2021
CD1a selectively captures endogenous cellular lipids that broadly block T cell response
Cotton R, Wegrecki M, Cheng T, Chen Y, Veerapen N, Le Nours J, Orgill D, Pomahac B, Talbot S, Willis R, Altman J, de Jong A, Van Rhijn I, Clark R, Besra G, Ogg G, Rossjohn J, Moody D. CD1a selectively captures endogenous cellular lipids that broadly block T cell response. Journal Of Experimental Medicine 2021, 218: e20202699. PMID: 33961028, PMCID: PMC8111460, DOI: 10.1084/jem.20202699.Peer-Reviewed Original ResearchConceptsNatural endogenous inhibitorsEndogenous lipidsCD1a proteinCellular lipidsT cell activationMembrane phospholipidsLonger lipidsSurface residuesEndogenous inhibitorLipidomics methodDetailed chemical structureCell activationLipidsCellsNatural blockerSphingolipidsDisplay platformProteinCrystal structureResiduesCell responsesBindingTetramerC42Sphingomyelin
2019
B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis
Li Y, Ma X, Chen Z, Wu H, Wang P, Wu W, Cheng N, Zeng L, Zhang H, Cai X, Chen SJ, Chen Z, Meng G. B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis. Nature Communications 2019, 10: 3789. PMID: 31439836, PMCID: PMC6706441, DOI: 10.1038/s41467-019-11746-0.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarcinogenesisGene Knockout TechniquesHeLa CellsHumansLeukemia, Promyelocytic, AcuteMiceMice, TransgenicMutationOncogene Proteins, FusionPromyelocytic Leukemia ProteinProtein DomainsProtein MultimerizationRetinoic Acid Receptor alphaScattering, Small AngleSequence Analysis, RNASingle-Cell AnalysisSumoylationX-Ray DiffractionConceptsSingle-cell RNA sequencing analysisRNA sequencing analysisNuclear assemblyPML SUMOylationBiogenesisImportant regulatorOligomerization mechanismSequencing analysisUltracentrifugation analysisOligomerizationPML-RARαTransgenic miceLeukemogenesisGel filtrationSUMOylationSAXS characterizationTransactivationRegulatorProteinMechanismTetramerAssemblyF158Vivo studiesPMLHuman keratin 1/10‐1B tetramer structures reveal a knob‐pocket mechanism in intermediate filament assembly
Eldirany SA, Ho M, Hinbest AJ, Lomakin IB, Bunick CG. Human keratin 1/10‐1B tetramer structures reveal a knob‐pocket mechanism in intermediate filament assembly. The EMBO Journal 2019, 38: embj2018100741. PMID: 31036554, PMCID: PMC6545558, DOI: 10.15252/embj.2018100741.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionCircular DichroismCrystallography, X-RayCytoskeletonDynamic Light ScatteringHumansHydrophobic and Hydrophilic InteractionsIntermediate Filament ProteinsKeratin-1Keratin-10Models, MolecularMutation, MissenseProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondarySkin DiseasesConceptsFilament assemblyN-terminal hydrophobic pocketIntermediate filament assemblyTetramer assemblyÅ structureÅ resolutionCircular dichroism measurementsTetramer formationAssembly mechanismHydrophobic faceHydrophobic pocketSecondary structureOctamer structureEpidermolytic palmoplantar keratodermaKeratin filamentsIntermediate filamentsMutationsPathogenic mutationsTetramer structureDichroism measurementsAtomic resolutionAssemblyBiochemical determinantsKeratin 1/10Tetramer
2013
The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation
Harper SL, Sriswasdi S, Tang HY, Gaetani M, Gallagher PG, Speicher DW. The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. Blood 2013, 122: 3045-3053. PMID: 23974198, PMCID: PMC3811177, DOI: 10.1182/blood-2013-02-487702.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCross-Linking ReagentsElliptocytosis, HereditaryErythrocyte MembraneHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSpectrinConceptsHereditary elliptocytosisMembrane destabilizationLarge conformational rearrangementsGel filtration analysisMembrane proteinsTetramer assemblyHereditary pyropoikilocytosisBiophysical analysisCommon hereditary elliptocytosisConformational rearrangementsDimer conformationHelical contentTetramerization siteFiltration analysisSpectrin tetramersNovel mechanismUnknown mechanismMutationsBinding assaysSpectrinChemical crosslinkingErythrocyte shapeTetramerErythrocyte membranesMembraneReal Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity
Bian S, Navaratnam D, Santos-Sacchi J. Real Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity. PLOS ONE 2013, 8: e66078. PMID: 23762468, PMCID: PMC3677934, DOI: 10.1371/journal.pone.0066078.Peer-Reviewed Original ResearchConceptsObligate tetramerPlasma membraneMembrane motor proteinIntegral membrane proteinsTetracycline-inducible cell lineMembrane proteinsMotor proteinsPrestin densityTemperature blockPrestinFluorescence measuresMembrane fluorescenceCell linesNonlinear capacitanceCochlear amplificationProteinTetramerMembraneFluorescencePrevious observationsVoltage clampFluorescence methodCellsAmplification
2012
Molecular Basis for a Protein-Mediated DNA-Bridging Mechanism that Functions in Condensation of the E. coli Chromosome
Dupaigne P, Tonthat NK, Espéli O, Whitfill T, Boccard F, Schumacher MA. Molecular Basis for a Protein-Mediated DNA-Bridging Mechanism that Functions in Condensation of the E. coli Chromosome. Molecular Cell 2012, 48: 560-571. PMID: 23084832, PMCID: PMC7505563, DOI: 10.1016/j.molcel.2012.09.009.Peer-Reviewed Original ResearchConceptsMolecular basisColi chromosomeLarge chromosomal domainsDNA-binding motifE. coli chromosomeChromosomal domainsChromosome condensationGenomic packagingLoop DNAC-terminalChromosomesMacrodomainsMat sitesMatPMatP.DNAMotifHelixMutationsResiduesElectron microscopy studiesMicroscopy studiesMechanismTetramerEnterobacteria
2006
Characterization of synthetic oxomanganese complexes and the inorganic core of the O2-evolving complex in photosystem II: Evaluation of the DFT/B3LYP level of theory
Sproviero EM, Gascon JA, McEvoy JP, Brudvig GW, Batista VS. Characterization of synthetic oxomanganese complexes and the inorganic core of the O2-evolving complex in photosystem II: Evaluation of the DFT/B3LYP level of theory. Journal Of Inorganic Biochemistry 2006, 100: 786-800. PMID: 16510187, DOI: 10.1016/j.jinorgbio.2006.01.017.Peer-Reviewed Original ResearchConceptsDFT/B3LYP levelOxomanganese complexesDFT/B3LYPB3LYP levelDensity functional theory (DFT) B3LYP levelBecke-3-LeeOxygen-evolving complexPhotosystem IISpin electronic statesInorganic coreImidazole ligandsMn complexesMu-oxoMagnetic experimental dataElectronic propertiesModest basis setsBasis setHybrid densityMechanistic studiesMn trimersComplexesMagnetic propertiesB3LYPTetramerBenchmark calculations
2003
Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis
Yoon J, Oh B, Kim K, Park JE, Wang J, Kim HS, Kim Y. Modifying the oligomeric state of cyclic amidase and its effect on enzymatic catalysis. Biochemical And Biophysical Research Communications 2003, 310: 651-659. PMID: 14521961, DOI: 10.1016/j.bbrc.2003.09.056.Peer-Reviewed Original ResearchConceptsCyclic amidasesD-hydantoinaseCatalytic propertiesHydrophobic interaction domainCatalytic activityEnzymatic catalysisHydrophobic interactionsCyclic ureidesReversible hydrolysisDimeric formHydrophobic patchDimeric interactionsOligomeric stateSpecific activityTetramerKinetic propertiesCatalysisLow specific activityDihydropyrimidinesPropertiesHydantoinsDimersDihydroorotaseHydrolysisInteraction
2000
Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond
Li F, Wang J, Steitz T. Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond. Journal Of Molecular Biology 2000, 304: 483-492. PMID: 11090289, DOI: 10.1006/jmbi.2000.4189.Peer-Reviewed Original ResearchConceptsActive siteMulti-angle laser lightSmall-angle X-ray scatteringSize exclusion chromatographyX-ray scatteringFurther dimerizationExclusion chromatographyMoleculesDimeric enzymeC basesOligomerization stateTetramerTransfer RNA moleculesLaser lightTRNA moleculesRNA moleculesMonomersPrimer strandChromatographyEnzymeDimersHigh specificityBindingCCA-adding enzymeDimerization
1995
High-valent oxomanganese clusters: structural and mechanistic work relevant to the oxygen-evolving center in photosystem II
Manchanda R, Brudvig G, Crabtree R. High-valent oxomanganese clusters: structural and mechanistic work relevant to the oxygen-evolving center in photosystem II. Coordination Chemistry Reviews 1995, 144: 1-38. DOI: 10.1016/0010-8545(95)01147-h.Peer-Reviewed Original ResearchO2-evolving centerActive siteOxygen-evolving centerPhotosystem IIOxomanganese clusterBioinorganic chemistryInorganic chemistsWater oxidationComplex chemistryMechanistic aspectsBiophysical studiesChemistryMagnetic propertiesNative enzymeMechanistic workPS IINuclearityChemistsMetalloproteinsSuch clustersConsiderable interestOxidationRecent effortsChemicalsTetramer
1990
Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction
Hughes R, Hatfull G, Rice P, Steitz T, Grindley N. Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction. Cell 1990, 63: 1331-1338. PMID: 2175679, DOI: 10.1016/0092-8674(90)90428-h.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsHigher-order protein-protein interactionsCooperativity mutantsSite-specific recombinaseGamma delta resolvaseMutant phenotypeResolvase mutantsNucleoprotein complexesCrystallographic tetramersResolvase dimersΓδ resolvaseResolvaseCooperative bindingMutantsDNARecombinationSide chainsRecombinaseProteinInteractionCointegrate intermediatePhenotypeRecombination reactionBindingTetramerThe crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution
Sanderson M, Freemont P, Rice P, Goldman A, Hatfull G, Grindley N, Steitz T. The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution. Cell 1990, 63: 1323-1329. PMID: 2175678, DOI: 10.1016/0092-8674(90)90427-g.Peer-Reviewed Original Research
1989
Modeling the oxygen evolving complex of photosystem II. Redox chemistry and ligand binding of biologically relevant manganese tetramers
Thorp H, Kulawiec R, Brudvig G, Crabtree R. Modeling the oxygen evolving complex of photosystem II. Redox chemistry and ligand binding of biologically relevant manganese tetramers. Journal Of Inorganic Biochemistry 1989, 36: 226. DOI: 10.1016/0162-0134(89)84235-7.Peer-Reviewed Original Research
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