2001
CCR2 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
1998
Macrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*
Swope M, Sun H, Klockow B, Blake P, Lolis E. Macrophage Migration Inhibitory Factor Interactions with Glutathione and S -Hexylglutathione*. Journal Of Biological Chemistry 1998, 273: 14877-14884. PMID: 9614090, DOI: 10.1074/jbc.273.24.14877.Peer-Reviewed Original ResearchBinding SitesCircular DichroismEnzyme InhibitorsFluorescenceGlutathioneHumansHydrogen-Ion ConcentrationIntramolecular OxidoreductasesMacrophage Migration-Inhibitory FactorsMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein ConformationProtein FoldingRecombinant ProteinsSulfhydryl Compounds
1990
Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Lolis E, Petsko G. Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis. Biochemistry 1990, 29: 6619-25. PMID: 2204418, DOI: 10.1021/bi00480a010.Peer-Reviewed Original ResearchConceptsHydrogen bondsSide chainsGlu-165Triosephosphate isomeraseLatter hydrogen bondTransition state analogueFinal R factorEnzyme-inhibitor complexSpectroscopic resultsActive siteConformational changesCrystallographic analysisLoop movesPhosphoglycolic acidIsomeraseUnbound formCatalysisR factorBondsEnzymeComplexesStructural termsAtomic modelBindingChain
1987
Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
Alber T, Davenport R, Giammona D, Lolis E, Petsko G, Ringe D. Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme? Cold Spring Harbor Symposia On Quantitative Biology 1987, 52: 603-13. PMID: 3331346, DOI: 10.1101/sqb.1987.052.01.069.Peer-Reviewed Original Research