2001
Glucocorticoid counter regulation: macrophage migration inhibitory factor as a target for drug discovery
Lolis E. Glucocorticoid counter regulation: macrophage migration inhibitory factor as a target for drug discovery. Current Opinion In Pharmacology 2001, 1: 662-668. PMID: 11757824, DOI: 10.1016/s1471-4892(01)00112-6.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCOP9 Signalosome ComplexDNA-Binding ProteinsDrug DesignGenes, p53GlucocorticoidsHumansInflammationInflammation MediatorsIntracellular Signaling Peptides and ProteinsMacrophage Migration-Inhibitory FactorsMembrane ProteinsMolecular Sequence DataNeoplasmsNeovascularization, PathologicPeptide HydrolasesPhosphoproteinsStructure-Activity RelationshipTranscription FactorsConceptsMacrophage migration inhibitory factorMigration inhibitory factorContribution of MIFInhibitory factorElevated MIF levelsMIF's biological activityActivity of CD4Natural killer cellsInflammatory neurological diseasesInflammatory lung diseasesMIF levelsUlcerative colitisKiller cellsRheumatoid arthritisLung diseaseInflammatory diseasesT cellsHuman studiesNeurological diseasesTherapeutic interventionsDiseaseEndothelial cellsNumber of diseasesIntracellular regulatory proteinsCancerCCR2 and CCR5 receptor‐binding properties of herpesvirus‐8 vMIP‐II based on sequence analysis and its solution structure
Shao W, Fernandez E, Sachpatzidis A, Wilken J, Thompson D, Schweitzer B, Lolis E. CCR2 and CCR5 receptor‐binding properties of herpesvirus‐8 vMIP‐II based on sequence analysis and its solution structure. The FEBS Journal 2001, 268: 2948-2959. PMID: 11358512, DOI: 10.1046/j.1432-1327.2001.02184.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesChemokinesChemokines, CCDimerizationEpitopesMagnetic Resonance SpectroscopyModels, ChemicalModels, MolecularMolecular Sequence DataPeptide BiosynthesisProtein BindingProtein ConformationProtein FoldingProtein Structure, SecondaryReceptors, CCR2Receptors, CCR5Receptors, ChemokineSequence Analysis, ProteinSequence Homology, Amino AcidConceptsHuman herpesvirus 8VMIP-IIChemokine receptorsCC chemokinesReceptor-binding propertiesNumerous chemokine receptorsPresence of epitopesHIV-1 viral entryHuman CC chemokineReceptor CCR2Kaposi's sarcomaHerpesvirus 8Infectious agentsCCR2Viral entryReceptor bindingReceptor specificityCCR5ChemokinesSarcomaReceptorsReceptor subfamiliesMagnetic resonanceBroad receptor specificityProtein II
2000
Comparison of the Structure of vMIP-II with Eotaxin-1, RANTES, and MCP-3 Suggests a Unique Mechanism for CCR3 Activation † , ‡
Fernandez E, Wilken J, Thompson D, Peiper S, Lolis E. Comparison of the Structure of vMIP-II with Eotaxin-1, RANTES, and MCP-3 Suggests a Unique Mechanism for CCR3 Activation † , ‡. Biochemistry 2000, 39: 12837-12844. PMID: 11041848, DOI: 10.1021/bi001166f.Peer-Reviewed Original ResearchAmino Acid SequenceAnti-HIV AgentsChemokine CCL11Chemokine CCL5Chemokine CCL7ChemokinesChemokines, CCChemotactic Factors, EosinophilCrystallography, X-RayCytokinesHerpesvirus 8, HumanHumansModels, MolecularMolecular Sequence DataMonocyte Chemoattractant ProteinsReceptors, CCR3Receptors, ChemokineReceptors, VirusSequence AlignmentSequence Homology, Amino Acid
1999
Macrophage migration inhibitory factor: Cytokine, hormone, or enzyme?
Swope M, Lolis E. Macrophage migration inhibitory factor: Cytokine, hormone, or enzyme? 1999, 139: 1-32. PMID: 10453691, DOI: 10.1007/bfb0033647.Peer-Reviewed Original Research
1998
Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II
Shao W, Fernandez E, Wilken J, Thompson D, Siani M, West J, Lolis E, Schweitzer B. Accessibility of selenomethionine proteins by total chemical synthesis: structural studies of human herpesvirus‐8 MIP‐II. FEBS Letters 1998, 441: 77-82. PMID: 9877169, DOI: 10.1016/s0014-5793(98)01520-8.Peer-Reviewed Original ResearchConceptsTotal chemical synthesisNuclear magnetic resonanceChemical synthesisX-ray crystallographyThree-dimensional structureStructural studiesSynthesisSecondary structureGenome programNew proteinsMagnetic resonanceSelenomethionine proteinsRecombinant proteinsProtein IIHeavy-atom derivativesProteinMIP IICrystallographyMonomersStructureDeterminationDerivativesCloningHigh resolutionResonanceDirect link between cytokine activity and a catalytic site for macrophage migration inhibitory factor
Swope M, Sun H, Blake P, Lolis E. Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor. The EMBO Journal 1998, 17: 3534-3541. PMID: 9649424, PMCID: PMC1170690, DOI: 10.1093/emboj/17.13.3534.Peer-Reviewed Original ResearchConceptsN-terminal prolineN-terminal regionStructure-based inhibitorsMultiple sequence alignmentThree-dimensional structureInvariant residuesEntire polypeptideMicrobial enzymesCatalytic basePro-1Sequence alignmentMIF homologuesCytokine activityHuman macrophage migration inhibitory factorCatalytic siteProlineInhibitory factorHomologuesUnderlying biological activityP-hydroxyphenylpyruvateProteinMacrophage migration inhibitory factorActive siteBiological activityCrystal structure of chemically synthesized [N33A] stromal cell-derived factor 1α, a potent ligand for the HIV-1 “fusin” coreceptor
Dealwis C, Fernandez E, Thompson D, Simon R, Siani M, Lolis E. Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1α, a potent ligand for the HIV-1 “fusin” coreceptor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 6941-6946. PMID: 9618518, PMCID: PMC22694, DOI: 10.1073/pnas.95.12.6941.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesChemokine CXCL12Chemokines, CXCHIV-1HumansLigandsMolecular Sequence DataProtein ConformationReceptors, CXCR4Solution Structure of Murine Macrophage Inflammatory Protein-2 † , ‡
Shao W, Jerva L, West J, Lolis E, Schweitzer B. Solution Structure of Murine Macrophage Inflammatory Protein-2 † , ‡. Biochemistry 1998, 37: 8303-8313. PMID: 9622482, DOI: 10.1021/bi980112r.Peer-Reviewed Original Research
1997
Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: Sequence analysis and mutagenesis identify receptor binding epitopes
Jerva L, Lolis E, Sullivan G. Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: Sequence analysis and mutagenesis identify receptor binding epitopes. Protein Science 1997, 6: 1643-1652. PMID: 9260277, PMCID: PMC2143775, DOI: 10.1002/pro.5560060805.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntigens, CDBase SequenceCell LineChemokine CXCL2Chemokines, CXCCloning, MolecularDNA PrimersEpitopesHumansIntercellular Signaling Peptides and ProteinsMiceMolecular Sequence DataMonokinesMutagenesis, Site-DirectedNeutrophilsReceptors, InterleukinReceptors, Interleukin-8ARecombinant ProteinsSequence Homology, Amino Acid
1995
Salvaging recombinants from low-efficiency ligase reactions for more efficient subcloning.
Sun H, Lolis E. Salvaging recombinants from low-efficiency ligase reactions for more efficient subcloning. BioTechniques 1995, 18: 644-6, 648, 650. PMID: 7598899.Peer-Reviewed Original Research
1994
Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.
Joseph-McCarthy D, Lolis E, Komives E, Petsko G. Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site. Biochemistry 1994, 33: 2815-23. PMID: 8130194, DOI: 10.1021/bi00176a010.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesCrystallizationCrystallography, X-RayDNA PrimersLigandsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPoint MutationProtein FoldingProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiaeTriose-Phosphate IsomeraseX-Ray DiffractionConceptsMutant enzymesSubstrate-binding loopActive-site LysLys-12Wild-type enzymeMet side chainsActive siteEnzyme-inhibitor complexThree-dimensional structureMutant structuresWild typeTriosephosphate isomeraseDianionic substrateEnzymeSame crystal formCrystal structureMET mutationsSide chainsIsomeraseSitesCrystal formsMutationsPhosphoglycolohydroxamateMethionine
1991
Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.
Komives E, Chang L, Lolis E, Tilton R, Petsko G, Knowles J. Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. Biochemistry 1991, 30: 3011-9. PMID: 2007138, DOI: 10.1021/bi00226a005.Peer-Reviewed Original Research
1990
Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Lolis E, Alber T, Davenport R, Rose D, Hartman F, Petsko G. Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 1990, 29: 6609-18. PMID: 2204417, DOI: 10.1021/bi00480a009.Peer-Reviewed Original ResearchConceptsHydrogen bonding interactionsYeast triosephosphate isomeraseActive site structureNon-hydrogen atomsWater moleculesActive siteActive site residuesDrug designGlu-165Triosephosphate isomeraseSite structureCatalytic baseCrystal contactsSite residuesR factorTIM structuresFlexible loopLys-12Polypeptide chainStructureSubunit interfaceCarboxylateMonomersHydroxylFirst time