1996
5 Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol
Willison K, Horwich A. 5 Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol. 1996, 107-136. DOI: 10.1016/b978-012237455-5/50006-3.Peer-Reviewed Original ResearchChaperonin-containing TCP-1Eukaryotic cytosolEukaryotic cellsTCP-1Protein foldingUnfolded proteinsChaperoninCytoskeletal proteinsSubunit speciesFunctional analysisGeneral functionProteinArchaebacteriaGeneral affinityCytosolFoldingSpecific affinityGenesSpeciesAffinityActinTubulinFunctionCellsUnusual type
1988
The processing peptidase of yeast mitochondria: the two co‐operating components MPP and PEP are structurally related.
Pollock R, Hartl F, Cheng M, Ostermann J, Horwich A, Neupert W. The processing peptidase of yeast mitochondria: the two co‐operating components MPP and PEP are structurally related. The EMBO Journal 1988, 7: 3493-3500. PMID: 3061797, PMCID: PMC454850, DOI: 10.1002/j.1460-2075.1988.tb03225.x.Peer-Reviewed Original ResearchConceptsMitochondrial processing peptidaseMitochondrial precursor proteinsProcessing peptidasePrecursor proteinMutant of SaccharomycesRemarkable sequence similarityYeast mitochondriaMPP geneSequence similarityHydrophilic proteinNovel peptidaseAmino acidsProteolytic cleavageProteinPeptidaseMutantsMitochondriaCommon originPresequenceSaccharomycesPEPGenesMutationsCleavageFunction