2019
Methodologies to monitor protein turnover at the inner nuclear membrane
Tsai PL, Zhao C, Schlieker C. Methodologies to monitor protein turnover at the inner nuclear membrane. Methods In Enzymology 2019, 619: 47-69. PMID: 30910029, PMCID: PMC6457266, DOI: 10.1016/bs.mie.2018.12.033.Peer-Reviewed Original ResearchConceptsLamin B receptorNuclear envelopeInner nuclear membrane proteinProtein turnoverProtein quality control pathwaysNuclear membrane proteinsQuality control pathwaysProtein turnover machineryHuman congenital disordersInner nuclear membraneSubcellular fractionation methodMammalian nuclear envelopeLive-cell imagingC-terminal truncationsNuclear laminaMembrane proteinsModel substrateBiochemical approachesNuclear compartmentActivity essentialControl pathwaysNuclear membraneRapid turnoverCholesterol biosynthesisCell imaging
2015
A designed repeat protein as an affinity capture reagent.
Speltz EB, Brown RS, Hajare HS, Schlieker C, Regan L. A designed repeat protein as an affinity capture reagent. Biochemical Society Transactions 2015, 43: 874-80. PMID: 26517897, PMCID: PMC5683849, DOI: 10.1042/bst20150091.Peer-Reviewed Original ResearchConceptsProtein-peptide interactionsAffinity capture reagentsSupramolecular arraysNovel reagentCapture reagentPractical applicationsReagentsProtein engineeringGeneral utilityAffinity purificationRational fashionProtein interactionsAttractive targetInteractionImportant practical applicationsPurification
2011
Enzymatic Blockade of the Ubiquitin-Proteasome Pathway
Ernst R, Claessen JH, Mueller B, Sanyal S, Spooner E, van der Veen AG, Kirak O, Schlieker CD, Weihofen WA, Ploegh HL. Enzymatic Blockade of the Ubiquitin-Proteasome Pathway. PLOS Biology 2011, 8: e1000605. PMID: 21468303, PMCID: PMC3066133, DOI: 10.1371/journal.pbio.1000605.Peer-Reviewed Original Research
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
2007
A Functional Ubiquitin-Specific Protease Embedded in the Large Tegument Protein (ORF64) of Murine Gammaherpesvirus 68 Is Active during the Course of Infection
Gredmark S, Schlieker C, Quesada V, Spooner E, Ploegh HL. A Functional Ubiquitin-Specific Protease Embedded in the Large Tegument Protein (ORF64) of Murine Gammaherpesvirus 68 Is Active during the Course of Infection. Journal Of Virology 2007, 81: 10300-10309. PMID: 17634221, PMCID: PMC2045495, DOI: 10.1128/jvi.01149-07.Peer-Reviewed Original ResearchConceptsLarge tegument proteinTegument proteinsMHV-68-infected cellsCysteine protease domainUbiquitin-specific proteaseAmino-terminal segmentActive site-directed probesActivity-based profilingDeubiquitinating proteaseEnzymatic functionSite-directed probesProtease domainBetaherpesvirus familyProteinORF64Murine gammaherpesvirus 68Tandem mass spectrometryProteaseGammaherpesvirus 68Course of infectionMass spectrometryHerpes simplex virus type 1Simplex virus type 1CellsUL36