2018
Misreading chaperone–substrate complexes from random noise
Wang J. Misreading chaperone–substrate complexes from random noise. Nature Structural & Molecular Biology 2018, 25: 989-990. PMID: 30297779, DOI: 10.1038/s41594-018-0144-3.Peer-Reviewed Original Research
2015
Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter
Lee Y, Min CK, Kim TG, Song HK, Lim Y, Kim D, Shin K, Kang M, Kang JY, Youn HS, Lee JG, An JY, Park KR, Lim JJ, Kim JH, Kim JH, Park ZY, Kim YS, Wang J, Kim DH, Eom SH. Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter. EMBO Reports 2015, 16: 1318-1333. PMID: 26341627, PMCID: PMC4662854, DOI: 10.15252/embr.201540436.Peer-Reviewed Original ResearchConceptsN-terminal domainMitochondrial calcium uniporterCalcium uniporterHuman mitochondrial calcium uniporterMitochondrial calcium uptake 1CaMKII phosphorylation siteDominant negative effectCell linesMitochondrial calcium uptakePhosphorylation sitesNovel foldDeletion mutantsMCU functionÅ resolutionTumor suppressorHeLa cell lineUniporterMutantsUptake 1Calcium uptakeS92SuppressorOncogeneRegulatorDomain
2008
A regulatable switch mediates self-association in an immunoglobulin fold
Calabrese MF, Eakin CM, Wang JM, Miranker AD. A regulatable switch mediates self-association in an immunoglobulin fold. Nature Structural & Molecular Biology 2008, 15: 965-971. PMID: 19172750, PMCID: PMC2680708, DOI: 10.1038/nsmb.1483.Peer-Reviewed Original ResearchMeSH KeywordsAmyloidAmyloidosisBeta 2-MicroglobulinCopperCrystallography, X-RayElectron Spin Resonance SpectroscopyHumansHydrophobic and Hydrophilic InteractionsImmunoglobulinsIn Vitro TechniquesModels, BiologicalModels, MolecularMultiprotein ComplexesProtein FoldingProtein Interaction Domains and MotifsProtein Structure, QuaternaryRenal Dialysis
2005
Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*
Park E, Rho YM, Koh OJ, Ahn SW, Seong IS, Song JJ, Bang O, Seol JH, Wang J, Eom SH, Chung CH. Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*. Journal Of Biological Chemistry 2005, 280: 22892-22898. PMID: 15849200, DOI: 10.1074/jbc.m500035200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCaseinsChromatographyCross-Linking ReagentsDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEndopeptidase ClpEscherichia coliEscherichia coli ProteinsGlycineHydrolysisModels, BiologicalModels, MolecularMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedMutationPeptidesProtein BindingProtein DenaturationProtein FoldingProtein TransportSequence Homology, Amino AcidTemperatureConceptsHslU ATPasePore motifHslVU complexHslV peptidaseCentral poreATP-dependent proteaseProtein unfoldingProteolytic active sitesHslU hexamerProteolytic chamberHslV dodecamerUnfolded proteinsHslV.HslUGly residueTranslocation processAmino acidsDegradation of caseinMotifProteinATP cleavageSame structural featuresATPase activityTranslocationATPase
2004
Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily
Wang J. Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily. Journal Of Structural Biology 2004, 148: 259-267. PMID: 15522774, DOI: 10.1016/j.jsb.2004.07.003.Peer-Reviewed Original ResearchConceptsNucleotide-dependent conformational changesT7 DNA helicaseImportant biological functionsMechanochemical motorOligomeric ringsDNA helicaseBiological functionsF1-ATPaseConformational changesDomain motionProteinMechanistic workForce generationHslUHelicaseFoldsChemical energyATPFamilyRing structureDomainMembers
2003
Domain Motions in GroEL upon Binding of an Oligopeptide
Wang J, Chen L. Domain Motions in GroEL upon Binding of an Oligopeptide. Journal Of Molecular Biology 2003, 334: 489-499. PMID: 14623189, DOI: 10.1016/j.jmb.2003.09.074.Peer-Reviewed Original Research
2002
Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP
Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA. Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP. Cell 2002, 111: 815-824. PMID: 12526808, DOI: 10.1016/s0092-8674(02)01115-7.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCrystallography, X-RayCytidine TriphosphateDimerizationDNA Polymerase betaGeobacillus stearothermophilusModels, MolecularMolecular Sequence DataProtein FoldingProtein Structure, TertiaryRNA NucleotidyltransferasesSequence Homology, Amino AcidConceptsCCA-adding enzymeResolution crystal structureDNA polymerase betaImmature tRNAsNew proteinsBase specificityNucleic acid templateBacillus stearothermophilusPalm domainPolymerase betaIncoming ATPTRNAATPTerminusSubunitsCrystal structureActive siteAdditional structural featuresEnzymeCTPStructural featuresComplexesImportant componentTailDomain
2001
Unraveling the means to the end in ATP-dependent proteases
Hochstrasser M, Wang J. Unraveling the means to the end in ATP-dependent proteases. Nature Structural & Molecular Biology 2001, 8: 294-296. PMID: 11276243, DOI: 10.1038/86153.Peer-Reviewed Original Research
1997
The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
Wang J, Hartling J, Flanagan J. The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis. Cell 1997, 91: 447-456. PMID: 9390554, DOI: 10.1016/s0092-8674(00)80431-6.Peer-Reviewed Original Research
1994
Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer.
Wang J, Smerdon S, Jäger J, Kohlstaedt L, Rice P, Friedman J, Steitz T. Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 7242-7246. PMID: 7518928, PMCID: PMC44375, DOI: 10.1073/pnas.91.15.7242.Peer-Reviewed Original Research