Urlaub, Henning

[["dc.bibliographiccitation.artnumber","e52640"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Batsukh, Tserendulam"],["dc.contributor.author","Schulz, Yvonne"],["dc.contributor.author","Wolf, Stephan"],["dc.contributor.author","Rabe, Tamara I."],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schaefer, Inga-Marie"],["dc.contributor.author","Pauli, Silke"],["dc.date.accessioned","2018-11-07T09:02:12Z"],["dc.date.available","2018-11-07T09:02:12Z"],["dc.date.issued","2012"],["dc.description.abstract","Background: Mutations in the chromodomain helicase DNA binding protein 7 gene (CHD7) lead to CHARGE syndrome, an autosomal dominant multiple malformation disorder. Proteins involved in chromatin remodeling typically act in multiprotein complexes. We previously demonstrated that a part of human CHD7 interacts with a part of human CHD8, another chromodomain helicase DNA binding protein presumably being involved in the pathogenesis of neurodevelopmental (NDD) and autism spectrum disorders (ASD). Because identification of novel CHD7 and CHD8 interacting partners will provide further insights into the pathogenesis of CHARGE syndrome and ASD/NDD, we searched for additional associated polypeptides using the method of stable isotope labeling by amino acids in cell culture (SILAC) in combination with mass spectrometry. Principle findings: The hitherto uncharacterized FAM124B (Family with sequence similarity 124B) was identified as a potential interaction partner of both CHD7 and CHD8. We confirmed the result by co-immunoprecipitation studies and showed a direct binding to the CHD8 part by direct yeast two hybrid experiments. Furthermore, we characterized FAM124B as a mainly nuclear localized protein with a widespread expression in embryonic and adult mouse tissues. Conclusion: Our results demonstrate that FAM124B is a potential interacting partner of a CHD7 and CHD8 containing complex. From the overlapping expression pattern between Chd7 and Fam124B at murine embryonic day E12.5 and the high expression of Fam124B in the developing mouse brain, we conclude that Fam124B is a novel protein possibly involved in the pathogenesis of CHARGE syndrome and neurodevelopmental disorders."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2012"],["dc.identifier.doi","10.1371/journal.pone.0052640"],["dc.identifier.isi","000313158800084"],["dc.identifier.pmid","23285124"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8490"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24622"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Identification and Characterization of FAM124B as a Novel Component of a CHD7 and CHD8 Containing Complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","549"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cancer Cell"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Mohr, Sebastian"],["dc.contributor.author","Döbele, Carmen"],["dc.contributor.author","Comoglio, Federico"],["dc.contributor.author","Berg, Tobias"],["dc.contributor.author","Beck, Julia"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Alexe, Gabriela"],["dc.contributor.author","Corso, Jasmin"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Wachter, Astrid"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Schnuetgen, Frank"],["dc.contributor.author","Cremer, Anjali"],["dc.contributor.author","Haetscher, Nadine"],["dc.contributor.author","Goellner, Stefanie"],["dc.contributor.author","Rouhi, Arefeh"],["dc.contributor.author","Palmqvist, Lars"],["dc.contributor.author","Rieger, Michael A."],["dc.contributor.author","Schroeder, Timm"],["dc.contributor.author","Boenig, Halvard"],["dc.contributor.author","Meuller-Tidow, Carsten"],["dc.contributor.author","Kuchenbauer, Florian"],["dc.contributor.author","Schuetz, Ekkehard"],["dc.contributor.author","Green, Anthony R."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Stegmaier, Kimberly"],["dc.contributor.author","Humphries, R. Keith"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Oellerich, Thomas"],["dc.date.accessioned","2018-11-07T10:25:02Z"],["dc.date.available","2018-11-07T10:25:02Z"],["dc.date.issued","2017"],["dc.description.abstract","The transcription factor Meis1 drives myeloid leukemogenesis in the context of Hox gene overexpression but is currently considered undruggable. We therefore investigated whether myeloid progenitor cells transformed by Hoxa9 and Meis1 become addicted to targetable signaling pathways. A comprehensive (phospho) proteomic analysis revealed that Meis1 increased Syk protein expression and activity. Syk upregulation occurs through a Meis1-dependent feedback loop. By dissecting this loop, we show that Syk is a direct target of miR-146a, whose expression is indirectly regulated by Meis1 through the transcription factor PU. 1. In the context of Hoxa9 overexpression, Syk signaling induces Meis1, recapitulating several leukemogenic features of Hoxa9/Meis1-driven leukemia. Finally, Syk inhibition disrupts the identified regulatory loop, prolonging survival of mice with Hoxa9/Meis1-driven leukemia."],["dc.identifier.doi","10.1016/j.ccell.2017.03.001"],["dc.identifier.isi","000398670600010"],["dc.identifier.pmid","28399410"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14438"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42772"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.issn","1878-3686"],["dc.relation.issn","1535-6108"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Hoxa9 and Meis1 Cooperatively Induce Addiction to Syk Signaling by Suppressing miR-146a in Acute Myeloid Leukemia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1738"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.lastpage","1750"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Gronborg, Mads"],["dc.contributor.author","Neumann, Konstantin"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Wienands, Juergen"],["dc.date.accessioned","2018-11-07T08:28:22Z"],["dc.date.available","2018-11-07T08:28:22Z"],["dc.date.issued","2009"],["dc.description.abstract","Understanding intracellular signal transduction by cell surface receptors requires information about the precise order of relevant modifications on the early transducer elements. Here we introduce the B cell line DT40 and its genetically engineered variants as a model system to determine and functionally characterize post-translational protein modifications in general. This is accomplished by a customized strategy that combines mass spectrometric analyses of protein modifications with subsequent mutational studies. When applied to the B cell receptor (BCR)proximal effector SLP-65, this approach uncovered a differential and highly dynamic engagement of numerous newly identified phospho-acceptor sites. Some of them serve as kinase substrates in resting cells and undergo rapid dephosphorylation upon BCR ligation. Stimulation-induced phosphorylation of SLP-65 can be early and transient, or early and sustained, or late. Functional elucidation of conspicuous phosphorylation at serine 170 in SLP-65 revealed a BCR-distal checkpoint for some but not all possible B cell responses. Our data show that SLP-65 phosphorylation acts upstream for signal initiation and also downstream during selective processing of the BCR signal. Such a phenomenon defines a receptor-specific signal integrator. Molecular & Cellular Proteomics 8: 1738-1750, 2009."],["dc.description.sponsorship","European Union, HYBLIB"],["dc.identifier.doi","10.1074/mcp.M800567-MCP200"],["dc.identifier.isi","000267960300023"],["dc.identifier.pmid","19372136"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16410"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1535-9476"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","SLP-65 Phosphorylation Dynamics Reveals a Functional Basis for Signal Integration by Receptor-proximal Adaptor Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","33"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Pathology: Clinical Research"],["dc.bibliographiccitation.lastpage","47"],["dc.bibliographiccitation.volume","8"],["dc.contributor.affiliation","Fichtner, Alexander; 1\r\nInstitute of Pathology\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Joost, Jasmin; 1\r\nInstitute of Pathology\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Brockmeyer, Philipp; 2\r\nDepartment of Oral and Maxillofacial Surgery\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Kauffmann, Philipp; 2\r\nDepartment of Oral and Maxillofacial Surgery\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Schliephake, Henning; 2\r\nDepartment of Oral and Maxillofacial Surgery\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Hammerstein‐Equord, Alexander; 3\r\nDepartment of Thoracic and Cardiovascular Surgery\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Kueffer, Stefan; 1\r\nInstitute of Pathology\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Urlaub, Henning; 4\r\nBioanalytical Mass Spectrometry Group\r\nMax Planck Institute for Biophysical Chemistry\r\nGöttingen Germany"],["dc.contributor.affiliation","Oellerich, Thomas; 6\r\nDepartment of Medicine II, Haematology/Oncology\r\nGoethe University\r\nFrankfurt Germany"],["dc.contributor.affiliation","Ströbel, Philipp; 1\r\nInstitute of Pathology\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Bohnenberger, Hanibal; 1\r\nInstitute of Pathology\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.affiliation","Bremmer, Felix; 1\r\nInstitute of Pathology\r\nUniversity Medical Centre Göttingen\r\nGöttingen Germany"],["dc.contributor.author","Richter, Annika"],["dc.contributor.author","Fichtner, Alexander"],["dc.contributor.author","Joost, Jasmin"],["dc.contributor.author","Brockmeyer, Philipp"],["dc.contributor.author","Kauffmann, Philipp"],["dc.contributor.author","Schliephake, Henning"],["dc.contributor.author","Hammerstein‐Equord, Alexander"],["dc.contributor.author","Kueffer, Stefan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Bremmer, Felix"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.date.accessioned","2021-12-01T09:23:20Z"],["dc.date.available","2021-12-01T09:23:20Z"],["dc.date.issued","2021"],["dc.date.updated","2022-03-20T23:05:20Z"],["dc.description.abstract","Abstract The differentiation between a pulmonary metastasis and a newly developed squamous cell carcinoma of the lung in patients with prior head and neck squamous cell carcinoma (HNSCC) is difficult due to a lack of biomarkers but is crucially important for the prognosis and therapy of the affected patient. By using high‐resolution mass spectrometry in combination with stable isotope labelling by amino acids in cell culture, we identified 379 proteins that are differentially expressed in squamous cell carcinomas of the lung and the head and neck. Of those, CAV1, CAV2, LGALS1, LGALS7, CK19, and UGDH were tested by immunohistochemistry on 194 tissue samples (98 lung and 96 HNSCCs). The combination of CAV1 and LGALS7 was able to distinguish the origin of the squamous cell carcinoma with high accuracy (area under the curve 0.876). This biomarker panel was tested on a cohort of 12 clinically classified lung tumours of unknown origin after HNSCC. Nine of those tumours were immunohistochemically classifiable."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1002/cjp2.244"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94624"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2056-4538"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Quantitative proteomics identifies biomarkers to distinguish pulmonary from head and neck squamous cell carcinomas by immunohistochemistry"],["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","914"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Cell Research"],["dc.bibliographiccitation.lastpage","934"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Helmke, Christina"],["dc.contributor.author","Raab, Monika"],["dc.contributor.author","Roedel, Franz"],["dc.contributor.author","Matthess, Yves"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Mandal, Ranadip"],["dc.contributor.author","Sanhaji, Mourad"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Roedel, Claus"],["dc.contributor.author","Becker, Sven"],["dc.contributor.author","Strebhardt, Klaus"],["dc.date.accessioned","2018-11-07T10:11:12Z"],["dc.date.available","2018-11-07T10:11:12Z"],["dc.date.issued","2016"],["dc.description.abstract","Upon interaction of the CD95 receptor with its ligand, sequential association of the adaptor molecule FADD (MORT1), pro-forms of caspases-8/10, and the caspase-8/10 regulator c-FLIP leads to the formation of a death-inducing signaling complex. Here, we identify polo-like kinase (Plk) 3 as a new interaction partner of the death receptor CD95. The enzymatic activity of Plk3 increases following interaction of the CD95 receptor with its ligand. Knockout (KO) or knockdown of caspase-8, CD95 or FADD prevents activation of Plk3 upon CD95 stimulation, suggesting a requirement of a functional DISC for Plk3 activation. Furthermore, we identify caspase-8 as a new substrate for Plk3. Phosphorylation occurs on T273 and results in stimulation of caspase-8 proapoptotic function. Stimulation of CD95 in cells expressing a non-phosphorylatable caspase-8-T273A mutant in a rescue experiment or in Plk3-KO cells generated by CRISPR/Cas9 reduces the processing of caspase-8 prominently. Low T273 phosphorylation correlates significantly with low Plk3 expression in a cohort of 95 anal tumor patients. Our data suggest a novel mechanism of kinase activation within the Plk family and propose a new model for the stimulation of the extrinsic death pathway in tumors with high Plk3 expression."],["dc.identifier.doi","10.1038/cr.2016.78"],["dc.identifier.isi","000380923900009"],["dc.identifier.pmid","27325299"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14111"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39998"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Inst Biochemistry & Cell Biology"],["dc.relation.issn","1748-7838"],["dc.relation.issn","1001-0602"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Ligand stimulation of CD95 induces activation of Plk3 followed by phosphorylation of caspase-8"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","135"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Immunological Reviews"],["dc.bibliographiccitation.lastpage","149"],["dc.bibliographiccitation.volume","232"],["dc.contributor.author","Neumann, Konstantin"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Wienands, Jürgen"],["dc.date.accessioned","2011-04-21T09:31:50Z"],["dc.date.accessioned","2021-10-27T13:22:42Z"],["dc.date.available","2011-04-21T09:31:50Z"],["dc.date.available","2021-10-27T13:22:42Z"],["dc.date.issued","2009"],["dc.description.abstract","The growth factor receptor-bound protein 2 (Grb2) is a ubiquitously expressed and evolutionary conserved adapter protein possessing a plethora of described interaction partners for the regulation of signal transduction. In B lymphocytes, the Grb2-mediated scaffolding function controls the assembly and subcellular targeting of activating as well as inhibitory signalosomes in response to ligation of the antigen receptor. Also, integration of simultaneous signals from B-cell coreceptors that amplify or attenuate antigen receptor signal output relies on Grb2. Hence, Grb2 is an essential signal integrator. The key question remains, however, of how pathway specificity can be maintained during signal homeostasis critically required for the balance between immune cell activation and tolerance induction. Here, we summarize the molecular network of Grb2 in B cells and introduce a proteomic approach to elucidate the interactome of Grb2 in vivo."],["dc.identifier.doi","10.1111/j.1600-065X.2009.00845.x"],["dc.identifier.isi","000271057600011"],["dc.identifier.pmid","19909361"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6258"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92119"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1600-065X"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","610"],["dc.subject.mesh","Animals"],["dc.subject.mesh","B-Lymphocytes"],["dc.subject.mesh","GRB2 Adaptor Protein"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Immune Tolerance"],["dc.subject.mesh","Lymphocyte Activation"],["dc.subject.mesh","Protein Interaction Domains and Motifs"],["dc.subject.mesh","Protein Multimerization"],["dc.subject.mesh","Proteomics"],["dc.subject.mesh","Receptor Cross-Talk"],["dc.subject.mesh","Receptors, Antigen, B-Cell"],["dc.subject.mesh","Signal Transduction"],["dc.title","The B-lymphoid Grb2 interaction code."],["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.artnumber","e52435"],["dc.bibliographiccitation.issue","96"],["dc.bibliographiccitation.journal","Journal of Visualized Experiments"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Stroebel, Philipp"],["dc.contributor.author","Mohr, Sebastian"],["dc.contributor.author","Corso, Jasmin"],["dc.contributor.author","Berg, Tobias"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Oellerich, Thomas"],["dc.date.accessioned","2018-11-07T10:01:07Z"],["dc.date.available","2018-11-07T10:01:07Z"],["dc.date.issued","2015"],["dc.description.abstract","In-depth analyses of cancer cell proteomes are needed to elucidate oncogenic pathomechanisms, as well as to identify potential drug targets and diagnostic biomarkers. However, methods for quantitative proteomic characterization of patient-derived tumors and in particular their cellular subpopulations are largely lacking. Here we describe an experimental set-up that allows quantitative analysis of proteomes of cancer cell subpopulations derived from either liquid or solid tumors. This is achieved by combining cellular enrichment strategies with quantitative Super-SILAC-based mass spectrometry followed by bioinformatic data analysis. To enrich specific cellular subsets, liquid tumors are first immunophenotyped by flow cytometry followed by FACS-sorting; for solid tumors, laser-capture microdissection is used to purify specific cellular subpopulations. In a second step, proteins are extracted from the purified cells and subsequently combined with a tumor-specific, SILAC-labeled spike-in standard that enables protein quantification. The resulting protein mixture is subjected to either gel electrophoresis or Filter Aided Sample Preparation (FASP) followed by tryptic digestion. Finally, tryptic peptides are analyzed using a hybrid quadrupole-orbitrap mass spectrometer, and the data obtained are processed with bioinformatic software suites including MaxQuant. By means of the workflow presented here, up to 8,000 proteins can be identified and quantified in patient-derived samples, and the resulting protein expression profiles can be compared among patients to identify diagnostic proteomic signatures or potential drug targets."],["dc.identifier.doi","10.3791/52435"],["dc.identifier.isi","000361533700047"],["dc.identifier.pmid","25867170"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12150"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37949"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Journal Of Visualized Experiments"],["dc.relation.issn","1940-087X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Quantitative Mass Spectrometric Profiling of Cancer-cell Proteomes Derived From Liquid and Solid Tumors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Disease Markers"],["dc.bibliographiccitation.lastpage","14"],["dc.bibliographiccitation.volume","2019"],["dc.contributor.author","Bremmer, Felix"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Küffer, Stefan"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Strauß, Arne"],["dc.contributor.author","Maatoug, Yasmine"],["dc.contributor.author","Behnes, Carl Ludwig"],["dc.contributor.author","Oing, Christoph"],["dc.contributor.author","Radzun, Heinz Joachim"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Balabanov, Stefan"],["dc.contributor.author","Honecker, Friedemann"],["dc.date.accessioned","2019-09-24T07:40:13Z"],["dc.date.available","2019-09-24T07:40:13Z"],["dc.date.issued","2019"],["dc.description.abstract","Malignant germ cell tumors (GCT) are the most common malignant tumors in young men between 18 and 40 years. The correct identification of histological subtypes, in difficult cases supported by immunohistochemistry, is essential for therapeutic management. Furthermore, biomarkers may help to understand pathophysiological processes in these tumor types. Two GCT cell lines, TCam-2 with seminoma-like characteristics, and NTERA-2, an embryonal carcinoma-like cell line, were compared by a quantitative proteomic approach using high-resolution mass spectrometry (MS) in combination with stable isotope labelling by amino acid in cell culture (SILAC). We were able to identify 4856 proteins and quantify the expression of 3936. 347 were significantly differentially expressed between the two cell lines. For further validation, CD81, CBX-3, PHF6, and ENSA were analyzed by western blot analysis. The results confirmed the MS results. Immunohistochemical analysis on 59 formalin-fixed and paraffin-embedded (FFPE) normal and GCT tissue samples (normal testis, GCNIS, seminomas, and embryonal carcinomas) of these proteins demonstrated the ability to distinguish different GCT subtypes, especially seminomas and embryonal carcinomas. In addition, siRNA-mediated knockdown of these proteins resulted in an antiproliferative effect in TCam-2, NTERA-2, and an additional embryonal carcinoma-like cell line, NCCIT. In summary, this study represents a proteomic resource for the discrimination of malignant germ cell tumor subtypes and the observed antiproliferative effect after knockdown of selected proteins paves the way for the identification of new potential drug targets."],["dc.identifier.doi","10.1155/2019/8298524"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16378"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62439"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","0278-0240"],["dc.relation.issn","1875-8630"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Proteomic Comparison of Malignant Human Germ Cell Tumor Cell Lines"],["dc.type","journal_article"],["dc.type.internalPublication","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","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","3620"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","3634"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Bremes, Vanessa"],["dc.contributor.author","Neumann, Konstantin"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Dittmann, Kai"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Engelke, Michael"],["dc.contributor.author","Schnyder, Tim"],["dc.contributor.author","Batista, Facundo D."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Wienands, Juergen"],["dc.date.accessioned","2018-11-07T08:53:03Z"],["dc.date.available","2018-11-07T08:53:03Z"],["dc.date.issued","2011"],["dc.description.abstract","Spleen tyrosine kinase Syk and its substrate SLP65 (also called BLNK) are proximal signal transducer elements of the B-cell antigen receptor (BCR). Yet, our understanding of signal initiation and processing is limited owing to the incomplete list of SLP65 interaction partners and our ignorance of their association kinetics. We have now determined and quantified the in vivo interactomes of SLP65 in resting and stimulated B cells by mass spectrometry. SLP65 orchestrated a complex signal network of about 30 proteins that was predominantly based on dynamic interactions. However, a stimulation-independent and constant association of SLP65 with the Cbl-interacting protein of 85 kDa (CIN85) was requisite for SLP65 phosphorylation and its inducible plasma membrane translocation. In the absence of a steady SLP65/CIN85 complex, BCR-induced Ca(2+) and NF-kappa B responses were abrogated. Finally, live cell imaging and co-immunoprecipitation experiments further confirmed that both SLP65 and CIN85 are key components of the BCR-associated primary transducer module required for the onset and progression phases of BCR signal transduction. The EMBO Journal (2011) 30, 3620-3634. doi:10.1038/emboj.2011.251; Published online 5 August 2011"],["dc.identifier.doi","10.1038/emboj.2011.251"],["dc.identifier.isi","000294460000015"],["dc.identifier.pmid","21822214"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7839"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22317"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The B-cell antigen receptor signals through a preformed transducer module of SLP65 and CIN85"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]