2011
Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier
Van der Veen AG, Schorpp K, Schlieker C, Buti L, Damon JR, Spooner E, Ploegh HL, Jentsch S. Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 1763-1770. PMID: 21209336, PMCID: PMC3033243, DOI: 10.1073/pnas.1014402108.Peer-Reviewed Original ResearchConceptsProtein modifiersLysine residuesMammalian cellsUbiquitin-like protein Urm1Cellular apoptosis susceptibility proteinC-terminal glycine residueSpecific lysine residuesUb-like modifiersCovalent peptide bondPeroxiredoxin Ahp1Protein urmylationSusceptibility proteinUrm1S. cerevisiaeTarget proteinsGlycine residueThioester intermediateUnique substrateAdditional roleUrmylationAhp1Sulfur carrierOxidant treatmentResiduesDual role
2008
A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway
Schlieker CD, Van der Veen AG, Damon JR, Spooner E, Ploegh HL. A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 18255-18260. PMID: 19017811, PMCID: PMC2584574, DOI: 10.1073/pnas.0808756105.Peer-Reviewed Original Research
2005
A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae
Schlieker C, Korbel GA, Kattenhorn LM, Ploegh HL. A Deubiquitinating Activity Is Conserved in the Large Tegument Protein of the Herpesviridae. Journal Of Virology 2005, 79: 15582-15585. PMID: 16306630, PMCID: PMC1316044, DOI: 10.1128/jvi.79.24.15582-15585.2005.Peer-Reviewed Original Research