Lenz, Christof

[["dc.bibliographiccitation.firstpage","185"],["dc.bibliographiccitation.lastpage","203"],["dc.bibliographiccitation.seriesnr","2228"],["dc.contributor.author","Silbern, Ivan"],["dc.contributor.author","Fang, Pan"],["dc.contributor.author","Ji, Yanlong"],["dc.contributor.author","Christof, Lenz"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Pan, Kuan-Ting"],["dc.contributor.editor","Marcus, Katrin"],["dc.contributor.editor","Eisenacher, Martin"],["dc.contributor.editor","Sitek, Barbara"],["dc.date.accessioned","2021-06-02T10:44:22Z"],["dc.date.available","2021-06-02T10:44:22Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1007/978-1-0716-1024-4_14"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87012"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer US"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-0716-1024-4"],["dc.relation.isbn","978-1-0716-1023-7"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","Quantitative Methods in Proteomics"],["dc.relation.ispartofseries","Methods in Molecular Biology; 2228"],["dc.title","Relative Quantification of Phosphorylated and Glycosylated from the Same Sample Using Isobaric Chemical Labelling with a Two-Step Enrichment Strategy"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Fang, Pan"],["dc.contributor.author","Ji, Yanlong"],["dc.contributor.author","Silbern, Ivan"],["dc.contributor.author","Doebele, Carmen"],["dc.contributor.author","Ninov, Momchil"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Pan, Kuan-Ting"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2021-04-14T08:31:49Z"],["dc.date.available","2021-04-14T08:31:49Z"],["dc.date.issued","2020"],["dc.description.abstract","Regulation of protein N-glycosylation is essential in human cells. However, large-scale, accurate, and site-specific quantification of glycosylation is still technically challenging. We here introduce SugarQuant, an integrated mass spectrometry-based pipeline comprising protein aggregation capture (PAC)-based sample preparation, multi-notch MS3 acquisition (Glyco-SPS-MS3) and a data-processing tool (GlycoBinder) that enables confident identification and quantification of intact glycopeptides in complex biological samples. PAC significantly reduces sample-handling time without compromising sensitivity. Glyco-SPS-MS3 combines high-resolution MS2 and MS3 scans, resulting in enhanced reporter signals of isobaric mass tags, improved detection of N-glycopeptide fragments, and lowered interference in multiplexed quantification. GlycoBinder enables streamlined processing of Glyco-SPS-MS3 data, followed by a two-step database search, which increases the identification rates of glycopeptides by 22% compared with conventional strategies. We apply SugarQuant to identify and quantify more than 5,000 unique glycoforms in Burkitt’s lymphoma cells, and determine site-specific glycosylation changes that occurred upon inhibition of fucosylation at high confidence."],["dc.identifier.doi","10.1038/s41467-020-19052-w"],["dc.identifier.pmid","33077710"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83721"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/59"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A06: Mitochondrienfunktion und -umsatz in Synapsen"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.title","A streamlined pipeline for multiplexed quantitative site-specific N-glycoproteomics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","12584"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Güran, Alican; 1British Heart Foundation Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King’s College London, St Thomas’ Hospital, Westminster Bridge Road, London SE1 7EH, UK; alican.guran@kcl.ac.uk (A.G.); metin.avkiran@kcl.ac.uk (M.A.)"],["dc.contributor.affiliation","Ji, Yanlong; 2Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany; yanlong.ji@mpibpc.mpg.de (Y.J.); pan.fang@mpibpc.mpg.de (P.F.); Kuan-Ting.Pan@kgu.de (K.-T.P.); hurlaub@gwdg.de (H.U.)"],["dc.contributor.affiliation","Fang, Pan; 2Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany; yanlong.ji@mpibpc.mpg.de (Y.J.); pan.fang@mpibpc.mpg.de (P.F.); Kuan-Ting.Pan@kgu.de (K.-T.P.); hurlaub@gwdg.de (H.U.)"],["dc.contributor.affiliation","Pan, Kuan-Ting; 2Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany; yanlong.ji@mpibpc.mpg.de (Y.J.); pan.fang@mpibpc.mpg.de (P.F.); Kuan-Ting.Pan@kgu.de (K.-T.P.); hurlaub@gwdg.de (H.U.)"],["dc.contributor.affiliation","Urlaub, Henning; 2Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany; yanlong.ji@mpibpc.mpg.de (Y.J.); pan.fang@mpibpc.mpg.de (P.F.); Kuan-Ting.Pan@kgu.de (K.-T.P.); hurlaub@gwdg.de (H.U.)"],["dc.contributor.affiliation","Avkiran, Metin; 1British Heart Foundation Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King’s College London, St Thomas’ Hospital, Westminster Bridge Road, London SE1 7EH, UK; alican.guran@kcl.ac.uk (A.G.); metin.avkiran@kcl.ac.uk (M.A.)"],["dc.contributor.affiliation","Lenz, Christof; 2Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany; yanlong.ji@mpibpc.mpg.de (Y.J.); pan.fang@mpibpc.mpg.de (P.F.); Kuan-Ting.Pan@kgu.de (K.-T.P.); hurlaub@gwdg.de (H.U.)"],["dc.contributor.author","Güran, Alican"],["dc.contributor.author","Ji, Yanlong"],["dc.contributor.author","Fang, Pan"],["dc.contributor.author","Pan, Kuan-Ting"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Avkiran, Metin"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2021-12-01T09:23:06Z"],["dc.date.available","2021-12-01T09:23:06Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-03T19:00:59Z"],["dc.description.abstract","β-adrenergic receptor (β-AR) stimulation represents a major mechanism of modulating cardiac output. In spite of its fundamental importance, its molecular basis on the level of cell signalling has not been characterised in detail yet. We employed mass spectrometry-based proteome and phosphoproteome analysis using SuperSILAC (spike-in stable isotope labelling by amino acids in cell culture) standardization to generate a comprehensive map of acute phosphoproteome changes in mice upon administration of isoprenaline (ISO), a synthetic β-AR agonist that targets both β1-AR and β2-AR subtypes. Our data describe 8597 quantitated phosphopeptides corresponding to 10,164 known and novel phospho-events from 2975 proteins. In total, 197 of these phospho-events showed significantly altered phosphorylation, indicating an intricate signalling network activated in response to β-AR stimulation. In addition, we unexpectedly detected significant cardiac expression and ISO-induced fragmentation of junctophilin-1, a junctophilin isoform hitherto only thought to be expressed in skeletal muscle. Data are available via ProteomeXchange with identifier PXD025569."],["dc.description.abstract","β-adrenergic receptor (β-AR) stimulation represents a major mechanism of modulating cardiac output. In spite of its fundamental importance, its molecular basis on the level of cell signalling has not been characterised in detail yet. We employed mass spectrometry-based proteome and phosphoproteome analysis using SuperSILAC (spike-in stable isotope labelling by amino acids in cell culture) standardization to generate a comprehensive map of acute phosphoproteome changes in mice upon administration of isoprenaline (ISO), a synthetic β-AR agonist that targets both β1-AR and β2-AR subtypes. Our data describe 8597 quantitated phosphopeptides corresponding to 10,164 known and novel phospho-events from 2975 proteins. In total, 197 of these phospho-events showed significantly altered phosphorylation, indicating an intricate signalling network activated in response to β-AR stimulation. In addition, we unexpectedly detected significant cardiac expression and ISO-induced fragmentation of junctophilin-1, a junctophilin isoform hitherto only thought to be expressed in skeletal muscle. Data are available via ProteomeXchange with identifier PXD025569."],["dc.identifier.doi","10.3390/ijms222212584"],["dc.identifier.pii","ijms222212584"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94558"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","1422-0067"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Quantitative Analysis of the Cardiac Phosphoproteome in Response to Acute β-Adrenergic Receptor Stimulation In Vivo"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]