2020
CX3CL1 homo-oligomerization drives cell-to-cell adherence
Ostuni M, Hermand P, Saindoy E, Guillou N, Guellec J, Coens A, Hattab C, Desuzinges-Mandon E, Jawhari A, Iatmanen-Harbi S, Lequin O, Fuchs P, Lacapere J, Combadière C, Pincet F, Deterre P. CX3CL1 homo-oligomerization drives cell-to-cell adherence. Scientific Reports 2020, 10: 9069. PMID: 32494000, PMCID: PMC7271195, DOI: 10.1038/s41598-020-65988-w.Peer-Reviewed Original ResearchConceptsNumerous adhesion moleculesPhotobleaching assaysNative electrophoresisAdhesive potencyTransmembrane peptidesLipid environmentKey immune processesAdhesive functionFluorescence recoveryFunctional roleDomain peptideFluorescence kineticsOligomerizationCellular adherenceMolecular modelingAdhesion moleculesCell adherenceTransmembrane chemokineImmune processesCompact bundlePeptidesBlood leukocytesClustersElectrophoresisCX3CL1
1997
Structure of the Transmembrane Cysteine Residues in Phospholamban
Arkin I, Adams P, Brünger A, Aimoto S, Engelman D, Smith S. Structure of the Transmembrane Cysteine Residues in Phospholamban. The Journal Of Membrane Biology 1997, 155: 199-206. PMID: 9050443, DOI: 10.1007/s002329900172.Peer-Reviewed Original ResearchConceptsTransmembrane domainCysteine residuesSide chainsPentameric complexCysteine side chainsTransmembrane cysteine residuesLong α-helixIntrahelical hydrogen bondsBackbone carbonyl oxygenSelective ion channelsPolar side chainsElectrostatic potential fieldCarbonyl oxygenSulfhydryl groupsHydrogen bondsMembrane proteinsWild-type phospholambanVibrational spectraMutagenesis studiesTransmembrane peptidesAlanine substitutionsMolecular dynamicsReticulum membraneElectrostatic calculationsΑ-helix
1996
Leucine side-chain rotamers in a glycophorin A transmembrane peptide as revealed by three-bond carbon—carbon couplings and 13C chemical shifts
MacKenzie K, Prestegard J, Engelman D. Leucine side-chain rotamers in a glycophorin A transmembrane peptide as revealed by three-bond carbon—carbon couplings and 13C chemical shifts. Journal Of Biomolecular NMR 1996, 7: 256-260. PMID: 8785502, DOI: 10.1007/bf00202043.Peer-Reviewed Original ResearchConceptsChemical shiftsPeptide dimersΑ-carbonSide chainsSide-chain rotamer populationsCarbon-carbon couplingLeucine side chainsThree-bond J couplingsNMR pulse sequencesΔ-methyl groupsRotamer populationsMethyl carbonFast exchangeSide-chain rotamersJ-couplingsTransmembrane peptidesDimer interfaceRotameric statesProtein systemsRotamersShift distributionGlycophorin A.DimersChainMethyl
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