2016
Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study
Laudermilch E, Tsai PL, Graham M, Turner E, Zhao C, Schlieker C. Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study. Molecular Biology Of The Cell 2016, 27: 3964-3971. PMID: 27798237, PMCID: PMC5156537, DOI: 10.1091/mbc.e16-07-0511.Peer-Reviewed Original ResearchConceptsTorsin ATPasesNuclear envelopeNuclear pore complex biogenesisComplex biogenesisRegulatory cofactorsValuable experimental platformHuman genomeCRISPR/Observed phenotypeGenetic studiesFunctional linkATPasesCofactor functionElectron microscopy tomographyImmunogold labelingPhenotypic measuresCell linesCofactor systemBleb structuresBleb formationTOR2ANucleoporinsLULL1BiogenesisGenome
2009
The Otubain YOD1 Is a Deubiquitinating Enzyme that Associates with p97 to Facilitate Protein Dislocation from the ER
Ernst R, Mueller B, Ploegh HL, Schlieker C. The Otubain YOD1 Is a Deubiquitinating Enzyme that Associates with p97 to Facilitate Protein Dislocation from the ER. Molecular Cell 2009, 36: 28-38. PMID: 19818707, PMCID: PMC2774717, DOI: 10.1016/j.molcel.2009.09.016.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAlpha 1-AntitrypsinCarrier ProteinsCatalytic DomainCell Cycle ProteinsCell LineEndopeptidasesEndoplasmic ReticulumHumansMembrane ProteinsPoint MutationProteasome Endopeptidase ComplexProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein TransportReceptors, Antigen, T-Cell, alpha-betaThiolester HydrolasesTransfectionUbiquitinUbiquitinationValosin Containing ProteinZinc FingersConceptsZinc finger domainOvarian tumor (OTU) familyDominant negative effectMisfolded proteinsMultiprotein complexesFinger domainMammalian cellsDislocation substratesProtein dislocationC-terminusEndoplasmic reticulumFunctional linkYOD1P97Core domainEnzymeUbxTumor familyTerminusCytosolDomainProteinReticulumPathwayRole