2025
Neuroendocrine Properties of the Ciliary Epithelium
Coca-Prados M. Neuroendocrine Properties of the Ciliary Epithelium. 2025, 130-145. DOI: 10.1016/b978-0-443-13820-1.00083-9.Peer-Reviewed Original ResearchGene expressionExpression of bioactive peptidesIdentity of genesGene expression of enzymesMicroarray-based analysisExpression of enzymesSensor proteinsRegulate metabolismGenesPhysiological processesCiliary epitheliumPhysiological functionsT4 to T3Neuronal Ca2Neuroendocrine propertiesVasoconstrictive functionVasoactive aminesPeptide receptorBioactive peptidesIon channelsMetabolismPeptideEyesEnzymeProtein
2010
Neuroendocrine Properties of the Ciliary Epithelium
Coca-Prados M. Neuroendocrine Properties of the Ciliary Epithelium. 2010, 107-112. DOI: 10.1016/b978-0-12-374203-2.00088-9.Peer-Reviewed Original ResearchCiliary epitheliumAqueous humorOcular hypotensive actionSame embryological originRetinal pigment epitheliumEye aqueous humorOcular ciliary epitheliumHypotensive actionAqueous humor secretionAnterior segmentEndocrine factorsPigment epitheliumNeuroendocrine propertiesEndocrine systemEmbryological originNeuroepithelial cellsEpitheliumAvascular tissueNeuropeptidesBioactive peptidesCellsCell communicationRetinaHormoneSecretion
2009
Aminopeptidase Fingerprints, an Integrated Approach for Identification of Good Substrates and Optimal Inhibitors*
Drag M, Bogyo M, Ellman JA, Salvesen GS. Aminopeptidase Fingerprints, an Integrated Approach for Identification of Good Substrates and Optimal Inhibitors*. Journal Of Biological Chemistry 2009, 285: 3310-3318. PMID: 19948737, PMCID: PMC2823418, DOI: 10.1074/jbc.m109.060418.Peer-Reviewed Original ResearchConceptsSubstrate specificityAminopeptidase NS1 pocketN-terminal amino acidsAmino acid substratesCell surface proteaseTypes of proteasesProteolytic eventsCell survivalRat orthologAcid substratesSurface proteaseSpecific inhibitorAmino acidsSubstrate hydrolysisCell compartmentTarget substrateAminopeptidasesGood substrateOptimal inhibitorSequential cleavageProteaseBioactive peptidesEukaryotesOrthologs
2007
Molecular Basis of Branched Peptides Resistance to Enzyme Proteolysis
Falciani C, Lozzi L, Pini A, Corti F, Fabbrini M, Bernini A, Lelli B, Niccolai N, Bracci L. Molecular Basis of Branched Peptides Resistance to Enzyme Proteolysis. Chemical Biology & Drug Design 2007, 69: 216-221. PMID: 17441908, DOI: 10.1111/j.1747-0285.2007.00487.x.Peer-Reviewed Original ResearchConceptsForm of dendrimersDifferent bioactive peptidesStructure-based hypothesesMass spectrometryUnmodified peptidesMultimeric peptidesProteolytic stabilityBioactive peptidesPressure liquid chromatographyLiquid chromatographyHigh-pressure liquid chromatographyLinear moleculesPeptide copiesEnzyme proteolysisProteolytic resistanceHuman plasmaSame peptideSynthetic peptidesPeptidesDendrimersPeptide resistanceSpectrometryMultimericityChromatographyMolecules
1998
Structure−Function Relationships in Side Chain Lactam Cross-Linked Peptide Models of a Conserved N-Terminal Domain of Apolipoprotein E †
Benzinger T, Braddock D, Dominguez S, Burkoth T, Miller-Auer H, Subramanian R, Fless G, Jones D, Lynn D, Meredith S. Structure−Function Relationships in Side Chain Lactam Cross-Linked Peptide Models of a Conserved N-Terminal Domain of Apolipoprotein E †. Biochemistry 1998, 37: 13222-13229. PMID: 9748329, DOI: 10.1021/bi980482f.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsApolipoproteins ECell LineCircular DichroismConserved SequenceEmbryo, MammalianFibroblastsIodine RadioisotopesLactamsMiceModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryReceptors, LDLStructure-Activity RelationshipConceptsPeptide IVPeptide modelsConformational switchSide chain lactamLipid surfaceSide chainsBioactive peptidesStructural orderMultiple conformationsBiological activityStructure-function relationshipsLactamsAlpha-helixStrategic modificationsSecondary structureHelical segmentsPeptide IIIConformationAlpha-helical segmentsShort alpha helixCOOHHelixAntipodeStructureSolution
1989
Amino-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 ResearchConceptsEndocrine cell linesRat preprosomatostatinCarboxy-terminal thirdDistinct cell typesAmino-terminal sequenceCell linesHybrid proteinLeader sequenceIntracellular targetingRegulated pathwayPreprosomatostatin 1Cellular factorsExpression vectorCell typesPattern of processingProcessing siteBioactive peptidesAnglerfish isletsSequenceDifferential processingPeptidesProteinResiduesPathwayHigh levels
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