Bao, Guobin

[["dc.bibliographiccitation.firstpage","2985"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","European Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","2995"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","de Jong, Danielle"],["dc.contributor.author","Alevra, Mihai"],["dc.contributor.author","Schild, Detlev"],["dc.date.accessioned","2018-11-07T09:48:00Z"],["dc.date.available","2018-11-07T09:48:00Z"],["dc.date.issued","2015"],["dc.description.abstract","Olfactory receptor neurons (ORNs) have high-voltage-gated Ca2+ channels whose physiological impact has remained enigmatic since the voltage-gated conductances in this cell type were first described in the 1980s. Here we show that in ORN somata of Xenopus laevis tadpoles these channels are clustered and co-expressed with large-conductance potassium (BK) channels. We found approximately five clusters per ORN and twelve Ca2+ channels per cluster. The action potential-triggered activation of BK channels accelerates the repolarization of action potentials and shortens interspike intervals during odour responses. This increases the sensitivity of individual ORNs to odorants. At the level of mitral cells of the olfactory bulb, odour qualities have been shown to be coded by first-spike-latency patterns. The system of Ca2+ and BK channels in ORNs appears to be important for correct odour coding because the blockage of BK channels not only affects ORN spiking patterns but also changes the latency pattern representation of odours in the olfactory bulb."],["dc.identifier.doi","10.1111/ejn.13095"],["dc.identifier.isi","000368243100011"],["dc.identifier.pmid","26452167"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35218"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1460-9568"],["dc.relation.issn","0953-816X"],["dc.title","Ca2+-BK channel clusters in olfactory receptor neurons and their role in odour coding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","7129"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Dankovich, Tal M."],["dc.contributor.author","Kaushik, Rahul"],["dc.contributor.author","Olsthoorn, Linda H. M."],["dc.contributor.author","Petersen, Gabriel Cassinelli"],["dc.contributor.author","Giro, Philipp Emanuel"],["dc.contributor.author","Kluever, Verena"],["dc.contributor.author","Agüi-Gonzalez, Paola"],["dc.contributor.author","Grewe, Katharina"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Beuermann, Sabine"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.date.accessioned","2022-01-11T14:05:59Z"],["dc.date.available","2022-01-11T14:05:59Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract The brain extracellular matrix (ECM) consists of extremely long-lived proteins that assemble around neurons and synapses, to stabilize them. The ECM is thought to change only rarely, in relation to neuronal plasticity, through ECM proteolysis and renewed protein synthesis. We report here an alternative ECM remodeling mechanism, based on the recycling of ECM molecules. Using multiple ECM labeling and imaging assays, from super-resolution optical imaging to nanoscale secondary ion mass spectrometry, both in culture and in brain slices, we find that a key ECM protein, Tenascin-R, is frequently endocytosed, and later resurfaces, preferentially near synapses. The TNR molecules complete this cycle within ~3 days, in an activity-dependent fashion. Interfering with the recycling process perturbs severely neuronal function, strongly reducing synaptic vesicle exo- and endocytosis. We conclude that the neuronal ECM can be remodeled frequently through mechanisms that involve endocytosis and recycling of ECM proteins."],["dc.identifier.doi","10.1038/s41467-021-27462-7"],["dc.identifier.pii","27462"],["dc.identifier.pmid","34880248"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/97795"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/371"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/163"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/145"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-507"],["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","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A03: Dynamische Analyse der Remodellierung der extrazellulären Matrix (ECM) als Mechanismus der Synapsenorganisation und Plastizität"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.rights","CC BY 4.0"],["dc.title","Extracellular matrix remodeling through endocytosis and resurfacing of Tenascin-R"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1740"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cell Stem Cell"],["dc.bibliographiccitation.lastpage","1757.e8"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Gabriel, Elke"],["dc.contributor.author","Albanna, Walid"],["dc.contributor.author","Pasquini, Giovanni"],["dc.contributor.author","Ramani, Anand"],["dc.contributor.author","Josipovic, Natasa"],["dc.contributor.author","Mariappan, Aruljothi"],["dc.contributor.author","Schinzel, Friedrich"],["dc.contributor.author","Karch, Celeste M."],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Gottardo, Marco"],["dc.contributor.author","Gopalakrishnan, Jay"],["dc.date.accessioned","2021-12-01T09:24:16Z"],["dc.date.available","2021-12-01T09:24:16Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.stem.2021.07.010"],["dc.identifier.pii","S1934590921002952"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94898"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.issn","1934-5909"],["dc.title","Human brain organoids assemble functionally integrated bilateral optic vesicles"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e90500"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Schild, Detlev"],["dc.date.accessioned","2018-11-07T09:42:40Z"],["dc.date.available","2018-11-07T09:42:40Z"],["dc.date.issued","2014"],["dc.description.abstract","The parameters of experimentally obtained exponentials are usually found by least-squares fitting methods. Essentially, this is done by minimizing the mean squares sum of the differences between the data, most often a function of time, and a parameter-defined model function. Here we delineate a novel method where the noisy data are represented and analyzed in the space of Legendre polynomials. This is advantageous in several respects. First, parameter retrieval in the Legendre domain is typically two orders of magnitude faster than direct fitting in the time domain. Second, data fitting in a low-dimensional Legendre space yields estimates for amplitudes and time constants which are, on the average, more precise compared to least-squares-fitting with equal weights in the time domain. Third, the Legendre analysis of two exponentials gives satisfactory estimates in parameter ranges where least-squares-fitting in the time domain typically fails. Finally, filtering exponentials in the domain of Legendre polynomials leads to marked noise removal without the phase shift characteristic for conventional lowpass filters."],["dc.identifier.doi","10.1371/journal.pone.0090500"],["dc.identifier.isi","000332483600058"],["dc.identifier.pmid","24603904"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10017"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34009"],["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 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Fast and Accurate Fitting and Filtering of Noisy Exponentials in Legendre Space"],["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","202"],["dc.bibliographiccitation.journal","Acta Physiologica"],["dc.bibliographiccitation.lastpage","204"],["dc.bibliographiccitation.volume","210"],["dc.contributor.author","Mueller, M."],["dc.contributor.author","Kizina, K."],["dc.contributor.author","Bao, Guobin"],["dc.date.accessioned","2018-11-07T09:42:49Z"],["dc.date.available","2018-11-07T09:42:49Z"],["dc.date.issued","2014"],["dc.identifier.isi","000332259900526"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34042"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1748-1716"],["dc.relation.issn","1748-1708"],["dc.title","Advanced ROS/redox imaging based on genetically-encoded probes, ratiometric 2-photon microscopy and fluorescence-lifetime imaging"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1542"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","ACS Chemical Neuroscience"],["dc.bibliographiccitation.lastpage","1551"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Agüi-Gonzalez, Paola"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Gomes de Castro, Maria Angela"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.contributor.author","Phan, Nhu T. N."],["dc.date.accessioned","2021-06-01T09:41:35Z"],["dc.date.available","2021-06-01T09:41:35Z"],["dc.date.issued","2021"],["dc.description.abstract","The cellular functions of lipids in the neuronal plasma membranes have been increasingly acknowledged, particularly their association to neuronal processes and synaptic plasticity. However, the knowledge of their regulatory mechanisms in neuronal cells remains sparse. To address this, we investigated the lipid organization of the plasma membranes of hippocampal neurons in relation to neuronal activity using secondary ion mass spectrometry imaging. The neurons were treated with drugs, particularly tetrodotoxin (TTX) and bicuculline (BIC), to induce chronic activation and silencing. Distinct lipid organization was found in the plasma membrane of the cell body and the neurites. Moreover, significant alterations of the levels of the membrane lipids, especially ceramides, phosphatidylserines, phosphatidic acids, and triacylglycerols, were observed under the TTX and BIC treatments. We suggest that many types of membrane lipids are affected by, and may be involved in, the regulation of neuronal function."],["dc.identifier.doi","10.1021/acschemneuro.1c00031"],["dc.identifier.pmid","33896172"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/84972"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/119"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation.eissn","1948-7193"],["dc.relation.issn","1948-7193"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.rights","CC BY 4.0"],["dc.title","Secondary Ion Mass Spectrometry Imaging Reveals Changes in the Lipid Structure of the Plasma Membranes of Hippocampal Neurons following Drugs Affecting Neuronal Activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","227"],["dc.bibliographiccitation.journal","Free Radical Biology & Medicine"],["dc.bibliographiccitation.lastpage","241"],["dc.bibliographiccitation.volume","76"],["dc.contributor.author","Weller, Jonathan"],["dc.contributor.author","Kizina, Kathrin M."],["dc.contributor.author","Can, Karolina"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Müller, Michael"],["dc.date.accessioned","2018-09-28T09:56:42Z"],["dc.date.available","2018-09-28T09:56:42Z"],["dc.date.issued","2014"],["dc.description.abstract","Reactive oxygen species mediate cellular signaling and neuropathologies. Hence, there is tremendous interest in monitoring (sub)cellular redox conditions. We evaluated the genetically engineered redox sensor HyPer in mouse hippocampal cell cultures. Two days after lipofection, neurons and glia showed sufficient expression levels, and H2O2 reversibly and dose-dependently increased the fluorescence ratio of cytosolic HyPer. Yet, repeated H2O2 treatment caused progressively declining responses, and with millimolar doses an apparent recovery started while H2O2 was still present. Although HyPer should be H2O2 specific, it seemingly responded also to other oxidants and altered cell-endogenous superoxide production. Control experiments with the SypHer pH sensor confirmed that the HyPer ratio responds to pH changes, decreasing with acidosis and increasing during alkalosis. Anoxia/reoxygenation evoked biphasic HyPer responses reporting apparent reduction/oxidation; replacing Cl(-) exerted only negligible effects. Mitochondria-targeted HyPer readily responded to H2O2-albeit less intensely than cytosolic HyPer. With ratiometric two-photon excitation, H2O2 increased the cytosolic HyPer ratio. Time-correlated fluorescence-lifetime imaging microscopy (FLIM) revealed a monoexponential decay of HyPer fluorescence, and H2O2 decreased fluorescence lifetimes. Dithiothreitol failed to further reduce HyPer or to induce reasonable FLIM and two-photon responses. By enabling dynamic recordings, HyPer is superior to synthetic redox-sensitive dyes. Its feasibility for two-photon excitation also enables studies in more complex preparations. Based on FLIM, quantitative analyses might be possible independent of switching excitation wavelengths. Yet, because of its pronounced pH sensitivity, adaptation to repeated oxidation, and insensitivity to reducing stimuli, HyPer responses have to be interpreted carefully. For reliable data, side-by-side pH monitoring with SypHer is essential."],["dc.identifier.doi","10.1016/j.freeradbiomed.2014.07.045"],["dc.identifier.pmid","25179473"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15849"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1873-4596"],["dc.title","Response properties of the genetically encoded optical H2O2 sensor HyPer"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1503"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1516"],["dc.bibliographiccitation.volume","1783"],["dc.contributor.author","Kobe, Fritz"],["dc.contributor.author","Renner, Ute"],["dc.contributor.author","Woehler, Andrew"],["dc.contributor.author","Wlodarczyk, Jakub"],["dc.contributor.author","Papusheva, Ekaterina"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Zeug, Andre"],["dc.contributor.author","Richter, Diethelm W."],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","Ponimaskin, Evgeni G."],["dc.date.accessioned","2018-11-07T11:12:17Z"],["dc.date.available","2018-11-07T11:12:17Z"],["dc.date.issued","2008"],["dc.description.abstract","In the present study we analyzed the oligomerization state of the serotonin 5-HT1A receptor and studied oligomerization dynamics in living cells. We also investigated the role of receptor palmitoylation in this process. Biochemical analysis performed in neuroblastoma N1E-115 cells demonstrated that both palmitoylated and non-palmitoylated 5-HT1A receptors form homo-oligomers and that the prevalent receptor species at the plasma membrane are dimers. A combination of an acceptor-photobleaching FRET approach with fluorescence lifetime measurements verified the interaction of CFP- and YFP-labeled wild-type as well as acylation-deficient 5-HT1A receptors at the plasma membrane of living cells. Using a novel FRET technique based on the spectral analysis we also confirmed the specific nature of receptor oligomerization. The analysis of oligomerization dynamics revealed that apparent FRET efficiency measured for wild-type oligomers significantly decreased in response to agonist stimulation, and our combined results suggest that this decrease was mediated by accumulation of FRET-negative complexes rather than by dissociation of oligomers to monomers. In contrast, the agonist-mediated decrease of FRET signal was completely abolished in oligomers composed by non-palmitoylated receptor mutants, demonstrating the importance of palmitoylation in modulation of the structure of oligomers. (C) 2008 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2008.02.021"],["dc.identifier.isi","000257641600004"],["dc.identifier.pmid","18381076"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7758"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53629"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0167-4889"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Stimulation- and palmitoylation-dependent changes in oligomeric conformation of serotonin 5-HT1A receptors"],["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","41"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Antioxidants & Redox Signaling"],["dc.bibliographiccitation.lastpage","58"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Wagener, Kerstin C."],["dc.contributor.author","Kolbrink, Benedikt"],["dc.contributor.author","Dietrich, Katharina"],["dc.contributor.author","Kizina, Kathrin M."],["dc.contributor.author","Terwitte, Lukas S."],["dc.contributor.author","Kempkes, Belinda"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Müller, Michael"],["dc.date.accessioned","2018-09-28T09:52:54Z"],["dc.date.available","2018-09-28T09:52:54Z"],["dc.date.issued","2016"],["dc.description.abstract","Reactive oxygen species (ROS) and downstream redox alterations not only mediate physiological signaling but also neuropathology. For long, ROS/redox imaging was hampered by a lack of reliable probes. Genetically encoded redox sensors overcame this gap and revolutionized (sub)cellular redox imaging. Yet, the successful delivery of sensor-coding DNA, which demands transfection/transduction of cultured preparations or stereotaxic microinjections of each subject, remains challenging. By generating transgenic mice, we aimed to overcome limiting cultured preparations, circumvent surgical interventions, and to extend effectively redox imaging to complex and adult preparations."],["dc.identifier.doi","10.1089/ars.2015.6587"],["dc.identifier.pmid","27059697"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15848"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1557-7716"],["dc.title","Redox Indicator Mice Stably Expressing Genetically Encoded Neuronal roGFP: Versatile Tools to Decipher Subcellular Redox Dynamics in Neuropathophysiology"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","23419"],["dc.bibliographiccitation.issue","26"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","23431"],["dc.bibliographiccitation.volume","286"],["dc.contributor.author","Salonikidis, Petrus S."],["dc.contributor.author","Niebert, Marcus"],["dc.contributor.author","Ullrich, Tim"],["dc.contributor.author","Bao, Guobin"],["dc.contributor.author","Zeug, Andre"],["dc.contributor.author","Richter, Diethelm W."],["dc.date.accessioned","2018-11-07T08:54:48Z"],["dc.date.available","2018-11-07T08:54:48Z"],["dc.date.issued","2011"],["dc.description.abstract","Ratiometric measurements with FRET-based biosensors in living cells using a single fluorescence excitation wavelength are often affected by a significant ion sensitivity and the aggregation behavior of the FRET pair. This is an important problem for quantitative approaches. Here we report on the influence of physiological ion concentration changes on quantitative ratiometric measurements by comparing different FRET pairs for a cAMP-detecting biosensor. We exchanged the enhanced CFP/enhanced YFP FRET pair of an established Epac1-based biosensor by the fluorophores mCerulean/mCitrine. In the case of enhanced CFP/enhanced YFP, we showed that changes in proton, and (to a lesser extent) chloride ion concentrations result in incorrect ratiometric FRET signals, which may exceed the dynamic range of the biosensor. Calcium ions have no direct, but an indirect pH-driven effect by mobilizing protons. These ion dependences were greatly eliminated when mCerulean/mCitrine fluorophores were used. For such advanced FRET pairs the biosensor is less sensitive to changes in ion concentration and allows consistent cAMP concentration measurements under different physiological conditions, as occur in metabolically active cells. In addition, we verified that the described FRET pair exchange increased the dynamic range of the FRET efficiency response. The time window for stable experimental conditions was also prolonged by a faster biosensor expression rate in transfected cells and a greatly reduced tendency to aggregate, which reduces cytotoxicity. These properties were verified in functional tests in single cells co-expressing the biosensor and the 5-HT1A receptor."],["dc.identifier.doi","10.1074/jbc.M111.236869"],["dc.identifier.isi","000292025000073"],["dc.identifier.pmid","21454618"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7623"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22755"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","An Ion-insensitive cAMP Biosensor for Long Term Quantitative Ratiometric Fluorescence Resonance Energy Transfer (FRET) Measurements under Variable Physiological Conditions"],["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"]]