1995
Cloning and characterization of chi-1: a developmentally regulated member of a novel class of the ionotropic glutamate receptor family
Ciabarra A, Sullivan J, Gahn L, Pecht G, Heinemann S, Sevarino K. Cloning and characterization of chi-1: a developmentally regulated member of a novel class of the ionotropic glutamate receptor family. Journal Of Neuroscience 1995, 15: 6498-6508. PMID: 7472412, PMCID: PMC6577996, DOI: 10.1523/jneurosci.15-10-06498.1995.Peer-Reviewed Original ResearchConceptsAgonist-activated currentsGlutamate receptor subunitsIonotropic glutamate receptor familyGlutamate receptor familyReceptor subunitsReceptor familyPostnatal day 1First postnatal weekNMDA receptor subunitsFunctional NMDA receptorsIonotropic glutamate receptorsSpinal cordCA1 fieldHeteromeric configurationsNMDA receptorsGlutamate receptorsPostnatal weekNMDA subunitsDay 1Functional expression studiesNeuronal signalingPrecise roleReceptorsTranscript levelsXenopus oocytes
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 ResearchAmino-terminal sequences of prosomatostatin direct intracellular targeting but not processing specificity
Sevarino K, Stork P, Ventimiglia R, Mandel G, Goodman R. Amino-terminal sequences of prosomatostatin direct intracellular targeting but not processing specificity. Cell 1989, 57: 11-19. PMID: 2564811, DOI: 10.1016/0092-8674(89)90167-0.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal CortexAmino Acid SequenceAnimalsCell LineFishesInsulinomaIslets of LangerhansMiceProtein PrecursorsRatsSomatostatinTransfectionConceptsEndocrine cell linesRat preprosomatostatinCarboxy-terminal thirdDistinct cell typesAmino-terminal sequenceCell linesHybrid proteinLeader sequenceIntracellular targetingRegulated pathwayPreprosomatostatin 1Cellular factorsExpression vectorCell typesPattern of processingProcessing siteBioactive peptidesAnglerfish isletsSequenceDifferential processingPeptidesProteinResiduesPathwayHigh levelsCharacterization and Expression of the Gene‐Encoding Rat Thyrotropin‐Releasing Hormone (TRH)
LEE S, SEVARINO K, ROOS B, GOODMAN R. Characterization and Expression of the Gene‐Encoding Rat Thyrotropin‐Releasing Hormone (TRH). Annals Of The New York Academy Of Sciences 1989, 553: 14-28. PMID: 2497670, DOI: 10.1111/j.1749-6632.1989.tb54475.x.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernBlotting, SouthernBrainCloning, MolecularDNAEnhancer Elements, GeneticGenesMolecular Sequence DataOrgan SpecificityPromoter Regions, GeneticProtein PrecursorsRatsRecombinant Fusion ProteinsRestriction MappingRNA, MessengerThyrotropin-Releasing HormoneTransfection
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