2024
Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection
Zhu S, Bradfield C, Maminska A, Park E, Kim B, Kumar P, Huang S, Kim M, Zhang Y, Bewersdorf J, MacMicking J. Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection. Science 2024, 383: eabm9903-eabm9903. PMID: 38422126, PMCID: PMC12091997, DOI: 10.1126/science.abm9903.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsCaspase-4Surface of Gram-negative bacteriaGuanosine triphosphate hydrolysisImmunity to infectionInnate immunity to infectionCryo-electron tomographyGram-negative bacteriaImmunity proteinSignaling platformsMembrane insertionHuman cellsNative structureCombat infectionsLipopolysaccharide releaseGasdermin DExtended conformationLiving organismsProteinDefense complexCellsNative architectureGBP1BacteriaInfection
2016
RNA Structural Determinants of Optimal Codons Revealed by MAGE-Seq
Kelsic E, Chung H, Cohen N, Park J, Wang H, Kishony R. RNA Structural Determinants of Optimal Codons Revealed by MAGE-Seq. Cell Systems 2016, 3: 563-571.e6. PMID: 28009265, PMCID: PMC5234859, DOI: 10.1016/j.cels.2016.11.004.Peer-Reviewed Original ResearchCodon choiceMAGE-seqRNA structureEnhanced translation initiationSynonymous codon choiceRNA folding predictionsDisruption of native structureSynthetic biology applicationsRNA structure determinationAmplicon deep sequencingGenes infACodon distributionCodon preferenceOptimal codonsTranslation initiationFold predictionRNA conformationDeep sequencingCodon optimizationCodonGene expressionCodon mutantsNative structureGenesMutants
2015
Regulation and aggregation of intrinsically disordered peptides
Levine ZA, Larini L, LaPointe NE, Feinstein SC, Shea JE. Regulation and aggregation of intrinsically disordered peptides. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 2758-2763. PMID: 25691742, PMCID: PMC4352815, DOI: 10.1073/pnas.1418155112.Peer-Reviewed Original ResearchConceptsStable native structureRole of osmolytesFragment of tauTrimethylamine N-oxideVital physiological functionsMicrotubule-associated tau proteinOsmolyte ureaAggregation propensityMicrotubule growthTau oligomerizationConformational ensemblesIDP structurePhysiological functionsNative structureCompact oligomersHelical filamentsProteinFibril formationCompact conformationNeurodegenerative diseasesTau proteinMonomer structureUnique classPeptidesN-oxide
2014
Cryo-electron tomography reveals ciliary defects underlying human RSPH1 primary ciliary dyskinesia
Lin J, Yin W, Smith MC, Song K, Leigh MW, Zariwala MA, Knowles MR, Ostrowski LE, Nicastro D. Cryo-electron tomography reveals ciliary defects underlying human RSPH1 primary ciliary dyskinesia. Nature Communications 2014, 5: 5727. PMID: 25473808, PMCID: PMC4267722, DOI: 10.1038/ncomms6727.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyNative 3D structureNormal human developmentDistant speciesHuman ciliaCilia structurePCD phenotypeCilia dysfunctionHuman diseasesNative structurePrimary ciliary dyskinesiaRadial spokesCiliaEssential roleFunctional heterogeneityHuman respiratory ciliaUnprecedented detailPrimary defectCiliary dyskinesiaUnknown primary defect
2012
Catalytic Site-Selective Thiocarbonylations and Deoxygenations of Vancomycin Reveal Hydroxyl-Dependent Conformational Effects
Fowler BS, Laemmerhold KM, Miller SJ. Catalytic Site-Selective Thiocarbonylations and Deoxygenations of Vancomycin Reveal Hydroxyl-Dependent Conformational Effects. Journal Of The American Chemical Society 2012, 134: 9755-9761. PMID: 22621706, PMCID: PMC3374881, DOI: 10.1021/ja302692j.Peer-Reviewed Original ResearchConceptsPeptide-based catalystsForm of vancomycinNew compoundsVancomycin derivativesRational designConformational consequencesCatalystConformational effectsNew analoguesSelectivity profileBiological activityThiocarbonylationDeoxygenationNative structureStructural roleHydroxylCompoundsDerivativesAnaloguesSubstrateStructure
2004
Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †
Scheuermann TH, Keeler C, Hodsdon ME. Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †. Biochemistry 2004, 43: 12198-12209. PMID: 15379558, DOI: 10.1021/bi0492556.Peer-Reviewed Original ResearchConceptsNMR chemical shift mapping experimentsChemical shift mapping experimentsNative structureS-adenosylmethionineProteasomal-dependent pathwayCatalytic mechanismProtein backboneIntracellular degradationIndirect conformational changesS-adenosylmethionine analogPresence of sinefunginBacterial orthologuesChemical shift changesProtein backbone dynamicsPseudomonas syringaeSubstrate recognitionProtein sequencesSAM analoguesConformational changesNMR spectroscopyBackbone dynamicsMapping experimentsBackbone mobilitySinefunginNMR relaxation
2001
Quality control of transmembrane domain assembly in the tetraspanin CD82
Cannon K, Cresswell P. Quality control of transmembrane domain assembly in the tetraspanin CD82. The EMBO Journal 2001, 20: 2443-2453. PMID: 11350933, PMCID: PMC125455, DOI: 10.1093/emboj/20.10.2443.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumTransmembrane segmentsDomain assemblyER quality controlFirst transmembrane segmentMore transmembrane segmentsER membraneER lumenChaperone calnexinSeparate polypeptidesTetraspanin CD82TM-1Extracellular domainCalnexinNative structureCell surfaceTM-2Lipid bilayersCD82AssemblyQuality controlPrimary mechanismProlonged interactionPolypeptideCalreticulinMechanisms of protein folding
Grantcharova V, Alm E, Baker D, Horwich A. Mechanisms of protein folding. Current Opinion In Structural Biology 2001, 11: 70-82. PMID: 11179895, DOI: 10.1016/s0959-440x(00)00176-7.Peer-Reviewed Original ResearchConceptsEscherichia coli chaperonin GroELNon-native proteinsATP-dependent formationCo-chaperonin GroESLowest free energy pathChaperonin GroELProtein foldingUnfolded proteinsLarge proteinsGroELNative stateNative structureContact orderProteinChaperoninKinetic trapsFoldingChaperonesGroESFree energy pathPolypeptideComplexes
1997
Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
Munson M, Anderson K, Regan L. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Structure 1997, 2: 77-87. PMID: 9080201, DOI: 10.1016/s1359-0278(97)00008-4.Peer-Reviewed Original Research
1992
Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment.
Kahn T, Engelman D. Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 1992, 31: 6144-51. PMID: 1627558, DOI: 10.1021/bi00141a027.Peer-Reviewed Original ResearchConceptsStable transmembrane helixSecond helical segmentX-ray diffractionCovalent connectionAbsorption spectroscopyTwo-dimensional crystalsIndependent folding domainsBacteriorhodopsinHelical segmentsNative structureHelixSpectroscopyPeptidesDiffractionTransmembrane helicesMoleculesCrystalsFragmentsMaterialsStructure
1990
Human Ro ribonucleoprotein particles: characterization of native structure and stable association with the La polypeptide.
Boire G, Craft J. Human Ro ribonucleoprotein particles: characterization of native structure and stable association with the La polypeptide. Journal Of Clinical Investigation 1990, 85: 1182-1190. PMID: 1690756, PMCID: PMC296550, DOI: 10.1172/jci114551.Peer-Reviewed Original ResearchConceptsHY4 RNAStable associationNative structurePossible functional associationRo RNPsCultured HeLa cellsRNA componentHY5 RNAFunctional associationHeLa cellsPolypeptideLa RNPsRNARNPHuman RoDiscrete subpopulationsMacromolecular targetsPotential macromolecular targetsRelated diseasesRNPsRibonucleoproteinHY1Characteristic physicochemical propertiesStable componentHY3
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