2001
ClpA mediates directional translocation of substrate proteins into the ClpP protease
Reid B, Fenton W, Horwich A, Weber-Ban E. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 3768-3772. PMID: 11259663, PMCID: PMC31127, DOI: 10.1073/pnas.071043698.Peer-Reviewed Original ResearchConceptsSubstrate proteinsClpP proteaseUnfolded substrate proteinsATP-dependent unfoldingATP-dependent mannerATP-dependent translocationChaperone ClpAProteolytic chamberFluorescence resonance energy transferDirectional translocationCOOH terminusClpAResonance energy transferProteinTranslocationIntracellular degradationFluorescence anisotropyProteaseRing complexTerminusLarge assembliesDonor fluorophoreRecognition elementRecent studiesHslUV
1999
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
Weber-Ban E, Reid B, Miranker A, Horwich A. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 1999, 401: 90-93. PMID: 10485712, DOI: 10.1038/43481.Peer-Reviewed Original ResearchConceptsSubstrate proteinsATP-dependent degradationGreen fluorescent protein GFPHydrogen exchange experimentsStable monomeric proteinFluorescent protein GFPNon-native formsChaperone ClpAChaperone familyEukaryotic proteinsProtease ClpPPresence of ATPChaperonin GroELHexameric ringClpAProteasome functionProtein GFPProtein structureMonomeric proteinNative proteinGlobal unfoldingProteinCentral channelRecognition peptideClpAP
1998
The Hsp70 and Hsp60 Chaperone Machines
Bukau B, Horwich A. The Hsp70 and Hsp60 Chaperone Machines. Cell 1998, 92: 351-366. PMID: 9476895, DOI: 10.1016/s0092-8674(00)80928-9.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
1991
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
Trent J, Nimmesgern E, Wall J, Hartl F, Horwich A. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 1991, 354: 490-493. PMID: 1836250, DOI: 10.1038/354490a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsArchaeal ProteinsBacterial ProteinsBase SequenceDNA-Binding ProteinsHeat-Shock ProteinsIntracellular Signaling Peptides and ProteinsMiceMicrotubule-Associated ProteinsMolecular ChaperonesMolecular Sequence DataNuclear ProteinsSaccharomyces cerevisiaeSequence Homology, Nucleic AcidSulfolobusT-Complex Genome RegionTemperatureUbiquitin-Protein LigasesConceptsComplex polypeptide 1Molecular chaperonesEukaryotic cytosolThermophilic archaebacteriumPolypeptide 1Ubiquitous eukaryotic proteinThermophilic factor 55Homo-oligomeric complexesMajor heat shock proteinsHeat shock proteinsChaperone componentsEukaryotic proteinsEssential proteinsProtein TAbundant proteinsSulfolobus shibataeComplex bindsS. shibataeChaperonesPrimary structureTF55ChaperoninProteinArchaebacteriaTCP1