2020
Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex
Wu X, Siggel M, Ovchinnikov S, Mi W, Svetlov V, Nudler E, Liao M, Hummer G, Rapoport TA. Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex. Science 2020, 368 PMID: 32327568, PMCID: PMC7380553, DOI: 10.1126/science.aaz2449.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCryoelectron MicroscopyEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationMembrane GlycoproteinsMembrane ProteinsMolecular Dynamics SimulationMultiprotein ComplexesProtein DomainsProtein FoldingProteolysisSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesConceptsHrd1 complexLuminal endoplasmic reticulum proteinsCryo-electron microscopy analysisHrd1 ubiquitin ligaseEndoplasmic reticulum proteinER membraneUbiquitin ligaseProtein degradationStructural basisReticulum proteinsPolypeptide loopMembrane regionsLateral gateLuminal binding sitesBinding sitesLuminal cavityForm twoYos9RetrotranslocationERADMicroscopy analysisSubcomplexLigaseHRD1Proteasome
2006
Uncoupling protein 2/3 immunoreactivity and the ascending dopaminergic and noradrenergic neuronal systems: Relevance for volume transmission
Rivera A, Agnati LF, Horvath TL, Valderrama JJ, de La Calle A, Fuxe K. Uncoupling protein 2/3 immunoreactivity and the ascending dopaminergic and noradrenergic neuronal systems: Relevance for volume transmission. Neuroscience 2006, 137: 1447-1461. PMID: 16387447, DOI: 10.1016/j.neuroscience.2005.05.051.Peer-Reviewed Original ResearchConceptsConfocal laser microscopy analysisReactive oxygen species productionLaser microscopy analysisProtein 2/3Oxygen species productionUncouple oxidative phosphorylationOxidative phosphorylationATP synthesisProteinSpecies productionDouble immunolabelingImportant roleMicroscopy analysisPhosphorylationMitochondriaRegulationCell groupsPlastic changesLocalizationIslandsAnimal modelsMagnaTyrosine hydroxylaseNeuronal systems
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