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
1994
A dimerization motif for transmembrane α–helices
Lemmon M, Treutlein H, Adams P, Brünger A, Engelman D. A dimerization motif for transmembrane α–helices. Nature Structural & Molecular Biology 1994, 1: 157-163. PMID: 7656033, DOI: 10.1038/nsb0394-157.Peer-Reviewed Original ResearchConceptsTransmembrane α-helicesHydrophobic transmembrane α-helicesSpecific helix-helix interactionsΑ-helixIntegral membrane proteinsHelix-helix interactionsHelix-helix interfaceDimerization motifSpecific dimerizationMembrane proteinsHelix associationFunctional analysisAmino acidsSuch motifsLipid bilayersMotifParticular motifsFoldingDimerizationSuch interactionsComplex membranesProteinOligomerizationVariety of systemsInteraction
1993
Mutations can cause large changes in the conformation of a denatured protein.
Flanagan J, Kataoka M, Fujisawa T, Engelman D. Mutations can cause large changes in the conformation of a denatured protein. Biochemistry 1993, 32: 10359-70. PMID: 8399179, DOI: 10.1021/bi00090a011.Peer-Reviewed Original ResearchConceptsAmino acid substitutionsPolypeptide chainSecondary structureCoil-like polymerAcid substitutionsCircular dichroism spectroscopySmall-angle X-ray scatteringSingle amino acid substitutionCarboxyl-terminal deletionsPersistent secondary structureResidual secondary structureX-ray scatteringUseful model systemDelta polypeptideSolvent conditionsDichroism spectroscopyConformational distributionCarboxyl terminusNative nucleaseRandom polymersAmino acidsSingle substitutionPolymersStaphylococcal nucleaseGlobular proteins
1992
Truncated staphylococcal nuclease is compact but disordered.
Flanagan J, Kataoka M, Shortle D, Engelman D. Truncated staphylococcal nuclease is compact but disordered. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 748-752. PMID: 1731350, PMCID: PMC48316, DOI: 10.1073/pnas.89.2.748.Peer-Reviewed Original ResearchConceptsComplete folding pathwayWild-type levelsCarboxyl-terminal deletionsSecondary structural featuresNative-like conformationPersistent secondary structureProtein foldsCarboxyl terminusFolding pathwaysPolypeptide chainSecondary structureAmino acidsStaphylococcal nucleaseSmall-angle X-rayNuclear magnetic resonanceCircular dichroismPhysiological conditionsNucleasePotent inhibitorDeletionSolvent exclusionMolecules resultsStructural featuresPresence of calciumRibosomes
1991
Structure-function studies of bacteriorhodopsin XV. Effects of deletions in loops B-C and E-F on bacteriorhodopsin chromophore and structure
Gilles-Gonzalez M, Engelman D, Khorana H. Structure-function studies of bacteriorhodopsin XV. Effects of deletions in loops B-C and E-F on bacteriorhodopsin chromophore and structure. Journal Of Biological Chemistry 1991, 266: 8545-8550. PMID: 2022666, DOI: 10.1016/s0021-9258(18)93009-7.Peer-Reviewed Original Research
1980
Bacteriorhodopsin is an inside-out protein.
Engelman D, Zaccai G. Bacteriorhodopsin is an inside-out protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 5894-5898. PMID: 6934521, PMCID: PMC350178, DOI: 10.1073/pnas.77.10.5894.Peer-Reviewed Original ResearchConceptsAmino acid sequenceSingle bacteriorhodopsin moleculePurple membrane structureAcid sequenceAlpha-helixBacteriorhodopsin moleculesSoluble proteinBiosynthetic incorporationBacteriorhodopsin structureAmino acidsHalobacterium halobiumProteinMembrane structureValineMolecular interiorPurple membranePhenylalanineDifference Fourier techniquesLipid regionsHelixHalobiumMoleculesSequenceBacteriorhodopsinMembrane