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