2018
Talin as a mechanosensitive signaling hub
Goult BT, Yan J, Schwartz MA. Talin as a mechanosensitive signaling hub. Journal Of Cell Biology 2018, 217: 3776-3784. PMID: 30254032, PMCID: PMC6219721, DOI: 10.1083/jcb.201808061.Peer-Reviewed Original ResearchConceptsSignaling hubsExtracellular matrixRod domainTalin rod domainIntegrin β subunitsDifferent protein interactionsLong rod domainSwitch-like behaviorActin cytoskeletonCytoplasmic domainCytoplasmic proteinsProtein interactionsHelical bundleGlobular head domainTalin functionTransmembrane receptorsHelix bundleΒ-subunitHead domainIntegrin familyTalinCell adhesionIndividual domainsRecent evidenceDomain
2016
Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5)
Georgieva E, Borbat P, Grushin K, Stoilova-McPhie S, Kulkarni N, Liang Z, Freed J. Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5). Frontiers In Physiology 2016, 7: 317. PMID: 27524969, PMCID: PMC4965473, DOI: 10.3389/fphys.2016.00317.Peer-Reviewed Original ResearchTransmembrane domainDouble electron-electron resonanceSingle transmembrane helixM2 transmembrane domainCore transmembrane domainNoticeable conformational changesC-terminal sideJuxtamembrane residuesTransmembrane helicesOligomer equilibriumHelix bundleConformational rearrangementsGolgi apparatusConformational responseM2 proteinStable tetramerConformational changesExit poreProton channelChannel closureG34A mutationSpecific mutationsLipid bilayersLow pH environmentViral cycle
2014
Sequence and conformational preferences at termini of α‐helices in membrane proteins: Role of the helix environment
Shelar A, Bansal M. Sequence and conformational preferences at termini of α‐helices in membrane proteins: Role of the helix environment. Proteins Structure Function And Bioinformatics 2014, 82: 3420-3436. PMID: 25257385, DOI: 10.1002/prot.24696.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsComputational BiologyConserved SequenceDatabases, ProteinHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane ProteinsModels, BiologicalProtein ConformationProtein FoldingProtein StabilityProtein Structure, SecondarySoftware ValidationTerminology as TopicConceptsMembrane proteinsSequence preferenceΑ-helixC-terminusHelical membrane proteinsCommon secondary structural elementsHelix terminiStructural motifsSecondary structural elementsSecondary structure predictionRat neurotensin receptorTransmembrane helicesMembrane environmentHelix bundleSequencing studiesHelical positionsAmino acidsProteinStructure predictionTerminusMembrane coreGlobular proteinsMotifHelixConformational preferences
1995
Structural Model of the Phospholamban Ion Channel Complex in Phospholipid Membranes
Arkin I, Rothman M, Ludlam C, Aimoto S, Engelman D, Rothschild K, Smith S. Structural Model of the Phospholamban Ion Channel Complex in Phospholipid Membranes. Journal Of Molecular Biology 1995, 248: 824-834. PMID: 7752243, DOI: 10.1006/jmbi.1995.0263.Peer-Reviewed Original ResearchConceptsSelective ion conductanceTransmembrane domainAmino acid residuesN-terminal 30 amino acid residuesAcid residuesCircular dichroismPentameric protein complexFull-length proteinC-terminal 22 amino acid residuesPhospholipid membranesIon channel complexTransmembrane helicesProtein complexesPhosphorylation sitesMembrane proteinsIon conductanceCarboxy terminusHelix bundleIon poreReticulum membraneInhibitory complexLong helixPentameric complexSecondary structureProtein
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