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
Chaperone rings in protein folding and degradation
Horwich A, Weber-Ban E, Finley D. Chaperone rings in protein folding and degradation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 11033-11040. PMID: 10500119, PMCID: PMC34237, DOI: 10.1073/pnas.96.20.11033.Peer-Reviewed Original ResearchConceptsSubstrate proteinsNon-native formsProcess of foldingCellular proteinsDegradation chamberProtein foldingStep of recognitionProteolytic complexRing assemblyDivergent fatesConformational changesNative stateProteinChaperoninFoldingCentral cavityCooperative interactionsATPPolypeptideFateChaperonesCompartmentalizationVital roleMotifProtease