2024
Dual roles for a tick protein disulfide isomerase during the life cycle of the Lyme disease agent
Tang X, Cui Y, Namarra U, Tian X, Rivas-Giorgi F, Fikrig E. Dual roles for a tick protein disulfide isomerase during the life cycle of the Lyme disease agent. MBio 2024, 15: e01754-24. PMID: 39470213, PMCID: PMC11633212, DOI: 10.1128/mbio.01754-24.Peer-Reviewed Original ResearchProtein disulfide isomeraseLyme disease agentDisulfide isomeraseBlood-feeding vectorsExtracellular pathogensGene expressionInvasion of host cellsThiol-disulfide oxidoreductasesDisease agentsGroup of enzymesStages of bacterial infectionVirulence factorsLife cycleChaperone activityMammalian hostsHost cellsBlood-feeding ticksIsomeraseMicrobial infectionsColonized ticksPathogensDiverse infectionsMicrobial invasionInfection of miceVector-borne diseases
2017
Multifunctional molecule ERp57: From cancer to neurodegenerative diseases
Hettinghouse A, Liu R, Liu C. Multifunctional molecule ERp57: From cancer to neurodegenerative diseases. Pharmacology & Therapeutics 2017, 181: 34-48. PMID: 28723413, PMCID: PMC5743601, DOI: 10.1016/j.pharmthera.2017.07.011.Peer-Reviewed Original ResearchConceptsProtein disulfide isomerase gene familyMultiple cellular localizationsEndoplasmic reticulum localizationDiverse pathological statesGene familyERp57 functionsProtein familyPDI familySubcellular compartmentsPhysiological processesCellular localizationMultifunctional memberERp57Aberrant functionalityNeurodegenerative diseasesTherapeutic developmentPathological statesFamilyLocalizationIsomeraseRedox activityAvailable knowledgeNumerous studiesHostExpression
2011
Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii
Banerjee M, Gupta K, Balaram H, Balaram P. Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii. Rapid Communications In Mass Spectrometry 2011, 25: 1915-1923. PMID: 21698673, DOI: 10.1002/rcm.5058.Peer-Reviewed Original ResearchConceptsMethanocaldococcus jannaschiiTriosephosphate isomeraseDisulfide bond formationIntramolecular disulfide bondsCysteine thiol groupsMonomer molecular massThree-dimensional structureThermophilic enzymesMass spectrometric identificationMS/MS analysisTetrameric enzymeTertiary structureMolecular massDisulfide bridgesDisulfide-bonded moleculesDisulfide bondsMonomeric massJannaschiiCircular dichroismComplete lossSpectrometric identificationIsomeraseEnzymeTryptic digestDa difference
2009
Role of Loop−Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase
Wang Y, Berlow RB, Loria JP. Role of Loop−Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase. Biochemistry 2009, 48: 4548-4556. PMID: 19348462, PMCID: PMC2713366, DOI: 10.1021/bi9002887.Peer-Reviewed Original ResearchConceptsLoop 7Triosephosphate isomeraseLoop 6Chicken triosephosphate isomeraseC-terminal hingeActive site loopActive site loop motionArchaeal homologueEnzyme triosephosphate isomeraseMutant enzymesEnzymatic functionProtein sequencesBiological functionsSite loopEnzymatic activityFold lossTemperature-dependent NMR experimentsLoop motionModel systemIsomeraseSequenceActive siteEnzymeEnzymatic reactionsMutants
2007
Proteomic Analysis of the Resistance to Aplidin in Human Cancer Cells
González-Santiago L, Alfonso P, Suárez Y, Núñez A, García-Fernández LF, Alvarez E, Muñoz A, Casal JI. Proteomic Analysis of the Resistance to Aplidin in Human Cancer Cells. Journal Of Proteome Research 2007, 6: 1286-1294. PMID: 17338558, DOI: 10.1021/pr060430+.Peer-Reviewed Original ResearchConceptsProtein disulfide isomeraseRole of PDINumber of proteinsRab geranylgeranyltransferaseInduction of apoptosisHuman cancer cellsDisulfide isomeraseProteomic approachMembrane proteinsProteomic analysisMALDI-TOF mass spectrometryApoptosis pathwayDatabase interrogationHeLa cellsCyclophilin AProteinCancer cellsAplidinApoptosisCystathionine gamma lyaseCellsMass spectrometryGeranylgeranyltransferaseEzrinIsomerase
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
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
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