Rhee, Jeong-Seop

[["dc.bibliographiccitation.firstpage","473"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","487"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Burgalossi, Andrea"],["dc.contributor.author","Jung, Sangyong"],["dc.contributor.author","Meyer, Guido"],["dc.contributor.author","Jockusch, Wolf J."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","O'Connor, V. M."],["dc.contributor.author","Nishiki, Tei-ichi"],["dc.contributor.author","Takahashi, Masami"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.date.accessioned","2017-09-07T11:45:13Z"],["dc.date.available","2017-09-07T11:45:13Z"],["dc.date.issued","2010"],["dc.description.abstract","Neurotransmitter release proceeds by Ca(2+)-triggered, SNARE-complex-dependent synaptic vesicle fusion. After fusion, the ATPase NSF and its cofactors alpha- and beta SNAP disassemble SNARE complexes, thereby recycling individual SNAREs for subsequent fusion reactions. We examined the effects of genetic perturbation of alpha- and beta SNAP expression on synaptic vesicle exocytosis, employing a new Ca(2+) uncaging protocol to study synaptic vesicle trafficking, priming, and fusion in small glutamatergic synapses of hippocampal neurons. By characterizing this protocol, we show that synchronous and asynchronous transmitter release involve different Ca(2+) sensors and are not caused by distinct releasable vesicle pools, and that tonic transmitter release is due to ongoing priming and fusion of new synaptic vesicles during high synaptic activity. Our analysis of alpha- and beta SNAP deletion mutant neurons shows that the two NSF cofactors support synaptic vesicle priming by determining the availability of free SNARE components, particularly during phases of high synaptic activity."],["dc.identifier.doi","10.1016/j.neuron.2010.09.019"],["dc.identifier.gro","3142831"],["dc.identifier.isi","000284255800015"],["dc.identifier.pmid","21040848"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/278"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max Planck Society; European Community [MEST-CT-2004-504193]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0896-6273"],["dc.title","SNARE Protein Recycling by alpha SNAP and beta SNAP Supports Synaptic Vesicle Priming"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","389"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","401"],["dc.bibliographiccitation.volume","118"],["dc.contributor.author","Junge, Harald J."],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Varoqueaux, Frederique"],["dc.contributor.author","Spiess, Joachim"],["dc.contributor.author","Waxham, M. N."],["dc.contributor.author","Rosenmund, C."],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:43:16Z"],["dc.date.available","2017-09-07T11:43:16Z"],["dc.date.issued","2004"],["dc.description.abstract","The efficacy of synaptic transmission between neurons can be altered transiently during neuronal network activity. This phenomenon of short-term plasticity is a key determinant of network properties; is involved in many physiological processes such as motor control, sound localization, or sensory adaptation; and is critically dependent on cytosolic [Call]. However, the underlying molecular mechanisms and the identity of the Ca²⁺ sensor/effector complexes involved are unclear. We now identify a conserved calmodulin binding site in UNC-13/Munc13s, which are essential regulators of synaptic vesicle priming and synaptic efficacy. Ca²⁺ sensor/effector complexes consisting of calmodulin and Munc13s regulate synaptic vesicle priming and synaptic efficacy in response to a residual [Ca²⁺] signal and thus shape short-term plasticity characteristics during periods of sustained synaptic activity."],["dc.identifier.doi","10.1016/j.cell.2004.06.029"],["dc.identifier.gro","3143957"],["dc.identifier.isi","000223353100014"],["dc.identifier.pmid","15294163"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1528"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.title","Calmodulin and Munc13 form a Ca²⁺ sensor/effector complex that controls short-term synaptic plasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Psychiatry"],["dc.contributor.author","Ambrozkiewicz, Mateusz C."],["dc.contributor.author","Borisova, Ekaterina"],["dc.contributor.author","Schwark, Manuela"],["dc.contributor.author","Ripamonti, Silvia"],["dc.contributor.author","Schaub, Theres"],["dc.contributor.author","Smorodchenko, Alina"],["dc.contributor.author","Weber, A. Ioana"],["dc.contributor.author","Rhee, Hong Jun"],["dc.contributor.author","Altas, Bekir"],["dc.contributor.author","Yilmaz, Rüstem"],["dc.contributor.author","Mueller, Susanne"],["dc.contributor.author","Piepkorn, Lars"],["dc.contributor.author","Horan, Stephen T."],["dc.contributor.author","Straussberg, Rachel"],["dc.contributor.author","Zaqout, Sami"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Dere, Ekrem"],["dc.contributor.author","Rosário, Marta"],["dc.contributor.author","Boehm-Sturm, Philipp"],["dc.contributor.author","Borck, Guntram"],["dc.contributor.author","Willig, Katrin I."],["dc.contributor.author","Rhee, JeongSeop"],["dc.contributor.author","Tarabykin, Victor"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.date.accessioned","2020-12-10T18:09:37Z"],["dc.date.available","2020-12-10T18:09:37Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41380-020-0714-8"],["dc.identifier.eissn","1476-5578"],["dc.identifier.issn","1359-4184"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73708"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The murine ortholog of Kaufman oculocerebrofacial syndrome protein Ube3b regulates synapse number by ubiquitinating Ppp3cc"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1005"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","1018"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Lipstein, Noa"],["dc.contributor.author","Verhoeven-Duif, Nanda M."],["dc.contributor.author","Michelassi, Francesco E."],["dc.contributor.author","Calloway, Nathaniel"],["dc.contributor.author","van Hasselt, Peter M."],["dc.contributor.author","Pienkowska, Katarzyna"],["dc.contributor.author","van Haaften, Gijs"],["dc.contributor.author","van Haelst, Mieke M."],["dc.contributor.author","van Empelen, Ron"],["dc.contributor.author","Cuppen, Inge"],["dc.contributor.author","van Teeseling, Heleen C."],["dc.contributor.author","Evelein, Annemieke M.V."],["dc.contributor.author","Vorstman, Jacob A."],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Duran, Karen J."],["dc.contributor.author","Monroe, Glen R."],["dc.contributor.author","Ryan, Timothy A."],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","Dittman, Jeremy S."],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Visser, Gepke"],["dc.contributor.author","Jans, Judith J."],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2020-12-10T18:38:19Z"],["dc.date.available","2020-12-10T18:38:19Z"],["dc.date.issued","2017"],["dc.description.abstract","Munc13 proteins are essential regulators of neurotransmitter release at nerve cell synapses. They mediate the priming step that renders synaptic vesicles fusion-competent, and their genetic elimination causes a complete block of synaptic transmission. Here we have described a patient displaying a disorder characterized by a dyskinetic movement disorder, developmental delay, and autism. Using whole-exome sequencing, we have shown that this condition is associated with a rare, de novo Pro814Leu variant in the major human Munc13 paralog UNC13A (also known as Munc13-1). Electrophysiological studies in murine neuronal cultures and functional analyses in Caenorhabditis elegans revealed that the UNC13A variant causes a distinct dominant gain of function that is characterized by increased fusion propensity of synaptic vesicles, which leads to increased initial synaptic vesicle release probability and abnormal short-term synaptic plasticity. Our study underscores the critical importance of fine-tuned presynaptic control in normal brain function. Further, it adds the neuronal Munc13 proteins and the synaptic vesicle priming process that they control to the known etiological mechanisms of psychiatric and neurological synaptopathies."],["dc.identifier.doi","10.1172/JCI90259"],["dc.identifier.eissn","1558-8238"],["dc.identifier.issn","0021-9738"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77270"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.relation.doi","10.1172/JCI90259"],["dc.relation.eissn","1558-8238"],["dc.relation.issn","0021-9738"],["dc.title","Synaptic UNC13A protein variant causes increased neurotransmission and dyskinetic movement disorder"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Akula, Asha Kiran"],["dc.contributor.author","Zhang, Xin"],["dc.contributor.author","Viotti, Julio S."],["dc.contributor.author","Nestvogel, Dennis"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Ebrecht, Rene"],["dc.contributor.author","Reim, Kerstin"],["dc.contributor.author","Wouters, Fred"],["dc.contributor.author","Liepold, Thomas"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Bogeski, Ivan"],["dc.contributor.author","Dresbach, Thomas"],["dc.date.accessioned","2020-12-10T18:44:35Z"],["dc.date.available","2020-12-10T18:44:35Z"],["dc.date.issued","2019"],["dc.description.abstract","Neurotransmitter release is mediated by an evolutionarily conserved machinery. The synaptic vesicle (SV) associated protein Mover/TPRGL/SVAP30 does not occur in all species and all synapses. Little is known about its molecular properties and how it may interact with the conserved components of the presynaptic machinery. Here, we show by deletion analysis that regions required for homomeric interaction of Mover are distributed across the entire molecule, including N-terminal, central and C-terminal regions. The same regions are also required for the accumulation of Mover in presynaptic terminals of cultured neurons. Mutating two phosphorylation sites in N-terminal regions did not affect these properties. In contrast, a point mutation in the predicted Calmodulin (CaM) binding sequence of Mover abolished both homomeric interaction and presynaptic targeting. We show that this sequence indeed binds Calmodulin, and that recombinant Mover increases Calmodulin signaling upon heterologous expression. Our data suggest that presynaptic accumulation of Mover requires homomeric interaction mediated by regions distributed across large areas of the protein, and corroborate the hypothesis that Mover functionally interacts with Calmodulin signaling."],["dc.identifier.doi","10.3389/fnmol.2019.00249"],["dc.identifier.eissn","1662-5099"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16645"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78512"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1662-5099"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The Calmodulin Binding Region of the Synaptic Vesicle Protein Mover Is Required for Homomeric Interaction and Presynaptic Targeting"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4628"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","4641"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Lipstein, Noa"],["dc.contributor.author","Schaks, Sabine"],["dc.contributor.author","Dimova, Kalina"],["dc.contributor.author","Kalkhof, Stefan"],["dc.contributor.author","Ihling, Christian"],["dc.contributor.author","Kölbel, Knut"],["dc.contributor.author","Ashery, Uri"],["dc.contributor.author","Rhee, JeongSeop"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Sinz, Andrea"],["dc.contributor.author","Jahn, Olaf"],["dc.date.accessioned","2017-09-07T11:48:22Z"],["dc.date.available","2017-09-07T11:48:22Z"],["dc.date.issued","2012"],["dc.description.abstract","Munc13s are presynaptic proteins that mediate synaptic vesicle priming and thereby control the size of the readily releasable pool of vesicles. During high synaptic activity, Munc13-1 and its closely related homolog, ubMunc13-2, bind Ca²⁺/calmodulin, resulting in enhanced priming activity and in changes of short-term synaptic plasticity characteristics. Here, we studied whether bMunc13-2 and Munc13-3, two remote isoforms of Munc13-1 with a neuronal subtype-specific expression pattern, mediate synaptic vesicle priming and regulate short-term synaptic plasticity in a Ca²⁺/calmodulin-dependent manner. We identified a single functional Ca²⁺/calmodulin binding site in these isoforms and provide structural evidence that all Munc13s employ a common mode of interaction with calmodulin despite the lack of sequence homology between their Ca²⁺/calmodulin binding sites. Electrophysiological analysis showed that, during high-frequency activity, Ca²⁺/calmodulin binding positively regulates the priming activity of bMunc13-2 and Munc13-3, resulting in an increase in the size of the readily releasable pool of vesicles and subsequently in strong short-term synaptic enhancement of neurotransmission. We conclude that Ca²⁺/calmodulin-dependent regulation of priming activity is structurally and functionally conserved in all Munc13 proteins, and that the composition of Munc13 isoforms in a neuron differentially controls its short-term synaptic plasticity characteristics."],["dc.identifier.doi","10.1128/MCB.00933-12"],["dc.identifier.gro","3142447"],["dc.identifier.isi","000310536000011"],["dc.identifier.pmid","22966208"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8385"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Minerva Foundation"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0270-7306"],["dc.title","Nonconserved Ca²⁺/Calmodulin Binding Sites in Munc13s Differentially Control Synaptic Short-Term Plasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","647"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","661"],["dc.bibliographiccitation.volume","154"],["dc.contributor.author","Ripamonti, Silvia"],["dc.contributor.author","Shomroni, Orr"],["dc.contributor.author","Rhee, Jeong Seop"],["dc.contributor.author","Chowdhury, Kamal"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Hellmann, Klaus Peter"],["dc.contributor.author","Bonn, Stefan"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Tirard, Marilyn"],["dc.date.accessioned","2021-04-14T08:26:35Z"],["dc.date.available","2021-04-14T08:26:35Z"],["dc.date.issued","2020"],["dc.description.abstract","SUMOylation is a dynamic post-translational protein modification that primarily takes place in cell nuclei, where it plays a key role in multiple DNA-related processes. In neurons, the SUMOylation-dependent control of a subset of neuronal transcription factors is known to regulate various aspects of nerve cell differentiation, development, and function. In an unbiased screen for endogenous SUMOylation targets in the developing mouse brain, based on a His6-HA-SUMO1 knock-in mouse line, we previously identified the transcription factor Zinc finger and BTB domain-containing 20 (Zbtb20) as a new SUMO1-conjugate. We show here that the three key SUMO paralogues SUMO1, SUMO2, and SUMO3 can all be conjugated to Zbtb20 in vitro in HEK293FT cells, and we confirm the SUMOylation of Zbtb20 in vivo in mouse brain. Using primary hippocampal neurons from wild-type and Zbtb20 knock-out (KO) mice as a model system, we then demonstrate that the expression of Zbtb20 is required for proper nerve cell development and neurite growth and branching. Furthermore, we show that the SUMOylation of Zbtb20 is essential for its function in this context, and provide evidence indicating that SUMOylation affects the Zbtb20-dependent transcriptional profile of neurons. Our data highlight the role of SUMOylation in the regulation of neuronal transcription factors that determine nerve cell development, and they demonstrate that key functions of the transcription factor Zbtb20 in neuronal development and neurite growth are under obligatory SUMOylation control."],["dc.identifier.doi","10.1111/jnc.15008"],["dc.identifier.pmid","32233089"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82001"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/73"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A09: SUMOylation und Neddylation in Synapsen"],["dc.relation","SFB 1286 | Z02: Integrative Datenanalyse und -interpretation. Generierung einer synaptisch-integrativen Datenstrategie (SynIDs)"],["dc.relation.eissn","1471-4159"],["dc.relation.issn","0022-3042"],["dc.relation.workinggroup","RG Bonn"],["dc.relation.workinggroup","RG Brose"],["dc.rights","CC BY 4.0"],["dc.title","SUMOylation controls the neurodevelopmental function of the transcription factor Zbtb20"],["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","358"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.lastpage","372"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Kawabe, Hiroshi"],["dc.contributor.author","Neeb, Antje"],["dc.contributor.author","Dimova, Kalina"],["dc.contributor.author","Young, Samuel M., Jr."],["dc.contributor.author","Takeda, Michiko"],["dc.contributor.author","Katsurabayashi, Shutaro"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Malakhova, Oxana A."],["dc.contributor.author","Zhang, Dong-Er"],["dc.contributor.author","Ulmilkawa, Masato"],["dc.contributor.author","Kariya, Ken-ichi"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Rosenmund, Christian"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.contributor.author","Brose, Nils"],["dc.date.accessioned","2017-09-07T11:46:08Z"],["dc.date.available","2017-09-07T11:46:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Nedd4-1 is a \"neuronal precursor cell expressed and developmentally downregulated protein\" and among the most abundant E3 ubiquitin ligases in mammalian neurons. In analyses of conventional and conditional Nedd4-1-deficient mice, we found that Nedd4-1 plays a critical role in dendrite formation. Nedd4-1, the serine/threonine kinase TNIK, and Rap2A form a complex that controls Nedd4-1-mediated ubiquitination of Rap2A. Ubiquitination by Nedd4-1 inhibits Rap2A function, which reduces the activity of Rap2 effector kinases of the TNIK family and promotes dendrite growth. We conclude that a Nedd4-1/Rap2A/TNIK signaling pathway regulates neurite growth and arborization in mammalian neurons."],["dc.identifier.doi","10.1016/j.neuron.2010.01.007"],["dc.identifier.gro","3142966"],["dc.identifier.isi","000275185200009"],["dc.identifier.pmid","20159449"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/428"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0896-6273"],["dc.title","Regulation of Rap2A by the Ubiquitin Ligase Nedd4-1 Controls Neurite Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","620"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Neuron"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Burgalossi, Andrea"],["dc.contributor.author","Jung, Sangyong"],["dc.contributor.author","Meyer, Guido"],["dc.contributor.author","Jockusch, Wolf J."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Taschenberger, Holger"],["dc.contributor.author","O'Connor, Vincent M."],["dc.contributor.author","Nishiki, Tei-ichi"],["dc.contributor.author","Takahashi, Masami"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Rhee, Jeong-Seop"],["dc.date.accessioned","2022-03-01T11:45:20Z"],["dc.date.available","2022-03-01T11:45:20Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1016/j.neuron.2012.01.015"],["dc.identifier.pii","S0896627312000979"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103295"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0896-6273"],["dc.title","SNARE Protein Recycling by αSNAP and βSNAP Supports Synaptic Vesicle Priming"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]