Gomes de Castro, Maria Angela

[["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.artnumber","e0173050"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","de Castro, Maria Angela Gomes"],["dc.contributor.author","Hoebartner, Claudia"],["dc.contributor.author","Opazo, Felipe"],["dc.date.accessioned","2018-11-07T10:27:12Z"],["dc.date.available","2018-11-07T10:27:12Z"],["dc.date.issued","2017"],["dc.description.abstract","Continuous improvements in imaging techniques are challenging biologists to search for more accurate methods to label cellular elements. This is particularly relevant for diffraction-unlimited fluorescence imaging, where the perceived resolution is affected by the size of the affinity probes. This is evident when antibodies, which are 10-15 nm in size, are used. Previously it has been suggested that RNA aptamers (similar to 3 nm) can be used to detect cellular proteins under super-resolution imaging. However, a direct comparison between several aptamers and antibodies is needed, to clearly show the advantages and/or disadvantages of the different probes. Here we have conducted such a comparative study, by testing several aptamers and antibodies using stimulated emission depletion microscopy (STED). We have targeted three membrane receptors, EGFR, ErbB2 and Epha2, which are relevant to human health, and recycle between plasma membrane and intracellular organelles. Our results suggest that the aptamers can reveal more epitopes than most antibodies, thus providing a denser labeling of the stained structures. Moreover, this improves the overall quality of the information that can be extracted from the images. We conclude that aptamers could become useful fluorescent labeling tools for light microscopy and super-resolution imaging, and that their development for novel targets is imperative."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2017"],["dc.identifier.doi","10.1371/journal.pone.0173050"],["dc.identifier.isi","000394688200190"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14378"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43201"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Aptamers provide superior stainings of cellular receptors studied under super-resolution microscopy"],["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.issue","17"],["dc.bibliographiccitation.journal","BIO-PROTOCOL"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Gomes de Castro, Maria Angela"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Opazo, Felipe"],["dc.date.accessioned","2020-12-10T18:43:03Z"],["dc.date.available","2020-12-10T18:43:03Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.21769/BioProtoc.2541"],["dc.identifier.issn","2331-8325"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78178"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Staining of Membrane Receptors with Fluorescently-labeled DNA Aptamers for Super-resolution Imaging"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]