Opazo Davila, Luis Felipe

[["dc.bibliographiccitation.firstpage","26349"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","26355"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Saul, Philip"],["dc.contributor.author","Yang, Shengjun"],["dc.contributor.author","Mamone, Salvatore"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Meyer, Andreas"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Glöggler, Stefan"],["dc.date.accessioned","2021-12-01T09:20:55Z"],["dc.date.available","2021-12-01T09:20:55Z"],["dc.date.issued","2021"],["dc.description.abstract","Dendrimers display an exotic spin state behavior that we propose to tune for ion sensing."],["dc.description.abstract","Dendrimers are a class of branched, highly symmetric macromolecules that have been shown to be useful for a vast number of different applications. Potential uses as fluorescence sensors, in catalysis and perhaps most importantly in medical applications as drug delivery systems or cytotoxica have been proposed. Herein we report on an exotic behaviour of the nuclear spins in a dendritic macromolecule in the presence of different paramagnetic ions. We show that the stability of the long lived nuclear singlet state, is affected by the presence of Cu( ii ), whereas other ions did not have any influence at all. This effect could not be observed in the case of a simple tripeptide, in which the nuclear singlet stability was influenced by all investigated paramagnetic ions, a potentially useful effect in the development of Cu( ii ) selective probes. By adding a fluorescent marker to our molecule we could show that the nuclear singlet multimer (NUSIMER) is taken up by living cells. Furthermore we were able to show that nuclear singlet state NMR can be used to investigate the NUSIMER in the presence of living cells, showing that an application in in vivo NMR can be feasible."],["dc.description.abstract","Dendrimers display an exotic spin state behavior that we propose to tune for ion sensing."],["dc.description.abstract","Dendrimers are a class of branched, highly symmetric macromolecules that have been shown to be useful for a vast number of different applications. Potential uses as fluorescence sensors, in catalysis and perhaps most importantly in medical applications as drug delivery systems or cytotoxica have been proposed. Herein we report on an exotic behaviour of the nuclear spins in a dendritic macromolecule in the presence of different paramagnetic ions. We show that the stability of the long lived nuclear singlet state, is affected by the presence of Cu( ii ), whereas other ions did not have any influence at all. This effect could not be observed in the case of a simple tripeptide, in which the nuclear singlet stability was influenced by all investigated paramagnetic ions, a potentially useful effect in the development of Cu( ii ) selective probes. By adding a fluorescent marker to our molecule we could show that the nuclear singlet multimer (NUSIMER) is taken up by living cells. Furthermore we were able to show that nuclear singlet state NMR can be used to investigate the NUSIMER in the presence of living cells, showing that an application in in vivo NMR can be feasible."],["dc.identifier.doi","10.1039/D1CP04483D"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94301"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","1463-9084"],["dc.relation.issn","1463-9076"],["dc.rights.uri","http://creativecommons.org/licenses/by/3.0/"],["dc.title","Exotic nuclear spin behavior in dendritic macromolecules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13221"],["dc.bibliographiccitation.issue","67"],["dc.bibliographiccitation.journal","Chemical Communications"],["dc.bibliographiccitation.lastpage","13224"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Kabatas, Selda"],["dc.contributor.author","Vreja, Ingrid C."],["dc.contributor.author","Saka, Sinem K."],["dc.contributor.author","Hoeschen, Carmen"],["dc.contributor.author","Kroehnert, Katharina"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Rizzoli, S. O."],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:44:43Z"],["dc.date.available","2017-09-07T11:44:43Z"],["dc.date.issued","2015"],["dc.description.abstract","Imaging techniques should differentiate between specific signals, from the biomolecules of interest, and non-specific signals, from the background. We present a probe containing N-15 and N-14 isotopes in approximately equal proportion, for secondary ion mass spectrometry imaging. This probe designed for a precise biomolecule analysis is insensitive to background signals."],["dc.identifier.doi","10.1039/c5cc03895b"],["dc.identifier.gro","3141979"],["dc.identifier.isi","000359246500017"],["dc.identifier.pmid","26195041"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3201"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1364-548X"],["dc.relation.issn","1359-7345"],["dc.title","A contamination-insensitive probe for imaging specific biomolecules by secondary ion mass spectrometry"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","427"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Communicative & Integrative Biology"],["dc.bibliographiccitation.lastpage","429"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Rizzoli, S. O."],["dc.date.accessioned","2017-09-07T11:54:04Z"],["dc.date.available","2017-09-07T11:54:04Z"],["dc.date.issued","2010"],["dc.description.abstract","Neurotransmitter release relies on the fusion of synaptic vesicles with the plasma membrane of synaptic boutons, which is followed by the recycling of vesicle components and formation of new vesicles. It is not yet clear whether upon fusion the vesicles persist as multimolecular patches in the plasma membrane, or whether they segregate into individual components. Evidence supporting each of these two models has been suggested in recent years. Using diffraction-unlimited imaging (stimulated emission depletion, or STED) of native synaptic vesicle proteins, we have proposed that vesicle proteins remain in clusters on the neuronal surface. These clusters do not appear to intermix. We discuss here these findings in the context of previous studies on synaptic vesicle fusion, and we propose a recycling model which accounts for most of the recent findings on the post-fusion fate of synaptic vesicle components."],["dc.identifier.doi","10.4161/cib.3.5.12132"],["dc.identifier.gro","3145094"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2793"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","1942-0889"],["dc.title","The fate of synaptic vesicle components upon fusion"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["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","16913"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Mandad, Sunit"],["dc.contributor.author","Rahman, Raza-Ur"],["dc.contributor.author","Centeno, Tonatiuh Pena"],["dc.contributor.author","Vidal, Ramon O."],["dc.contributor.author","Wildhagen, Hanna"],["dc.contributor.author","Rammner, Burkhard"],["dc.contributor.author","Keihani, Sarva"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Urban, Inga"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Kirli, Koray"],["dc.contributor.author","Benito, Eva"],["dc.contributor.author","Fischer, André"],["dc.contributor.author","Yousefi, Roya Y."],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Feußner, Ivo"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.date.accessioned","2019-07-09T11:50:21Z"],["dc.date.available","2019-07-09T11:50:21Z"],["dc.date.issued","2018"],["dc.description.abstract","The homeostasis of the proteome depends on the tight regulation of the mRNA and protein abundances, of the translation rates, and of the protein lifetimes. Results from several studies on prokaryotes or eukaryotic cell cultures have suggested that protein homeostasis is connected to, and perhaps regulated by, the protein and the codon sequences. However, this has been little investigated for mammals in vivo. Moreover, the link between the coding sequences and one critical parameter, the protein lifetime, has remained largely unexplored, both in vivo and in vitro. We tested this in the mouse brain, and found that the percentages of amino acids and codons in the sequences could predict all of the homeostasis parameters with a precision approaching experimental measurements. A key predictive element was the wobble nucleotide. G-/C-ending codons correlated with higher protein lifetimes, protein abundances, mRNA abundances and translation rates than A-/U-ending codons. Modifying the proportions of G-/C-ending codons could tune these parameters in cell cultures, in a proof-of-principle experiment. We suggest that the coding sequences are strongly linked to protein homeostasis in vivo, albeit it still remains to be determined whether this relation is causal in nature."],["dc.identifier.doi","10.1038/s41598-018-35277-8"],["dc.identifier.pmid","30443017"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15918"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59754"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/209"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/44"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/339580/EU//MITRAC"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/614765/EU//NEUROMOLANATOMY"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P09: Proteinsortierung in der Synapse: Prinzipien und molekulare Organisation"],["dc.relation.issn","2045-2322"],["dc.relation.workinggroup","RG A. Fischer (Epigenetics and Systems Medicine in Neurodegenerative Diseases)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","The codon sequences predict protein lifetimes and other parameters of the protein life cycle in the mouse brain"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e21"],["dc.bibliographiccitation.journal","Molecular Therapy — Nucleic Acids"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Wilner, Samantha E."],["dc.contributor.author","Wengerter, Brian"],["dc.contributor.author","Maier, Keith"],["dc.contributor.author","Borba Magalhaes, Maria de Lourdes"],["dc.contributor.author","Amo, David Soriano del"],["dc.contributor.author","Pai, Supriya"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Rizzoli, S. O."],["dc.contributor.author","Yan, Amy"],["dc.contributor.author","Levy, Matthew"],["dc.date.accessioned","2017-09-07T11:48:53Z"],["dc.date.available","2017-09-07T11:48:53Z"],["dc.date.issued","2012"],["dc.description.abstract","The transferrin receptor, CD71, is an attractive target for drug development because of its high expression on a number of cancer cell lines and the blood brain barrier. To generate serum-stabilized aptamers that recognize the human transferrin receptor, we have modified the traditional aptamer selection protocol by employing a functional selection step that enriches for RNA molecules which bind the target receptor and are internalized by cells. Selected aptamers were specific for the human receptor, rapidly endocytosed by cells and shared a common core structure. A minimized variant was found to compete with the natural ligand, transferrin, for receptor binding and cell uptake, but performed similar to twofold better than it in competition experiments. Using this molecule, we generated aptamer-targeted siRNA-laden liposomes. Aptamer targeting enhanced both uptake and target gene knockdown in cells grown in culture when compared to nonmodified or nontargeted liposomes. The aptamer should prove useful as a surrogate for transferrin in many applications including cell imaging and targeted drug delivery."],["dc.identifier.doi","10.1038/mtna.2012.14"],["dc.identifier.gro","3142542"],["dc.identifier.isi","000208875500001"],["dc.identifier.pmid","23344001"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8904"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2162-2531"],["dc.title","An RNA Alternative to Human Transferrin: A New Tool for Targeting Human Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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","436"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","BioEssays"],["dc.bibliographiccitation.lastpage","451"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.contributor.author","Opazo, Felipe"],["dc.date.accessioned","2018-11-07T09:59:15Z"],["dc.date.available","2018-11-07T09:59:15Z"],["dc.date.issued","2015"],["dc.description.abstract","The recent 2014 Nobel Prize in chemistry honored an era of discoveries and technical advancements in the field of super-resolution microscopy. However, the applications of diffraction-unlimited imaging in biology have a long road ahead and persistently engage scientists with new challenges. Some of the bottlenecks that restrain the dissemination of super-resolution techniques are tangible, and include the limited performance of affinity probes and the yet not capillary diffusion of imaging setups. Likewise, super-resolution microscopy has introduced new paradigms in the design of projects that require imaging with nanometer-resolution and in the interpretation of biological images. Besides structural or morphological characterization, super-resolution imaging is quickly expanding towards interaction mapping, multiple target detection and live imaging. Here we review the recent progress of biologists employing super-resolution imaging, some pitfalls, implications and new trends, with the purpose of animating the field and spurring future developments."],["dc.identifier.doi","10.1002/bies.201400170"],["dc.identifier.isi","000351546000013"],["dc.identifier.pmid","25581819"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37549"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1521-1878"],["dc.relation.issn","0265-9247"],["dc.title","Super-resolution imaging for cell biologists Concepts, applications, current challenges and developments"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","7977"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Ta, Haisen"],["dc.contributor.author","Keller, Jan"],["dc.contributor.author","Haltmeier, Markus"],["dc.contributor.author","Saka, Sinem K."],["dc.contributor.author","Schmied, Juregen"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Tinnefeld, Philip"],["dc.contributor.author","Munk, Axel"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:43:37Z"],["dc.date.available","2017-09-07T11:43:37Z"],["dc.date.issued","2015"],["dc.description.abstract","In fluorescence microscopy, the distribution of the emitting molecule number in space is usually obtained by dividing the measured fluorescence by that of a single emitter. However, the brightness of individual emitters may vary strongly in the sample or be inaccessible. Moreover, with increasing (super-) resolution, fewer molecules are found per pixel, making this approach unreliable. Here we map the distribution of molecules by exploiting the fact that a single molecule emits only a single photon at a time. Thus, by analysing the simultaneous arrival of multiple photons during confocal imaging, we can establish the number and local brightness of typically up to 20 molecules per confocal (diffraction sized) recording volume. Subsequent recording by stimulated emission depletion microscopy provides the distribution of the number of molecules with subdiffraction resolution. The method is applied to mapping the three-dimensional nanoscale organization of internalized transferrin receptors on human HEK293 cells."],["dc.identifier.doi","10.1038/ncomms8977"],["dc.identifier.gro","3141850"],["dc.identifier.isi","000360346900018"],["dc.identifier.pmid","26269133"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13587"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1767"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Mapping molecules in scanning far-field fluorescence nanoscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e251"],["dc.bibliographiccitation.journal","Molecular Therapy — Nucleic Acids"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Eiden, Laura"],["dc.contributor.author","Hansen, Line"],["dc.contributor.author","Rohrbach, Falk"],["dc.contributor.author","Wengel, Jesper"],["dc.contributor.author","Kjems, Jorgen"],["dc.contributor.author","Mayer, Guenter"],["dc.date.accessioned","2018-11-07T09:51:53Z"],["dc.date.available","2018-11-07T09:51:53Z"],["dc.date.issued","2015"],["dc.description.abstract","Aptamers are valuable tools that provide great potential to develop cost-effective diagnostics and therapies in the biomedical field. Here, we report a novel DNA aptamer that folds into an unconventional G-quadruplex structure able to recognize and enter specifically into human Burkitt's lymphoma cells. We further optimized this aptamer to a highly versatile and stable minimized version. The minimized aptamer can be easily equipped with different functionalities like quantum dots, organic dyes, or even a second different aptamer domain yielding a bi-paratopic aptamer. Although the target molecule of the aptamer remains unknown, our microscopy and pharmacological studies revealed that the aptamer hijacks the clathrin-mediated endocytosis pathway for its cellular internalization. We conclude that this novel class of aptamers can be used as a modular tool to specifically deliver different cargoes into malignant cells. This work provides a thorough characterization of the aptamer and we expect that our strategy will pave the path for future therapeutic applications."],["dc.identifier.doi","10.1038/mtna.2015.25"],["dc.identifier.isi","000368911800002"],["dc.identifier.pmid","26325628"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12867"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36003"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2162-2531"],["dc.rights","CC BY-NC-SA 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/4.0"],["dc.title","Modular Assembly of Cell-targeting Devices Based on an Uncommon G-quadruplex Aptamer"],["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"]]