Bohnenberger, Hanibal

[["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","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.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Schneider, Constanze"],["dc.contributor.author","Thomas, Dominique"],["dc.contributor.author","Knecht, Kirsten M."],["dc.contributor.author","Buzovetsky, Olga"],["dc.contributor.author","Kaderali, Lars"],["dc.contributor.author","Schliemann, Christoph"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Angenendt, Linus"],["dc.contributor.author","Hartmann, Wolfgang"],["dc.contributor.author","Wardelmann, Eva"],["dc.contributor.author","Rothenburger, Tamara"],["dc.contributor.author","Mohr, Sebastian"],["dc.contributor.author","Scheich, Sebastian"],["dc.contributor.author","Comoglio, Federico"],["dc.contributor.author","Wilke, Anne"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Michaelis, Martin"],["dc.contributor.author","Ferreirós, Nerea"],["dc.contributor.author","Geisslinger, Gerd"],["dc.contributor.author","Xiong, Yong"],["dc.contributor.author","Keppler, Oliver T."],["dc.contributor.author","Cinatl, Jindrich"],["dc.date.accessioned","2019-11-25T13:37:34Z"],["dc.date.accessioned","2021-10-27T13:21:34Z"],["dc.date.available","2019-11-25T13:37:34Z"],["dc.date.available","2021-10-27T13:21:34Z"],["dc.date.issued","2019"],["dc.description.abstract","Hypomethylating agents decitabine and azacytidine are regarded as interchangeable in the treatment of acute myeloid leukemia (AML). However, their mechanisms of action remain incompletely understood, and predictive biomarkers for HMA efficacy are lacking. Here, we show that the bioactive metabolite decitabine triphosphate, but not azacytidine triphosphate, functions as activator and substrate of the triphosphohydrolase SAMHD1 and is subject to SAMHD1-mediated inactivation. Retrospective immunohistochemical analysis of bone marrow specimens from AML patients at diagnosis revealed that SAMHD1 expression in leukemic cells inversely correlates with clinical response to decitabine, but not to azacytidine. SAMHD1 ablation increases the antileukemic activity of decitabine in AML cell lines, primary leukemic blasts, and xenograft models. AML cells acquire resistance to decitabine partly by SAMHD1 up-regulation. Together, our data suggest that SAMHD1 is a biomarker for the stratified use of hypomethylating agents in AML patients and a potential target for the treatment of decitabine-resistant leukemia."],["dc.identifier.doi","10.1038/s41467-019-11413-4"],["dc.identifier.pmid","31375673"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16724"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92032"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.eissn","2041-1723"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Selective inactivation of hypomethylating agents by SAMHD1 provides a rationale for therapeutic stratification in AML"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["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.artnumber","8928"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Haetscher, Nadine"],["dc.contributor.author","Feuermann, Yonatan D."],["dc.contributor.author","Wingert, Susanne"],["dc.contributor.author","Rehage, Maike"],["dc.contributor.author","Thalheimer, Frederic B."],["dc.contributor.author","Weiser, Christian"],["dc.contributor.author","Bohnenberger, Hanibal"],["dc.contributor.author","Jung, Klaus"],["dc.contributor.author","Schroeder, Timm"],["dc.contributor.author","Serve, Hubert"],["dc.contributor.author","Oellerich, Thomas"],["dc.contributor.author","Hennighausen, Lothar"],["dc.contributor.author","Rieger, Michael A."],["dc.date.accessioned","2018-11-07T09:49:18Z"],["dc.date.available","2018-11-07T09:49:18Z"],["dc.date.issued","2015"],["dc.description.abstract","Haematopoietic stem cells (HSCs) require the right composition of microRNAs (miR) for proper life-long balanced blood regeneration. Here we show a regulatory circuit that prevents excessive HSC self-renewal by upregulation of miR-193b upon self-renewal promoting thrombopoietin (TPO)-MPL-STAT5 signalling. In turn, miR-193b restricts cytokine signalling, by targeting the receptor tyrosine kinase c-KIT. We generated a miR-193b knockout mouse model to unravel the physiological function of miR-193b in haematopoiesis. MiR-193b(-/-) mice show a selective gradual enrichment of functional HSCs, which are fully competent in multilineage blood reconstitution upon transplantation. The absence of miR-193b causes an accelerated expansion of HSCs, without altering cell cycle or survival, but by decelerating differentiation. Conversely, ectopic miR-193b expression restricts long-term repopulating HSC expansion and blood reconstitution. MiR-193b-deficient haematopoietic stem and progenitor cells exhibit increased basal and cytokine-induced STAT5 and AKT signalling. This STAT5-induced microRNA provides a negative feedback for excessive signalling to restrict uncontrolled HSC expansion."],["dc.identifier.doi","10.1038/ncomms9928"],["dc.identifier.isi","000366379400010"],["dc.identifier.pmid","26603207"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12733"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35481"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","STAT5-regulated microRNA-193b controls haematopoietic stem and progenitor cell expansion by modulating cytokine receptor signalling"],["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","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"]]