2019
De Novo Missense Variants in FBXW11 Cause Diverse Developmental Phenotypes Including Brain, Eye, and Digit Anomalies
Holt RJ, Young RM, Crespo B, Ceroni F, Curry CJ, Bellacchio E, Bax DA, Ciolfi A, Simon M, Fagerberg CR, van Binsbergen E, De Luca A, Memo L, Dobyns WB, Mohammed AA, Clokie SJH, Seco C, Jiang YH, Sørensen KP, Andersen H, Sullivan J, Powis Z, Chassevent A, Smith-Hicks C, Petrovski S, Antoniadi T, Shashi V, Gelb BD, Wilson SW, Gerrelli D, Tartaglia M, Chassaing N, Calvas P, Ragge NK. De Novo Missense Variants in FBXW11 Cause Diverse Developmental Phenotypes Including Brain, Eye, and Digit Anomalies. American Journal Of Human Genetics 2019, 105: 640-657. PMID: 31402090, PMCID: PMC6731360, DOI: 10.1016/j.ajhg.2019.07.005.Peer-Reviewed Original ResearchConceptsF-box (SCF) ubiquitin ligase complexF-box proteinsMultiple developmental processesPectoral fin developmentSubstrate-binding domainUbiquitin ligase complexGli transcription factorsHuman developmental disordersSecond-generation sequencingDe novo missense variantsWhole-genome sequencingSkp1-CullinDevelopmental phenotypesLigase complexFin developmentResidue clustersTranscription factorsProteasomal degradationEye developmentNovo missense variantsDevelopmental processesFBXW11Genome sequencingEmbryonic tissuesUnderdeveloped eyes
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 cellsProtein