2001
Folding of malate dehydrogenase inside the GroEL–GroES cavity
Chen J, Walter S, Horwich A, Smith D. Folding of malate dehydrogenase inside the GroEL–GroES cavity. Nature Structural & Molecular Biology 2001, 8: 721-728. PMID: 11473265, DOI: 10.1038/90443.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesChaperonin 10Chaperonin 60Chromatography, High Pressure LiquidDeuteriumDimerizationHydrogen BondingKineticsMalate DehydrogenaseMass SpectrometryMitochondria, HeartModels, MolecularPeptide FragmentsProtein BindingProtein DenaturationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsSwineConceptsMalate dehydrogenaseNonnative substrate proteinGroEL-GroES cavitySubstrate proteinsProductive foldingChaperonin GroELApical domainGroESGroELMechanical unfoldingGlobal destabilizationSecondary structureHydrophilic chamberCentral cavityInitial proteinDeuterium exchangeFoldingProteinATPDehydrogenaseHydrophobic central cavityMass spectrometryOpen ringPolypeptideUnfolding
2000
Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL
Farr G, Furtak K, Rowland M, Ranson N, Saibil H, Kirchhausen T, Horwich A. Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL. Cell 2000, 100: 561-573. PMID: 10721993, DOI: 10.1016/s0092-8674(00)80692-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBacterial ProteinsBinding SitesCattleChaperonin 10Chaperonin 60Chemical PhenomenaChemistry, PhysicalCryoelectron MicroscopyCystineEscherichia coliEthylmaleimideImage Processing, Computer-AssistedMacromolecular SubstancesMalate DehydrogenaseModels, MolecularPeptidesProtein BindingProtein ConformationProtein FoldingProtein Structure, TertiaryRibulose-Bisphosphate CarboxylaseStructure-Activity RelationshipThiosulfate SulfurtransferaseConceptsNonnative substrate proteinApical domainSubstrate proteinsChaperonin GroELWild-type domainCross-linking experimentsCochaperonin GroESNonnative proteinsProductive foldingGroEL ringSingle polypeptideHydrophobic residuesMalate dehydrogenaseBinary complex formationRubiscoProteinInside aspectMultivalent bindingGroELCentral cavityComplex formationBindingDomainGroESOpen ring
1997
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Xu Z, Horwich A, Sigler P. The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex. Nature 1997, 388: 741-750. PMID: 9285585, DOI: 10.1038/41944.Peer-Reviewed Original ResearchConceptsGroEL-GroESApical domainCis ringMulti-subunit protein assembliesCo-chaperonin GroESRings of subunitsPeptide-binding residuesChaperonin complexConsumption of ATPProtein foldingGroEL subunitProtein assembliesTrans ringAllosteric mechanismGroESEquatorial domainBloc movementDouble toroidSecond GroESEscherichia coliOutward tiltAsymmetric intermediatesCentral cavitySubunitsInward tilt
1995
From the Cradle to the Grave: Ring Complexes in the Life of a Protein
Weissman J, Sigler P, Horwich A. From the Cradle to the Grave: Ring Complexes in the Life of a Protein. Science 1995, 268: 523-524. PMID: 7725096, DOI: 10.1126/science.7725096.Peer-Reviewed Original Research
1994
Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
Kim S, Willison K, Horwich A. Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends In Biochemical Sciences 1994, 19: 543-548. PMID: 7846767, DOI: 10.1016/0968-0004(94)90058-2.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceBinding SitesBiological EvolutionChaperonin 60ChaperoninsConserved SequenceIntracellular Signaling Peptides and ProteinsMicrotubule-Associated ProteinsMolecular Sequence DataNuclear ProteinsPeptidesSequence AlignmentT-Complex Genome RegionUbiquitin-Protein Ligases
1985
A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites
Kraus J, Hodges P, Williamson C, Horwich A, Kalousek F, Williams K, Rosenberg L. A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. Nucleic Acids Research 1985, 13: 943-952. PMID: 3839075, PMCID: PMC341044, DOI: 10.1093/nar/13.3.943.Peer-Reviewed Original ResearchConceptsAmino acid sequenceLeader sequenceAcid sequenceBasic residuesAmino-terminal leader sequenceE. coliComplete sequence homologyAmino acid residuesProtein sequence dataOrnithine transcarbamylaseCDNA clonesSequence dataDNA complementaryOrnithine transcarbamylasesSequence homologyEntire proteinHuman enzymeAcid residuesTranscarbamylasesComplementary DNAAmino acidsMessenger RNARat enzymeNucleotidesCatalytic site