2011
First Step in Folding of Nonconstitutive Membrane Proteins: Spontaneous Insertion of a Polypeptide into a Lipid Bilayer and Formation of Helical Structure
Karabadzhak A, Weerakkody D, Thakur M, Anderson M, Engelman D, Andreev O, Markin V, Reshetnyak Y. First Step in Folding of Nonconstitutive Membrane Proteins: Spontaneous Insertion of a Polypeptide into a Lipid Bilayer and Formation of Helical Structure. Biophysical Journal 2011, 100: 346a. DOI: 10.1016/j.bpj.2010.12.2088.Peer-Reviewed Original Research
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
2001
Helical membrane proteins: diversity of functions in the context of simple architecture
Ubarretxena-Belandia I, Engelman D. Helical membrane proteins: diversity of functions in the context of simple architecture. Current Opinion In Structural Biology 2001, 11: 370-376. PMID: 11406389, DOI: 10.1016/s0959-440x(00)00217-7.Peer-Reviewed Original ResearchConceptsHelical membrane proteinsGenome-wide scaleAlpha-helical conformationDiversity of functionsIdentification of motifsMembrane proteinsProtein regionsHelix interactionsPolar sidechainsStructural roleLipid bilayersProteinDiversityMotifUse of deviationsConformationSidechainsFunctionFurther investigationBilayersSequestrationIdentification
2000
HELICAL MEMBRANE PROTEIN FOLDING, STABILITY, AND EVOLUTION
Popot J, Engelman D. HELICAL MEMBRANE PROTEIN FOLDING, STABILITY, AND EVOLUTION. Annual Review Of Biochemistry 2000, 69: 881-922. PMID: 10966478, DOI: 10.1146/annurev.biochem.69.1.881.Peer-Reviewed Original Research
1997
Spontaneous, pH-Dependent Membrane Insertion of a Transbilayer α-Helix †
Hunt J, Rath P, Rothschild K, Engelman D. Spontaneous, pH-Dependent Membrane Insertion of a Transbilayer α-Helix †. Biochemistry 1997, 36: 15177-15192. PMID: 9398245, DOI: 10.1021/bi970147b.Peer-Reviewed Original ResearchConceptsLipid bilayersIntegral membrane protein bacteriorhodopsinMembrane-spanning regionIntegral membrane proteinsPH-dependent membrane insertionAspartic acid residuesMembrane protein bacteriorhodopsinInsertion reactionMembrane insertionMembrane proteinsAqueous solutionHydrophobic sequenceAqueous bufferPoor solubilityAlpha-helixAcid residuesSignificant solubilityC-helixSpectroscopic assaysΑ-helixSecondary structureProtein bacteriorhodopsinNeutral pHPeptide associatesBilayersAssessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody
Hunt J, McCrea P, Zaccaı̈ G, Engelman D. Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody. Journal Of Molecular Biology 1997, 273: 1004-1019. PMID: 9367787, DOI: 10.1006/jmbi.1997.1330.Peer-Reviewed Original ResearchConceptsMembrane protein complexesIntegral membrane proteinsProtein complexesMembrane proteinsIntegral membrane protein complexPhospholipid vesiclesSmall unilamellar phospholipid vesiclesUnilamellar phospholipid vesiclesMolecular massF. MoodySpatial arrangementNon-ionic detergentIndividual complexesVesiclesModel systemMonomeric bacteriorhodopsinProteinUnknown scopeComplexesAggregation stateRadius of gyrationBacteriorhodopsinDetergentsBilayers
1996
Crossing the Hydrophobic Barrier--Insertion of Membrane Proteins
Engelman D. Crossing the Hydrophobic Barrier--Insertion of Membrane Proteins. Science 1996, 274: 1850-1851. PMID: 8984645, DOI: 10.1126/science.274.5294.1850.Peer-Reviewed Original Research
1995
Small angle x-ray scattering studies of magnetically oriented lipid bilayers
Hare B, Prestegard J, Engelman D. Small angle x-ray scattering studies of magnetically oriented lipid bilayers. Biophysical Journal 1995, 69: 1891-1896. PMID: 8580332, PMCID: PMC1236422, DOI: 10.1016/s0006-3495(95)80059-7.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonanceLipid bilayersMembrane-associated moleculesBilayer thicknessLipid particlesSmall-angle X-rayX-ray scatteringAngle X-rayNMR dataDLPC vesiclesOrientational parametersX-ray solutionMolar ratioPhospholipid moleculesStructural studiesOrientational energyPhospholipid bilayersAnalogue 3MoleculesBilayersInterparticle spacingX-rayMagnetic resonanceParticlesComplexes
1994
Specificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. FEBS Letters 1994, 346: 17-20. PMID: 8206151, DOI: 10.1016/0014-5793(94)00467-6.Peer-Reviewed Original Research
1990
Membrane protein folding and oligomerization: the two-stage model.
Popot J, Engelman D. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 1990, 29: 4031-7. PMID: 1694455, DOI: 10.1021/bi00469a001.Peer-Reviewed Original ResearchConceptsMembrane protein foldingIntegral membrane proteinsMembrane proteinsProtein foldingMembrane protein subunitsTransmembrane segmentsTransmembrane structureSequence dataProtein subunitsVariety of functionsAqueous channelsLipid bilayersFoldingProteinSubunitsOligomerizationAssemblyFragmentsBilayers
1987
Folding of Integral Membrane Proteins: Renaturation Experiments with Bacteriorhodopsin Support a Two-Stage Mechanism
Popot J, Engelman D. Folding of Integral Membrane Proteins: Renaturation Experiments with Bacteriorhodopsin Support a Two-Stage Mechanism. 1987, 345-346. DOI: 10.1007/978-1-4613-1941-2_48.Peer-Reviewed Original Research
1986
On the Folding of Bacteriorhodopsin
Engelman D. On the Folding of Bacteriorhodopsin. 1986, 167-172. DOI: 10.1007/978-1-4684-8410-6_18.Peer-Reviewed Original Research