2004
Human disorders of ubiquitination and proteasomal degradation
Jiang YH, Beaudet AL. Human disorders of ubiquitination and proteasomal degradation. Current Opinion In Pediatrics 2004, 16: 419-426. PMID: 15273504, DOI: 10.1097/01.mop.0000133634.79661.cd.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAngelman SyndromeAnimalsFanconi AnemiaGenetic Diseases, InbornGenetic Predisposition to DiseaseHumansNF-kappa BPolyendocrinopathies, AutoimmuneProteasome Endopeptidase ComplexUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUbiquitinsVon Hippel-Lindau DiseaseConceptsProteasomal degradationProteasomal subunitsAdditional functional classesUbiquitin E3 ligaseAutosomal recessive juvenile Parkinson's diseaseUbiquitin signalingE3 ligasesUbiquitin pathwayGenetic inborn errorsUbiquitin genesE3 ligaseSubcellular localizationUbiquitinationRelated proteinsMultiple functional defectsRelevant genesHuman disordersCongenital polycythemiaRegulatory signalingFanconi anemiaGenetic classesOvarian cancer susceptibilityFunctional classificationProteolytic degradationUbiquitin
1999
Mutation of the E6-AP Ubiquitin Ligase Reduces Nuclear Inclusion Frequency While Accelerating Polyglutamine-Induced Pathology in SCA1 Mice
Cummings C, Reinstein E, Sun Y, Antalffy B, Jiang Y, Ciechanover A, Orr H, Beaudet A, Zoghbi H. Mutation of the E6-AP Ubiquitin Ligase Reduces Nuclear Inclusion Frequency While Accelerating Polyglutamine-Induced Pathology in SCA1 Mice. Neuron 1999, 24: 879-892. PMID: 10624951, DOI: 10.1016/s0896-6273(00)81035-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxin-1AtaxinsCell NucleusCells, CulturedCysteine EndopeptidasesFluorescent Antibody TechniqueHeLa CellsHumansImmunoblottingImmunohistochemistryInclusion BodiesLigasesMiceMice, KnockoutMicroscopy, ConfocalMultienzyme ComplexesMutationNerve Tissue ProteinsNuclear ProteinsPeptidesPhenotypePlasmidsProteasome Endopeptidase ComplexPurkinje CellsSpinocerebellar DegenerationsUbiquitin-Protein LigasesUbiquitinsConceptsMutant ataxin-1Ataxin-1Spinocerebellar ataxia type 1Ataxin-1 aggregationUbiquitin-protein ligaseUbiquitin-positive nuclear inclusionsUbiquitin-proteasome pathwayNuclear inclusionsPolyglutamine proteinsProteasomal degradationProteasome distributionMutant formsSCA1 pathogenesisAtaxia type 1Patient neuronsPurkinje cell pathologySCA1 miceCell pathologyInclusion frequencyCellsLigasePurkinje cellsProteinGenetics of Angelman Syndrome
Jiang Y, Lev-Lehman E, Bressler J, Tsai T, Beaudet A. Genetics of Angelman Syndrome. American Journal Of Human Genetics 1999, 65: 1-6. PMID: 10364509, PMCID: PMC1378067, DOI: 10.1086/302473.Peer-Reviewed Original Research
1997
De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome
Matsuura T, Sutcliffe J, Fang P, Galjaard R, Jiang Y, Benton C, Rommens J, Beaudet A. De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome. Nature Genetics 1997, 15: 74-77. PMID: 8988172, DOI: 10.1038/ng0197-74.Peer-Reviewed Original ResearchConceptsGene productsAngelman syndromeNovo truncating mutationsUbiquitin protein ligase geneUbiquitin-dependent proteolytic pathwayE6-AP ubiquitin-protein ligaseHuman genetic disordersUbiquitin-protein ligaseUBE3A geneTruncating mutationsEvidence of expressionUnlikely candidate geneGenetic disordersLigase geneParental allelesAS genesHuman chromosomesPaternal uniparental disomyCandidate genesDe novo truncating mutationsProteolytic pathwayNovo nonsense mutationGenesIntragenic mutationsMolecular defects