1998
Maturation of Human Cyclin E Requires the Function of Eukaryotic Chaperonin CCT
Won K, Schumacher R, Farr G, Horwich A, Reed S. Maturation of Human Cyclin E Requires the Function of Eukaryotic Chaperonin CCT. Molecular And Cellular Biology 1998, 18: 7584-7589. PMID: 9819444, PMCID: PMC109339, DOI: 10.1128/mcb.18.12.7584.Peer-Reviewed Original ResearchConceptsHuman cyclin EChaperonin CCTCyclin EEukaryotic cytosolic chaperonin CCTCytosolic chaperonin CCTEukaryotic chaperonin CCTLarge oligomeric assembliesYeast-based screenG1/S phase transitionCyclin-dependent kinase CDK2ATP-dependent processS phase transitionCCT complexPresence of ATPProteasomal actionCCT functionHuman proteinsKinase CDK2Oligomeric assembliesHuman cellsNative stateCDK2ProteinMaturationBiogenesisFolding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
Kim S, Schilke B, Craig E, Horwich A. Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12860-12865. PMID: 9789005, PMCID: PMC23633, DOI: 10.1073/pnas.95.22.12860.Peer-Reviewed Original ResearchConceptsOrnithine transcarbamoylaseYeast cytosolic enzymesCytosolic enzymeNative stateCytosolic Hsp70 proteinsGalpha transducinCytosolic chaperoninEukaryotic cytosolYeast Hsp70Chaperone actionPosttranslational mannerYeast cytosolCytosolic proteinsHSP70 proteinHomotrimeric enzymeProteinSpecific activity
1993
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
Horwich A, Low K, Fenton W, Hirshfield I, Furtak K. Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL. Cell 1993, 74: 909-917. PMID: 8104102, DOI: 10.1016/0092-8674(93)90470-b.Peer-Reviewed Original ResearchMeSH KeywordsATP-Binding Cassette TransportersBacterial ProteinsBacteriophage lambdaCarrier ProteinsChaperonin 60Citrate (si)-SynthaseEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsKetoglutarate Dehydrogenase ComplexMaltoseMaltose-Binding ProteinsMethionineMonosaccharide Transport ProteinsOperonOrnithine CarbamoyltransferasePlasmidsPolyribonucleotide NucleotidyltransferasePromoter Regions, GeneticProtein BiosynthesisProtein FoldingProtein Sorting SignalsSequence DeletionTemperatureTransduction, GeneticConceptsCytoplasmic proteinsTemperature-sensitive lethal mutationBacterial cytoplasmic proteinsE. coli chaperonin GroELMaltose-binding proteinRole of GroELNative tertiary structureEssential genesChaperonin GroELBacterial cytoplasmMutant cellsLethal mutationsNonpermissive temperatureGenetic informationPolynucleotide phosphorylaseGeneral translationTertiary structureCitrate synthasePathways of transferKetoglutarate dehydrogenaseGeneral roleGroELNative conformationProteinTest proteins
1992
TCP1 complex is a molecular chaperone in tubulin biogenesis
Yaffe M, Farr G, Miklos D, Horwich A, Sternlicht M, Sternlicht H. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 1992, 358: 245-248. PMID: 1630491, DOI: 10.1038/358245a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCycloheximideDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsKineticsMacromolecular SubstancesMicrotubule-Associated ProteinsMolecular WeightNuclear ProteinsProtein BiosynthesisProtein ConformationRabbitsReticulocytesRNA, MessengerT-Complex Genome RegionTubulinUbiquitin-Protein LigasesConceptsReticulocyte lysateTubulin subunitsCytosol of eukaryotesComplex polypeptide 1Protease-sensitive conformationRabbit reticulocyte lysateCytosolic chaperonesTubulin biogenesisMajor cytosolic proteinMolecular chaperonesTCP1 complexK proteinCytosolic proteinsΒ heterodimerBiogenesisPolypeptide 1Β-tubulinProteinSubunitsChaperonesMg-ATPK-complexesMolecular targetsNonhydrolysable analogueTubulin
1987
The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge.
Horwich A, Kalousek F, Fenton W, Furtak K, Pollock R, Rosenberg L. The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge. Journal Of Cell Biology 1987, 105: 669-677. PMID: 3624306, PMCID: PMC2114782, DOI: 10.1083/jcb.105.2.669.Peer-Reviewed Original Research
1985
A leader peptide is sufficient to direct mitochondrial import of a chimeric protein.
Horwich A, Kalousek F, Mellman I, Rosenberg L. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. The EMBO Journal 1985, 4: 1129-1135. PMID: 3891325, PMCID: PMC554314, DOI: 10.1002/j.1460-2075.1985.tb03750.x.Peer-Reviewed Original ResearchConceptsChimeric precursor proteinsMitochondrial importLeader peptideChimeric precursorsDihydrofolate reductaseMost mitochondrial proteinsPost-translational importMutant CHO cell linesCloned nucleotide sequencePrecursor proteinOrnithine transcarbamylaseCell-free systemCHO cell linesEnzyme dihydrofolate reductaseMitochondrial proteinsMitochondrial localizationRegulatory elementsLeader sequenceNucleotide sequenceStable transformantsAdditional proteinsSelectable markerChimeric proteinLarger precursorIntact cells
1984
Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase
Horwich A, Fenton W, Williams K, Kalousek F, Kraus J, Doolittle R, Konigsberg W, Rosenberg L. Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase. Science 1984, 224: 1068-1074. PMID: 6372096, DOI: 10.1126/science.6372096.Peer-Reviewed Original ResearchConceptsComplementary DNALeader peptideOrnithine transcarbamylaseAmino-terminal leader peptideMost mitochondrial proteinsComplete primary structureHuman ornithine transcarbamylaseFree cytoplasmic ribosomesMitochondrial matrix enzymeCultured HeLa cellsMitochondrial proteinsCytoplasmic ribosomesRegulatory elementsNucleotide sequenceStable transformantsMatrix enzymeAsparagine residuesAcidic residuesLarger precursorMature formPrimary structureProtein occursHeLa cellsEscherichia coliAmino acids
1983
Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase.
Horwich A, Kraus J, Williams K, Kalousek F, Konigsberg W, Rosenberg L. Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 4258-4262. PMID: 6576335, PMCID: PMC384016, DOI: 10.1073/pnas.80.14.4258.Peer-Reviewed Original ResearchConceptsOrnithine transcarbamoylaseSequential Edman analysesCDNA probeMitochondrial matrix enzymeInsertion of cDNAAmino acid residuesConsecutive amino acid residuesCarboxyl-terminal portionCytoplasmic polysomesMolecular cloningCDNA clonesEdman analysisDifferential colony hybridizationTranslation assaysX chromosomeCDNA codingMatrix enzymeEnzyme subunitMessenger speciesAcid residuesSequence presentPolysome immunoadsorptionIdentical subunitsColony hybridizationEscherichia coli