2009
Translocating cell‐impermeable molecules through the plasma membrane of cancer cells
THEVENIN D, An M, Andreev O, Reshetnyak Y, Engelman D. Translocating cell‐impermeable molecules through the plasma membrane of cancer cells. The FASEB Journal 2009, 23: 796.7-796.7. DOI: 10.1096/fasebj.23.1_supplement.796.7.Peer-Reviewed Original ResearchCell-impermeable moleculesCell-impermeable cargo moleculesDrug designLipid bilayersHost-guest modelMembrane-impermeable cargoNovel delivery systemPhysiological pHTraverse membranesModel cargoCancer cell membraneDelivery systemCargo moleculesMoleculesCargo propertiesBilayersPeptidesMembraneSingle amino acidPropertiesC-terminusAmino acidsPotential therapeutic agentTherapeutic agentsAcidity
2006
ph‐Triggered Transport of Molecules into Cells by Transmembrane Helix Insertion
Engelman D, Andreev O, Reshetnyak Y. ph‐Triggered Transport of Molecules into Cells by Transmembrane Helix Insertion. The FASEB Journal 2006, 20: a457-a457. DOI: 10.1096/fasebj.20.4.a457-b.Peer-Reviewed Original ResearchC-terminusTransmembrane helix insertionActin cytoskeletonHelix insertionPlasma membraneTransbilayer helicesTarget cellsCell contractilityBiophysical measurementsCancer cellsDisulfide linksCytoplasmCellsWater-soluble peptidesDiseased tissuesPeptidesMembraneAcidic pHCytoskeletonFluorescent dyeHelixPhalloidinAcidic environmentMoleculesInjection of molecules
1992
Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment.
Kahn T, Engelman D. Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 1992, 31: 6144-51. PMID: 1627558, DOI: 10.1021/bi00141a027.Peer-Reviewed Original ResearchConceptsStable transmembrane helixSecond helical segmentX-ray diffractionCovalent connectionAbsorption spectroscopyTwo-dimensional crystalsIndependent folding domainsBacteriorhodopsinHelical segmentsNative structureHelixSpectroscopyPeptidesDiffractionTransmembrane helicesMoleculesCrystalsFragmentsMaterialsStructure
1989
Melittin binding causes a large calcium-dependent conformational change in calmodulin.
Kataoka M, Head J, Seaton B, Engelman D. Melittin binding causes a large calcium-dependent conformational change in calmodulin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 6944-6948. PMID: 2780551, PMCID: PMC297967, DOI: 10.1073/pnas.86.18.6944.Peer-Reviewed Original ResearchConceptsConformational changesCalcium-dependent conformational changeDependent conformational changesCellular functionsTarget proteinsMelittin bindsCalmodulin functionCalmodulinSolution structureCalmodulin-melittin complexSmall-angle X-ray scatteringConformation changeAbsence of calciumCompetitive inhibitorOverall structureMelittin bindingTarget peptideMelittinPresence of calciumGlobular shapeCa2PeptidesX-ray scatteringProteinBinds