Opazo Davila, Luis Felipe

[["dc.bibliographiccitation.firstpage","4744"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The Analyst"],["dc.bibliographiccitation.lastpage","4747"],["dc.bibliographiccitation.volume","146"],["dc.contributor.author","Glowacki, Selda Kabatas"],["dc.contributor.author","Gomes de Castro, Maria Angela"],["dc.contributor.author","Yip, Ka Man"],["dc.contributor.author","Asadpour, Ommolbanin"],["dc.contributor.author","Münchhalfen, Matthias"],["dc.contributor.author","Engels, Niklas"],["dc.contributor.author","Opazo, Felipe"],["dc.date.accessioned","2021-08-12T07:45:03Z"],["dc.date.available","2021-08-12T07:45:03Z"],["dc.date.issued","2021"],["dc.description.abstract","Monovalent NIP probes for studying B cell antigen receptors in fluorescence-based techniques, including diffraction unlimited microscopy."],["dc.description.abstract","We have developed a series of monovalent fluorophore-conjugated affinity probes based on the hapten 3-nitro-4-hydroxy-5-iodophenylacetyl (NIP), which is widely used as a model antigen to study B lymphocytes and the functional principles of B cell antigen receptors (BCRs). We successfully used them in flow-cytometry, confocal and super-resolution microscopy techniques."],["dc.description.abstract","Monovalent NIP probes for studying B cell antigen receptors in fluorescence-based techniques, including diffraction unlimited microscopy."],["dc.description.abstract","We have developed a series of monovalent fluorophore-conjugated affinity probes based on the hapten 3-nitro-4-hydroxy-5-iodophenylacetyl (NIP), which is widely used as a model antigen to study B lymphocytes and the functional principles of B cell antigen receptors (BCRs). We successfully used them in flow-cytometry, confocal and super-resolution microscopy techniques."],["dc.identifier.doi","10.1039/D1AN00601K"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/88359"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-448"],["dc.relation.eissn","1364-5528"],["dc.relation.issn","0003-2654"],["dc.title","A fluorescent probe for STED microscopy to study NIP-specific B cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","820"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Gomes de Castro, Maria Angela"],["dc.contributor.author","Wildhagen, Hanna"],["dc.contributor.author","Sograte-Idrissi, Shama"],["dc.contributor.author","Hitzing, Christoffer"],["dc.contributor.author","Binder, Mascha"],["dc.contributor.author","Trepel, Martin"],["dc.contributor.author","Engels, Niklas"],["dc.contributor.author","Opazo, Felipe"],["dc.date.accessioned","2019-07-09T11:50:13Z"],["dc.date.available","2019-07-09T11:50:13Z"],["dc.date.issued","2019"],["dc.description.abstract","Stimulation of the B cell antigen receptor (BCR) triggers signaling pathways that promote the differentiation of B cells into plasma cells. Despite the pivotal function of BCR in B cell activation, the organization of the BCR on the surface of resting and antigen-activated B cells remains unclear. Here we show, using STED super-resolution microscopy, that IgM-containing BCRs exist predominantly as monomers and dimers in the plasma membrane of resting B cells, but form higher oligomeric clusters upon stimulation. By contrast, a chronic lymphocytic leukemia-derived BCR forms dimers and oligomers in the absence of a stimulus, but a single amino acid exchange reverts its organization to monomers in unstimulated B cells. Our super-resolution microscopy approach for quantitatively analyzing cell surface proteins may thus help reveal the nanoscale organization of immunoreceptors in various cell types."],["dc.identifier.doi","10.1038/s41467-019-08677-1"],["dc.identifier.pmid","30778055"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15884"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59725"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Differential organization of tonic and chronic B cell antigen receptors in the plasma membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","441"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","European Journal of Immunology"],["dc.bibliographiccitation.lastpage","453"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Vanshylla, Kanika"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Gronke, Konrad"],["dc.contributor.author","Wienands, Jürgen"],["dc.contributor.author","Engels, Niklas"],["dc.date.accessioned","2020-12-10T14:06:25Z"],["dc.date.available","2020-12-10T14:06:25Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1002/eji.v48.3"],["dc.identifier.issn","0014-2980"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69888"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The extracellular membrane-proximal domain of membrane-bound IgE restricts B cell activation by limiting B cell antigen receptor surface expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Götzke, Hansjörg"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Martínez-Carranza, Markel"],["dc.contributor.author","Sograte-Idrissi, Shama"],["dc.contributor.author","Rajavel, Abirami"],["dc.contributor.author","Schlichthaerle, Thomas"],["dc.contributor.author","Engels, Niklas"],["dc.contributor.author","Jungmann, Ralf"],["dc.contributor.author","Stenmark, Pål"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Frey, Steffen"],["dc.date.accessioned","2020-12-10T18:09:51Z"],["dc.date.available","2020-12-10T18:09:51Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41467-019-12301-7"],["dc.identifier.eissn","2041-1723"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16514"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73776"],["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","The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]