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http://purl.uniprot.org/citations/30004689http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30004689http://www.w3.org/2000/01/rdf-schema#comment"This study investigated the enzyme-substrate interaction between Saccharomyces cerevisiae arginine methyltransferase Hmt1p and nucleolar protein Npl3p, using chemical cross linking/mass spectrometry (XL/MS). We show that XL/MS can capture transient interprotein interactions that occur during the process of methylation, involving a disordered region in Npl3p with tandem SRGG repeats, and we confirm that Hmt1p and Npl3p exist as homomultimers. Additionally, the study investigated the interdependencies between variables of an XL/MS experiment that lead to the identification of identical or different cross-linked peptides. We report that there are substantial benefits, in terms of biologically relevant cross-links identified, that result from the use of two mass-spectrometry-cleavable cross-linkers [disuccinimido sulfoxide (DSSO) and disuccinimido dibutyric urea (DSBU)], two fragmentation approaches [collision-induced dissociation and electron-transfer dissociation (CID+ETD)] and stepped high-energy collision dissociation (HCD)], and two programs (MeroX and XlinkX). We also show that there are specific combinations of XL/MS methods that are more successful than others for the two proteins investigated here; these are explored in detail in the text. Data are available via ProteomeXchange with identifier PXD008348."xsd:string
http://purl.uniprot.org/citations/30004689http://purl.org/dc/terms/identifier"doi:10.1021/acs.analchem.8b01525"xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/author"Smith D.L."xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/author"Wilkins M.R."xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/author"Hart-Smith G."xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/author"Gotze M."xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/author"Bartolec T.K."xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/name"Anal Chem"xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/pages"9101-9108"xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/title"Characterization of the Interaction between Arginine Methyltransferase Hmt1 and Its Substrate Npl3: Use of Multiple Cross-Linkers, Mass Spectrometric Approaches, and Software Platforms."xsd:string
http://purl.uniprot.org/citations/30004689http://purl.uniprot.org/core/volume"90"xsd:string
http://purl.uniprot.org/citations/30004689http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30004689
http://purl.uniprot.org/citations/30004689http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30004689
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http://purl.uniprot.org/uniprot/P38074http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30004689
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