Lenz, Christof

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Weninger, Gunnar"],["dc.contributor.author","Pochechueva, Tatiana"],["dc.contributor.author","El Chami, Dana"],["dc.contributor.author","Luo, Xiaojing"],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Brandenburg, Sören"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Guan, Kaomei"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.date.accessioned","2022-07-01T07:34:53Z"],["dc.date.available","2022-07-01T07:34:53Z"],["dc.date.issued","2022"],["dc.description.abstract","Calpains are calcium-activated neutral proteases involved in the regulation of key signaling pathways. Junctophilin-2 (JP2) is a Calpain-specific proteolytic target and essential structural protein inside Ca 2+ release units required for excitation-contraction coupling in cardiomyocytes. While downregulation of JP2 by Calpain cleavage in heart failure has been reported, the precise molecular identity of the Calpain cleavage sites and the (patho-)physiological roles of the JP2 proteolytic products remain controversial. We systematically analyzed the JP2 cleavage fragments as function of Calpain-1 versus Calpain-2 proteolytic activities, revealing that both Calpain isoforms preferentially cleave mouse JP2 at R565, but subsequently at three additional secondary Calpain cleavage sites. Moreover, we identified the Calpain-specific primary cleavage products for the first time in human iPSC-derived cardiomyocytes. Knockout of RyR2 in hiPSC-cardiomyocytes destabilized JP2 resulting in an increase of the Calpain-specific cleavage fragments. The primary N-terminal cleavage product NT 1 accumulated in the nucleus of mouse and human cardiomyocytes in a Ca 2+ -dependent manner, closely associated with euchromatic chromosomal regions, where NT 1 is proposed to function as a cardio-protective transcriptional regulator in heart failure. Taken together, our data suggest that stabilizing NT 1 by preventing secondary cleavage events by Calpain and other proteases could be an important therapeutic target for future studies."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Deutsches Zentrum für Herz-Kreislaufforschung http://dx.doi.org/10.13039/100010447"],["dc.description.sponsorship","Herzzentrum Göttingen"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s41598-022-14320-9"],["dc.identifier.pii","14320"],["dc.identifier.pmid","35725601"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112032"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/179"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/508"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/435"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P03: Erhaltung und funktionelle Kopplung von ER-Kontakten mit der Plasmamembran"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A09: Lokale molekulare Nanodomänen-Regulation der kardialen Ryanodin-Rezeptor-Funktion"],["dc.relation.eissn","2045-2322"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Calpain cleavage of Junctophilin-2 generates a spectrum of calcium-dependent cleavage products and DNA-rich NT1-fragment domains in cardiomyocytes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2004"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","EMBO reports"],["dc.bibliographiccitation.lastpage","2014"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Warda, Ahmed S"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Sloan, Katherine E"],["dc.contributor.author","Bohnsack, Markus T"],["dc.date.accessioned","2020-12-10T18:42:38Z"],["dc.date.available","2020-12-10T18:42:38Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.15252/embr.201744940"],["dc.identifier.eissn","1469-3178"],["dc.identifier.issn","1469-221X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78032"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Human METTL16 is a N 6 ‐methyladenosine (m 6 A) methyltransferase that targets pre‐mRNAs and various non‐coding RNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Haematologica"],["dc.bibliographiccitation.volume","100"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Corso, Jasmin"],["dc.contributor.author","Beck, J."],["dc.contributor.author","Pan, K.-T."],["dc.contributor.author","Döbele, Carmen"],["dc.contributor.author","Wachter, Astrid"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Schuetz, Eckehardt"],["dc.contributor.author","Tomska, Katarzyna"],["dc.contributor.author","Sellner, L."],["dc.contributor.author","Zenz, Thorsten"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2018-11-07T09:56:10Z"],["dc.date.available","2018-11-07T09:56:10Z"],["dc.date.issued","2015"],["dc.format.extent","178"],["dc.identifier.isi","000361204901386"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36907"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ferrata Storti Foundation"],["dc.publisher.place","Pavia"],["dc.relation.eventlocation","Vienna, AUSTRIA"],["dc.relation.issn","0390-6078"],["dc.title","THE B CELL RECEPTOR SIGNALING OUTPUT IN BURKITT'S LYMPHOMA IS GENOTYPE-SPECIFIC AND IMPACTS SENSITIVITY TOWARDS BCR SIGNALING INHIBITORS"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","862"],["dc.bibliographiccitation.issue","5-6"],["dc.bibliographiccitation.journal","PROTEOMICS"],["dc.bibliographiccitation.lastpage","879"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2018-11-07T10:00:03Z"],["dc.date.available","2018-11-07T10:00:03Z"],["dc.date.issued","2015"],["dc.description.abstract","A majority of cellular functions are carried out by macromolecular complexes. A host of biochemical and spectroscopic methods exists to characterize especially protein/protein complexes, however there has been a lack of a universal method to determine protein stoichiometries. Peptide-based MS, especially as a complementary method to the MS analysis of intact protein complexes, has now been developed to a point where it can be employed to assay protein stoichiometries in a routine manner. While the experimental demands are still significant, peptide-based MS has been successfully applied to analyze stoichiometries for a variety of protein complexes from very different biological backgrounds. In this review, we discuss the requirements especially for targeted MS acquisition strategies to be used in this context, with a special focus on the interconnected experimental aspects of sample preparation, protein digestion, and peptide stability. In addition, different strategies for the introduction of quantitative peptide standards and their suitability for different scenarios are compared."],["dc.description.sponsorship","Max Planck Society"],["dc.identifier.doi","10.1002/pmic.201400466"],["dc.identifier.isi","000352510500002"],["dc.identifier.pmid","25546807"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13839"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37718"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley"],["dc.relation.issn","1615-9861"],["dc.relation.issn","1615-9853"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Studying macromolecular complex stoichiometries by peptide-based mass spectrometry"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1375"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Clinical Oral Investigations"],["dc.bibliographiccitation.lastpage","1384"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Batschkus, Sarah"],["dc.contributor.author","Cingoez, Goekhan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Miosge, Nicolai"],["dc.contributor.author","Kirschneck, Christian"],["dc.contributor.author","Meyer-Marcotty, Philipp"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2020-12-10T14:11:03Z"],["dc.date.available","2020-12-10T14:11:03Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1007/s00784-017-2213-0"],["dc.identifier.eissn","1436-3771"],["dc.identifier.issn","1432-6981"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70949"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","A new albumin-depletion strategy improves proteomic research of gingival crevicular fluid from periodontitis patients"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5581"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5593"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Kuehn-Hoelsken, Eva"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Richter, Florian M."],["dc.contributor.author","Kastner, Berthold"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Urlaub, Henning"],["dc.date.accessioned","2017-09-07T11:45:20Z"],["dc.date.available","2017-09-07T11:45:20Z"],["dc.date.issued","2010"],["dc.description.abstract","Mass spectrometry allows the elucidation of molecular details of the interaction domains of the individual components in macromolecular complexes subsequent to cross-linking of the individual components. Here, we applied chemical and UV cross-linking combined with tandem mass-spectrometric analysis to identify contact sites of the nuclear import adaptor snurportin 1 to the small ribonucleoprotein particle U1 snRNP in addition to the known interaction of m(3)G cap and snurportin 1. We were able to define previously unknown sites of protein-protein and protein-RNA interactions on the molecular level within U1 snRNP. We show that snurportin 1 interacts with its central m(3)G-cap-binding domain with Sm proteins and with its extreme C-terminus with stem-loop III of U1 snRNA. The crosslinking data support the idea of a larger interaction area between snurportin 1 and U snRNPs and the contact sites identified prove useful for modeling the spatial arrangement of snurportin 1 domains when bound to U1 snRNP. Moreover, this suggests a functional nuclear import complex that assembles around the m(3)G cap and the Sm proteins only when the Sm proteins are bound and arranged in the proper orientation to the cognate Sm site in U snRNA."],["dc.identifier.doi","10.1093/nar/gkq272"],["dc.identifier.gro","3142869"],["dc.identifier.isi","000281720500034"],["dc.identifier.pmid","20421206"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/320"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","0305-1048"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Mapping the binding site of snurportin 1 on native U1 snRNP by cross-linking and mass spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Cancer Research"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Stroebel, Philipp"],["dc.contributor.author","Henric-Petri, Hannah"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Emmert, Alexander"],["dc.contributor.author","Bremmer, Felix"],["dc.contributor.author","Strecker, Jasmin"],["dc.contributor.author","Holland, Rainer"],["dc.contributor.author","Hinterthaner, Marc"],["dc.contributor.author","Corso, Jasmin"],["dc.contributor.author","Wagner, Sebastian"],["dc.contributor.author","Kueffer, Stefan"],["dc.contributor.author","Sebastian, Martin"],["dc.contributor.author","Bergmann, Lothar"],["dc.contributor.author","Danner, Bernd"],["dc.contributor.author","Schoendube, Friedrich Albert"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Oellerich, Thomas"],["dc.date.accessioned","2018-11-07T09:33:49Z"],["dc.date.available","2018-11-07T09:33:49Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1158/1538-7445.AM2014-2487"],["dc.identifier.isi","000349906903219"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32050"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Assoc Cancer Research"],["dc.publisher.place","Philadelphia"],["dc.relation.conference","105th Annual Meeting of the American-Association-for-Cancer-Research (AACR)"],["dc.relation.eventlocation","San Diego, CA"],["dc.relation.issn","1538-7445"],["dc.relation.issn","0008-5472"],["dc.title","Comprehensive quantitative proteomic profiling of lung cancers reveals novel biomarkers and potential drug targets"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","eaaz1436"],["dc.bibliographiccitation.issue","647"],["dc.bibliographiccitation.journal","Science Signaling"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Menzel, Julia"],["dc.contributor.author","Kownatzki-Danger, Daniel"],["dc.contributor.author","Tokar, Sergiy"],["dc.contributor.author","Ballone, Alice"],["dc.contributor.author","Unthan-Fechner, Kirsten"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Mori, Mattia"],["dc.contributor.author","Ottmann, Christian"],["dc.contributor.author","Shattock, Michael J."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2021-04-14T08:32:51Z"],["dc.date.available","2021-04-14T08:32:51Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1126/scisignal.aaz1436"],["dc.identifier.pmid","32873725"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84038"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/68"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/368"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/126"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A07: Rolle der TRC40-Maschinerie im Proteostase-Netzwerk von Kardiomyozyten"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation.eissn","1937-9145"],["dc.relation.issn","1945-0877"],["dc.relation.workinggroup","RG Lehnart"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Lenz"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.title","14-3-3 binding creates a memory of kinase action by stabilizing the modified state of phospholamban"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","1800491"],["dc.bibliographiccitation.firstpage","1800491"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","PROTEOMICS"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Jevtić, Živojin"],["dc.contributor.author","Stoll, Britta"],["dc.contributor.author","Pfeiffer, Friedhelm"],["dc.contributor.author","Sharma, Kundan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Marchfelder, Anita"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2019-10-22T08:18:15Z"],["dc.date.accessioned","2021-10-27T13:21:22Z"],["dc.date.available","2019-10-22T08:18:15Z"],["dc.date.available","2021-10-27T13:21:22Z"],["dc.date.issued","2019"],["dc.description.abstract","n-depth proteome analysis of the haloarchaeal model organism Haloferax volcanii has been performed under standard, low/high salt, and low/high temperature conditions using label-free mass spectrometry. Qualitative analysis of protein identification data from high-pH/reversed-phase fractionated samples indicates 61.1% proteome coverage (2509 proteins), which is close to the maximum recorded values in archaea. Identified proteins match to the predicted proteome in their physicochemical properties, with only a small bias against low-molecular-weight and membrane-associated proteins. Cells grown under low and high salt stress as well as low and high temperature stress are quantitatively compared to standard cultures by sequential window acquisition of all theoretical mass spectra (SWATH-MS). A total of 2244 proteins, or 54.7% of the predicted proteome, are quantified across all conditions at high reproducibility, which allowed for global analysis of protein expression changes under these stresses. Of these, 2034 are significantly regulated under at least one stress condition. KEGG pathway enrichment analysis shows that several major cellular pathways are part of H. volcanii's universal stress response. In addition, specific pathways (purine, cobalamin, and tryptophan) are affected by temperature stress. The most strongly downregulated proteins under all stress conditions, zinc finger protein HVO_2753 and ribosomal protein S14, are found oppositely regulated to their immediate genetic neighbors from the same operon."],["dc.identifier.doi","10.1002/pmic.201800491"],["dc.identifier.eissn","1615-9861"],["dc.identifier.issn","1615-9853"],["dc.identifier.pmid","31502396"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16512"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92016"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.eissn","1615-9861"],["dc.relation.issn","1615-9861"],["dc.relation.issn","1615-9853"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.subject.ddc","610"],["dc.title","The Response of Haloferax volcanii to Salt and Temperature Stress: A Proteome Study by Label‐Free Mass Spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Schulze, Stefan"],["dc.contributor.author","Adams, Zachary"],["dc.contributor.author","Cerletti, Micaela"],["dc.contributor.author","De Castro, Rosana"],["dc.contributor.author","Ferreira-Cerca, Sébastien"],["dc.contributor.author","Fufezan, Christian"],["dc.contributor.author","Giménez, María Inés"],["dc.contributor.author","Hippler, Michael"],["dc.contributor.author","Jevtic, Zivojin"],["dc.contributor.author","Knüppel, Robert"],["dc.contributor.author","Legerme, Georgio"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Marchfelder, Anita"],["dc.contributor.author","Maupin-Furlow, Julie"],["dc.contributor.author","Paggi, Roberto A."],["dc.contributor.author","Pfeiffer, Friedhelm"],["dc.contributor.author","Poetsch, Ansgar"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Pohlschroder, Mechthild"],["dc.date.accessioned","2021-04-14T08:25:49Z"],["dc.date.available","2021-04-14T08:25:49Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41467-020-16784-7"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81739"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2041-1723"],["dc.title","The Archaeal Proteome Project advances knowledge about archaeal cell biology through comprehensive proteomics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]