2016
Spider Silk Peptide Is a Compact, Linear Nanospring Ideal for Intracellular Tension Sensing
Brenner MD, Zhou R, Conway DE, Lanzano L, Gratton E, Schwartz MA, Ha T. Spider Silk Peptide Is a Compact, Linear Nanospring Ideal for Intracellular Tension Sensing. Nano Letters 2016, 16: 2096-2102. PMID: 26824190, PMCID: PMC4851340, DOI: 10.1021/acs.nanolett.6b00305.Peer-Reviewed Original ResearchConceptsSingle-molecule fluorescence-force spectroscopyFluorescence-force spectroscopyFluorescence resonance energy transferResonance energy transferRodlike structureSensor constructsShort peptidesIndividual chainsAccessible forcesEnergy transferSilk peptideCell imagingSpider silk proteinsBiological systemsRemarkable elasticitySilk proteinsFRETPN.PeptidesSpider silkPolymersSpectroscopyRecent developmentsForce sensitivityWide range
2015
Coordinated Regulation of Vasopressin Inactivation and Glucose Uptake by Action of TUG Protein in Muscle*
Habtemichael EN, Alcázar-Román A, Rubin BR, Grossi LR, Belman JP, Julca O, Löffler MG, Li H, Chi NW, Samuel VT, Bogan JS. Coordinated Regulation of Vasopressin Inactivation and Glucose Uptake by Action of TUG Protein in Muscle*. Journal Of Biological Chemistry 2015, 290: 14454-14461. PMID: 25944897, PMCID: PMC4505512, DOI: 10.1074/jbc.c115.639203.Peer-Reviewed Original ResearchConceptsInsulin-regulated aminopeptidaseVesicle translocationGLUT4 intracellular retentionGlucose uptakeT-tubule fractionTransgenic miceTransmembrane aminopeptidaseAQP2 water channelsTUG ProteinCoordinated regulationGLUT4 translocationInsulin stimulationPhysiological importanceGlucose transporterProteolytic processingIntracellular retentionTranslocationWater homeostasisMuscle cellsGLUT4Skeletal muscleShort peptidesProteolysisProteinAbundance
2014
Identification of small ORFs in vertebrates using ribosome footprinting and evolutionary conservation
Bazzini AA, Johnstone TG, Christiano R, Mackowiak SD, Obermayer B, Fleming ES, Vejnar CE, Lee MT, Rajewsky N, Walther TC, Giraldez AJ. Identification of small ORFs in vertebrates using ribosome footprinting and evolutionary conservation. The EMBO Journal 2014, 33: 981-993. PMID: 24705786, PMCID: PMC4193932, DOI: 10.1002/embj.201488411.Peer-Reviewed Original Research
1996
UBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser M. UBIQUITIN-DEPENDENT PROTEIN DEGRADATION. Annual Review Of Genetics 1996, 30: 405-439. PMID: 8982460, DOI: 10.1146/annurev.genet.30.1.405.Peer-Reviewed Original ResearchConceptsRegulatory mechanismsUbiquitin-dependent protein degradationLarge enzyme familyAttachment of ubiquitinCellular regulatory mechanismsSignal transduction pathwaysHigh substrate specificityReceptor-mediated endocytosisPolypeptide ubiquitinProtein ubiquitinationUbiquitin systemTransduction pathwaysEnzyme familyUbiquitinated proteinsSubstrate specificityProtein modificationProtein degradationCell cycleProteasomeUbiquitinationKey transitionsUbiquitinShort peptidesProteinDeubiquitinationAmyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*
Desdouits F, Buxbaum J, Desdouits-Magnen J, Nairn A, Greengard P. Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*. Journal Of Biological Chemistry 1996, 271: 24670-24674. PMID: 8798734, DOI: 10.1074/jbc.271.40.24670.Peer-Reviewed Original ResearchConceptsProtein kinase CAction of PKCCell-free systemIntact cellsKinase CProtein phosphatase calcineurinCell-permeant inhibitorStimulation of PKCSpecific peptide inhibitorPhosphatase calcineurinMolecular mechanismsCalcineurinPeptide inhibitorRegulationShort peptidesCalmodulinCellsBeta peptideInhibitorsPeptide formationPeptidesMajor constituentsPronounced inhibitionCyclosporin ASingle substrate
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