Winkler, Michael

[["dc.bibliographiccitation.artnumber","e97695"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Eckert, Nadine"],["dc.contributor.author","Wrensch, Florian"],["dc.contributor.author","Gärtner, Sabine"],["dc.contributor.author","Palanisamy, Navaneethan"],["dc.contributor.author","Goedecke, Ulrike"],["dc.contributor.author","Jäger, Nils"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Winkler, Michael"],["dc.date.accessioned","2019-07-09T11:39:43Z"],["dc.date.available","2019-07-09T11:39:43Z"],["dc.date.issued","2014"],["dc.description.abstract","Reporter genes inserted into viral genomes enable the easy and rapid quantification of virus replication, which is instrumental to efficient in vitro screening of antiviral compounds or in vivo analysis of viral spread and pathogenesis. Based on a published design, we have generated several replication competent influenza A viruses carrying either fluorescent proteins or Gaussia luciferase. Reporter activity could be readily quantified in infected cultures, but the virus encoding Gaussia luciferase was more stable than viruses bearing fluorescent proteins and was therefore analyzed in detail. Quantification of Gaussia luciferase activity in the supernatants of infected culture allowed the convenient and highly sensitive detection of viral spread, and enzymatic activity correlated with the number of infectious particles released from infected cells. Furthermore, the Gaussia luciferase encoding virus allowed the sensitive quantification of the antiviral activity of the neuraminidase inhibitor (NAI) zanamivir and the host cell interferon-inducible transmembrane (IFITM) proteins 1–3, which are known to inhibit influenza virus entry. Finally, the virus was used to demonstrate that influenza A virus infection is sensitive to a modulator of endosomal cholesterol, in keeping with the concept that IFITMs inhibit viral entry by altering cholesterol levels in the endosomal membrane. In sum, we report the characterization of a novel influenza A reporter virus, which allows fast and sensitive detection of viral spread and its inhibition, and we show that influenza A virus entry is sensitive to alterations of endosomal cholesterol levels."],["dc.identifier.doi","10.1371/journal.pone.0097695"],["dc.identifier.pmid","24842154"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10118"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58030"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Influenza A Virus Encoding Secreted Gaussia Luciferase as Useful Tool to Analyze Viral Replication and Its Inhibition by Antiviral Compounds and Cellular Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3859"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Wrensch, Florian"],["dc.contributor.author","Bosch, Pascale"],["dc.contributor.author","Knoth, Maike"],["dc.contributor.author","Schindler, Michael"],["dc.contributor.author","Gärtner, Sabine"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2020-12-10T18:47:09Z"],["dc.date.available","2020-12-10T18:47:09Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3390/ijms20163859"],["dc.identifier.eissn","1422-0067"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16799"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78659"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Analysis of IFITM-IFITM Interactions by a Flow Cytometry-Based FRET Assay"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13863"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","13873"],["dc.bibliographiccitation.volume","293"],["dc.contributor.author","Zmora, Pawel"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Kollmus, Heike"],["dc.contributor.author","Moldenhauer, Anna-Sophie"],["dc.contributor.author","Danov, Olga"],["dc.contributor.author","Braun, Armin"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Schughart, Klaus"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2020-12-10T18:12:58Z"],["dc.date.available","2020-12-10T18:12:58Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1074/jbc.RA118.001273"],["dc.identifier.eissn","1083-351X"],["dc.identifier.issn","0021-9258"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74544"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","TMPRSS11A activates the influenza A virus hemagglutinin and the MERS coronavirus spike protein and is insensitive against blockade by HAI-1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","186"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Xenotransplantation"],["dc.bibliographiccitation.lastpage","196"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Loss, M."],["dc.contributor.author","Vangerow, B."],["dc.contributor.author","Schmidtko, J."],["dc.contributor.author","Kunz, R."],["dc.contributor.author","Jalali, A."],["dc.contributor.author","Arends, H."],["dc.contributor.author","Przemeck, M."],["dc.contributor.author","Rückholt, H."],["dc.contributor.author","Leuwer, M."],["dc.contributor.author","Kaup, F. J."],["dc.contributor.author","Winkler, M."],["dc.date.accessioned","2022-10-06T13:34:08Z"],["dc.date.available","2022-10-06T13:34:08Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1034/j.1399-3089.2000.00059.x"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115837"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.issn","0908-665X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Acute vascular rejection is associated with systemic complement activation ina pig-to-primate kidney xenograft model"],["dc.title.alternative","Acute vascular rejection is associated with complement activation"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e00246-17"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.volume","91"],["dc.contributor.author","Gerlach, Thomas"],["dc.contributor.author","Hensen, Luca"],["dc.contributor.author","Matrosovich, Tatyana"],["dc.contributor.author","Bergmann, Janina"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Peteranderl, Christin"],["dc.contributor.author","Klenk, Hans-Dieter"],["dc.contributor.author","Weber, Friedemann"],["dc.contributor.author","Herold, Susanne"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.editor","Dermody, Terence S."],["dc.date.accessioned","2022-10-06T13:25:32Z"],["dc.date.available","2022-10-06T13:25:32Z"],["dc.date.issued","2017"],["dc.description.abstract","ABSTRACT\n The replication and pathogenicity of influenza A viruses (IAVs) critically depend on their ability to tolerate the antiviral interferon (IFN) response. To determine a potential role for the IAV hemagglutinin (HA) in viral sensitivity to IFN, we studied the restriction of IAV infection in IFN-β-treated human epithelial cells by using 2:6 recombinant IAVs that shared six gene segments of A/Puerto Rico/8/1934 virus (PR8) and contained HAs and neuraminidases of representative avian, human, and zoonotic H5N1 and H7N9 viruses. In A549 and Calu-3 cells, viruses displaying a higher pH optimum of HA-mediated membrane fusion, H5N1-PR8 and H7N9-PR8, were less sensitive to the IFN-induced antiviral state than their counterparts with HAs from duck and human viruses, which fused at a lower pH. The association between a high pH optimum of fusion and reduced IFN sensitivity was confirmed by using HA point mutants of A/Hong Kong/1/1968-PR8 that differed solely by their fusion properties. Furthermore, similar effects of the viral fusion pH on IFN sensitivity were observed in experiments with (i) primary human type II alveolar epithelial cells and differentiated cultures of human airway epithelial cells, (ii) nonrecombinant zoonotic and pandemic IAVs, and (iii) preparations of IFN-α and IFN-λ1. A higher pH of membrane fusion and reduced sensitivity to IFN correlated with lower restriction of the viruses in MDCK cells stably expressing the IFN-inducible transmembrane proteins IFITM2 and IFITM3, which are known to inhibit viral fusion. Our results reveal that the pH optimum of HA-driven membrane fusion of IAVs is a determinant of their sensitivity to IFN and IFITM proteins.\n \n IMPORTANCE\n The IFN system constitutes an important innate defense against viral infection. Substantial information is available on how IAVs avoid detection by sensors of the IFN system and disable IFN signaling pathways. Much less is known about the ability of IAVs to tolerate the antiviral activity of IFN-induced cellular proteins. The IFN-induced proteins of the IFITM family block IAV entry into target cells and can restrict viral spread and pathogenicity. Here we show for the first time that the sensitivity of IAVs to the IFN-induced antiviral state and IFITM2 and IFITM3 proteins depends on the pH value at which the viral HA undergoes a conformational transition and mediates membrane fusion. Our data imply that the high pH optimum of membrane fusion typical of zoonotic IAVs of gallinaceous poultry, such as H5N1 and H7N9, may contribute to their enhanced virulence in humans."],["dc.description.sponsorship"," European Commission Seventh Framework Programme https://doi.org/10.13039/501100000780"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft https://doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft https://doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft https://doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Leibniz-Gemeinschaft https://doi.org/10.13039/501100001664"],["dc.identifier.doi","10.1128/JVI.00246-17"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114863"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","pH Optimum of Hemagglutinin-Mediated Membrane Fusion Determines Sensitivity of Influenza A Viruses to the Interferon-Induced Antiviral State and IFITMs"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","S1"],["dc.bibliographiccitation.journal","Retrovirology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Koppensteiner, Herwig"],["dc.contributor.author","Höhne, Kristin"],["dc.contributor.author","Gondim, Marcos Vinicius"],["dc.contributor.author","Gobert, Francois-Xavier"],["dc.contributor.author","Widder, Miriam"],["dc.contributor.author","Gundlach, Swantje"],["dc.contributor.author","Heigele, Anke"],["dc.contributor.author","Kirchhoff, Frank"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Benaroch, Philippe"],["dc.contributor.author","Schindler, Michael"],["dc.date.accessioned","2022-10-06T13:26:11Z"],["dc.date.available","2022-10-06T13:26:11Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1186/1742-4690-10-S1-P42"],["dc.identifier.pii","3514"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115018"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1742-4690"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Nef variants from non-pathogenic lentiviral strains inhibit iron uptake through an AP2-dependent inhibition of transferrin endocytosis"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6150"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.lastpage","6160"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Bertram, Stephanie"],["dc.contributor.author","Dijkman, Ronald"],["dc.contributor.author","Habjan, Matthias"],["dc.contributor.author","Heurich, Adeline"],["dc.contributor.author","Gierer, Stefanie"],["dc.contributor.author","Glowacka, Ilona"],["dc.contributor.author","Welsch, Kathrin"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Schneider, Heike"],["dc.contributor.author","Hofmann-Winkler, Heike"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.date.accessioned","2022-10-06T13:25:38Z"],["dc.date.available","2022-10-06T13:25:38Z"],["dc.date.issued","2013"],["dc.description.abstract","ABSTRACT\n \n Infection with human coronavirus 229E (HCoV-229E) is associated with the common cold and may result in pneumonia in immunocompromised patients. The viral spike (S) protein is incorporated into the viral envelope and mediates infectious entry of HCoV-229E into host cells, a process that depends on the activation of the S-protein by host cell proteases. However, the proteases responsible for HCoV-229E activation are incompletely defined. Here we show that the type II transmembrane serine proteases TMPRSS2 and HAT cleave the HCoV-229E S-protein (229E-S) and augment 229E-S-driven cell-cell fusion, suggesting that TMPRSS2 and HAT can activate 229E-S. Indeed, engineered expression of TMPRSS2 and HAT rendered 229E-S-driven virus-cell fusion insensitive to an inhibitor of cathepsin L, a protease previously shown to facilitate HCoV-229E infection. Inhibition of endogenous cathepsin L or TMPRSS2 demonstrated that both proteases can activate 229E-S for entry into cells that are naturally susceptible to infection. In addition, evidence was obtained that activation by TMPRSS2 rescues 229E-S-dependent cell entry from inhibition by IFITM proteins. Finally, immunohistochemistry revealed that TMPRSS2 is coexpressed with CD13, the HCoV-229E receptor, in human airway epithelial (HAE) cells, and that CD13\n +\n TMPRSS2\n +\n cells are preferentially targeted by HCoV-229E, suggesting that TMPRSS2 can activate HCoV-229E in infected humans. In sum, our results indicate that HCoV-229E can employ redundant proteolytic pathways to ensure its activation in host cells. In addition, our observations and previous work suggest that diverse human respiratory viruses are activated by TMPRSS2, which may constitute a target for antiviral intervention."],["dc.identifier.doi","10.1128/JVI.03372-12"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114884"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.rights.uri","https://journals.asm.org/non-commercial-tdm-license"],["dc.title","TMPRSS2 Activates the Human Coronavirus 229E for Cathepsin-Independent Host Cell Entry and Is Expressed in Viral Target Cells in the Respiratory Epithelium"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e49630"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Sinigalia, Elisa"],["dc.contributor.author","Alvisi, Gualtiero"],["dc.contributor.author","Segre, Chiara V."],["dc.contributor.author","Mercorelli, Beatrice"],["dc.contributor.author","Muratore, Giulia"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Hsiao, He-Hsuan"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ripalti, Alessandro"],["dc.contributor.author","Chiocca, Susanna"],["dc.contributor.author","Palu, Giorgio"],["dc.contributor.author","Loregian, Arianna"],["dc.date.accessioned","2018-11-07T09:03:26Z"],["dc.date.available","2018-11-07T09:03:26Z"],["dc.date.issued","2012"],["dc.description.abstract","During the replication of human cytomegalovirus (HCMV) genome, the viral DNA polymerase subunit UL44 plays a key role, as by binding both DNA and the polymerase catalytic subunit it confers processivity to the holoenzyme. However, several lines of evidence suggest that UL44 might have additional roles during virus life cycle. To shed light on this, we searched for cellular partners of UL44 by yeast two-hybrid screenings. Intriguingly, we discovered the interaction of UL44 with Ubc9, an enzyme involved in the covalent conjugation of SUMO (Small Ubiquitin-related MOdifier) to cellular and viral proteins. We found that UL44 can be extensively sumoylated not only in a cell-free system and in transfected cells, but also in HCMV-infected cells, in which about 50% of the protein resulted to be modified at late times post-infection, when viral genome replication is accomplished. Mass spectrometry studies revealed that UL44 possesses multiple SUMO target sites, located throughout the protein. Remarkably, we observed that binding of UL44 to DNA greatly stimulates its sumoylation both in vitro and in vivo. In addition, we showed that overexpression of SUMO alters the intranuclear distribution of UL44 in HCMV-infected cells, and enhances both virus production and DNA replication, arguing for an important role for sumoylation in HCMV life cycle and UL44 function(s). These data report for the first time the sumoylation of a viral processivity factor and show that there is a functional interplay between the HCMV UL44 protein and the cellular sumoylation system."],["dc.identifier.doi","10.1371/journal.pone.0049630"],["dc.identifier.isi","000311272300059"],["dc.identifier.pmid","23166733"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9466"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24902"],["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","The Human Cytomegalovirus DNA Polymerase Processivity Factor UL44 Is Modified by SUMO in a DNA-Dependent Manner"],["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","17510"],["dc.bibliographiccitation.issue","43"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","17515"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Bogdanow, Boris"],["dc.contributor.author","Weisbach, Henry"],["dc.contributor.author","von Einem, Jens"],["dc.contributor.author","Straschewski, Sarah"],["dc.contributor.author","Voigt, Sebastian"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Hagemeier, Christian"],["dc.contributor.author","Wiebusch, Lüder"],["dc.date.accessioned","2022-10-06T13:34:31Z"],["dc.date.available","2022-10-06T13:34:31Z"],["dc.date.issued","2013"],["dc.description.abstract","Significance\n Depending on the host cell type and differentiation status, herpesviruses establish different modes of infection to either maintain or replicate their genomes. How viruses discriminate between individual host cell environments upon infection is poorly understood. Here we identify a viral sensor mechanism that restricts human cytomegalovirus (HCMV) replication to the G0/G1 phase of the cell division cycle and to differentiated cells. The mechanism is based on the HCMV tegument 150-kDa phosphoprotein which enters the cell as a constituent of the virus particle, interacts with cyclin A2, and blocks the onset of viral lytic gene expression when cyclin A2-dependent kinase activity is high. This suggests a scenario where specific tegument–host interactions enable herpesviruses to select sites of silent or productive infection."],["dc.description.abstract","Upon cell entry, herpesviruses deliver a multitude of premade virion proteins to their hosts. The interplay between these incoming proteins and cell-specific regulatory factors dictates the outcome of infections at the cellular level. Here, we report a unique type of virion–host cell interaction that is essential for the cell cycle and differentiation state-dependent onset of human cytomegalovirus (HCMV) lytic gene expression. The major tegument 150-kDa phosphoprotein (pp150) of HCMV binds to cyclin A2 via a functional RXL/Cy motif resulting in its cyclin A2-dependent phosphorylation. Alanine substitution of the RXL/Cy motif prevents this interaction and allows the virus to fully escape the cyclin-dependent kinase (CDK)-mediated block of immediate early (IE) gene expression in S/G2 phase that normally restricts the onset of the HCMV replication cycle to G0/G1. Furthermore, the cyclin A2–CDK–pp150 axis is also involved in the establishment of HCMV quiescence in NTera2 cells, showing the importance of this molecular switch for differentiation state-dependent regulation of IE gene expression. Consistent with the known nucleocapsid-binding function of pp150, its RXL/Cy-dependent phosphorylation affects gene expression of the parental virion only, suggesting a\n cis\n -acting, virus particle-associated mechanism of control. The pp150 homologs of other primate and mammalian CMVs lack an RXL/Cy motif and accordingly even the nearest relative of HCMV, chimpanzee CMV, starts its lytic cycle in a cell cycle-independent manner. Thus, HCMV has evolved a molecular sensor for cyclin A2–CDK activity to restrict its IE gene expression program as a unique level of self-limitation and adaptation to its human host."],["dc.identifier.doi","10.1073/pnas.1312235110"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/115930"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-602"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.relation.orgunit","Deutsches Primatenzentrum"],["dc.title","Human cytomegalovirus tegument protein pp150 acts as a cyclin A2–CDK-dependent sensor of the host cell cycle and differentiation state"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Virology Journal"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Lambertz, Ruth Lydia Olga"],["dc.contributor.author","Gerhauser, Ingo"],["dc.contributor.author","Nehlmeier, Inga"],["dc.contributor.author","Gärtner, Sabine"],["dc.contributor.author","Winkler, Michael"],["dc.contributor.author","Leist, Sarah Rebecca"],["dc.contributor.author","Kollmus, Heike"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Schughart, Klaus"],["dc.date.accessioned","2020-12-10T18:39:01Z"],["dc.date.available","2020-12-10T18:39:01Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1186/s12985-020-01323-z"],["dc.identifier.eissn","1743-422X"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17233"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77513"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","H2 influenza A virus is not pathogenic in Tmprss2 knock-out mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]