorptionProgrammable shapesRecognition behaviorBuilding blocksAmino acidsEnhanced affinityPeptide bindingPolar amino acidsCrystallographic planesAcidPeptidesBiomoleculesBionanomaterialsNanomaterials
1985
A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
Gallione C, Rose J. A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. Journal Of Virology 1985, 54: 374-382. PMID: 2985803, PMCID: PMC254807, DOI: 10.1128/jvi.54.2.374-382.1985.Peer-Reviewed Original ResearchConceptsCDNA clonesHydrophobic domainAmino acidsCell surface transportSingle amino acid substitutionVesicular stomatitis virus glycoproteinWild-type parent strainDNA sequence analysisPolar amino acidsHydrophobic amino acidsAmino acid changesAmino acid substitutionsProtein transportDNA sequencesNonpermissive temperatureVesicular stomatitis virusCOS cellsNonconservative substitutionsSequence analysisSpontaneous revertantsAcid substitutionsAcid changesSingle substitutionTransport defectStomatitis virus
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