1999
The Biology of pro-Thyrotropin-Releasing Hormone-Derived Peptides*
Nillni E, Sevarino K. The Biology of pro-Thyrotropin-Releasing Hormone-Derived Peptides*. Endocrine Reviews 1999, 20: 599-648. PMID: 10529897, DOI: 10.1210/edrv.20.5.0379.Peer-Reviewed Original Research
1993
Identification of the thyrotropin-releasing hormone-prohormone and its posttranslational processing in a transfected AtT20 tumoral cell line.
Nillni E, Sevarino K, Jackson I. Identification of the thyrotropin-releasing hormone-prohormone and its posttranslational processing in a transfected AtT20 tumoral cell line. Endocrinology 1993, 132: 1260-70. PMID: 8440187, DOI: 10.1210/endo.132.3.8440187.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBlotting, WesternElectrophoresis, Polyacrylamide GelKineticsMiceModels, GeneticMolecular Sequence DataMolecular WeightPeptide FragmentsPituitary NeoplasmsProtein PrecursorsProtein Processing, Post-TranslationalPyrrolidonecarboxylic AcidThyrotropin-Releasing HormoneTransfectionTrypsinTumor Cells, Cultured
1989
Thyrotropin-releasing hormone (TRH) precursor processing Characterization of mature TRH and non-TRH peptides synthesized by transfected mammalian cells*
Sevarino K, Goodman R, Spiess J, Jackson I, Wu P. Thyrotropin-releasing hormone (TRH) precursor processing Characterization of mature TRH and non-TRH peptides synthesized by transfected mammalian cells*. Journal Of Biological Chemistry 1989, 264: 21529-21535. PMID: 2513321, DOI: 10.1016/s0021-9258(20)88217-9.Peer-Reviewed Original Research
1984
The nuclear-coded subunits of yeast cytochrome c oxidase. I. Fractionation of the holoenzyme into chemically pure polypeptides and the identification of two new subunits using solvent extraction and reversed phase high performance liquid chromatography.
Power S, Lochrie M, Sevarino K, Patterson T, Poyton R. The nuclear-coded subunits of yeast cytochrome c oxidase. I. Fractionation of the holoenzyme into chemically pure polypeptides and the identification of two new subunits using solvent extraction and reversed phase high performance liquid chromatography. Journal Of Biological Chemistry 1984, 259: 6564-6570. PMID: 6327684, DOI: 10.1016/s0021-9258(20)82178-4.Peer-Reviewed Original Research
1980
PROTEIN PRECURSORS IN THE ASSEMBLY OF YEAST CYTOCHROME c OXIDASE, A TRANSMEMBRANOUS OLIGOMER OF THE INNER MITOCHONDRIAL MEMBRANE*
Poyton R, Sevarino K, George‐Nascimento C, Power S. PROTEIN PRECURSORS IN THE ASSEMBLY OF YEAST CYTOCHROME c OXIDASE, A TRANSMEMBRANOUS OLIGOMER OF THE INNER MITOCHONDRIAL MEMBRANE*. Annals Of The New York Academy Of Sciences 1980, 343: 275-292. PMID: 6249163, DOI: 10.1111/j.1749-6632.1980.tb47258.x.Peer-Reviewed Original ResearchMitochondrial membrane biogenesis: identification of a precursor to yeast cytochrome c oxidase subunit II, an integral polypeptide.
Sevarino K, Poyton R. Mitochondrial membrane biogenesis: identification of a precursor to yeast cytochrome c oxidase subunit II, an integral polypeptide. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 142-146. PMID: 6244538, PMCID: PMC348224, DOI: 10.1073/pnas.77.1.142.Peer-Reviewed Original ResearchConceptsMitochondrial translation productsInner mitochondrial membraneTranslation productsMitochondrial membraneIntegral polypeptidesCytochrome c oxidase subunit IIMitochondrial translation systemOligomeric enzyme complexesAurintricarboxylic acidNH2-terminal extensionCytochrome c oxidaseYeast mitochondriaInner membraneLeader sequenceSubunit IIEnzyme complexLarger precursorC oxidaseUnprocessed formPolypeptideTranslation systemMembraneTransient precursorNormal conditionsRibosomes