Neumann, Piotr D.

[["dc.bibliographiccitation.artnumber","5715"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Dybkov, Olexandr"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Cruz-Zaragoza, Luis Daniel"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2021-10-01T09:57:33Z"],["dc.date.available","2021-10-01T09:57:33Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Nuclear-encoded mitochondrial proteins destined for the matrix have to be transported across two membranes. The TOM and TIM23 complexes facilitate the transport of precursor proteins with N-terminal targeting signals into the matrix. During transport, precursors are recognized by the TIM23 complex in the inner membrane for handover from the TOM complex. However, we have little knowledge on the organization of the TOM-TIM23 transition zone and on how precursor transfer between the translocases occurs. Here, we have designed a precursor protein that is stalled during matrix transport in a TOM-TIM23-spanning manner and enables purification of the translocation intermediate. Combining chemical cross-linking with mass spectrometric analyses and structural modeling allows us to map the molecular environment of the intermembrane space interface of TOM and TIM23 as well as the import motor interactions with amino acid resolution. Our analyses provide a framework for understanding presequence handover and translocation during matrix protein transport."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1038/s41467-021-26016-1"],["dc.identifier.pii","26016"],["dc.identifier.pmid","34588454"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89863"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/348"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/157"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG Ficner (Molecular Structural Biology)"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.title","Mapping protein interactions in the active TOM-TIM23 supercomplex"],["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","960"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","965"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Haselbach, David"],["dc.contributor.author","Voss, Bela"],["dc.contributor.author","Russek, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Thomson, Emma"],["dc.contributor.author","Hurt, Ed"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-beta superfamily termed importins and exportins. The highly versatile exportin chromosome region maintenance 1 (CRM1) is essential for nuclear depletion of numerous structurally and functionally unrelated protein and ribonucleoprotein cargoes. CRM1 has been shown to adopt a toroidal structure in several functional transport complexes and was thought to maintain this conformation throughout the entire nucleocytoplasmic transport cycle. We solved crystal structures of free CRM1 from the thermophilic eukaryote Chaetomium thermophilum. Surprisingly, unbound CRM1 exhibits an overall extended and pitched superhelical conformation. The two regulatory regions, namely the acidic loop and the C-terminal a-helix, are dramatically repositioned in free CRM1 in comparison with the ternary CRM1-Ran-Snurportin1 export complex. Single-particle EM analysis demonstrates that, in a noncrystalline environment, free CRM1 exists in equilibrium between extended, superhelical and compact, ring-like conformations. Molecular dynamics simulations show that the C-terminal helix plays an important role in regulating the transition from an extended to a compact conformation and reveal how the binding site for nuclear export signals of cargoes is modulated by different CRM1 conformations. Combining these results, we propose a model for the cooperativity of CRM1 export complex assembly involving the long-range allosteric communication between the distant binding sites of GTP-bound Ran and cargo."],["dc.identifier.doi","10.1073/pnas.1215214110"],["dc.identifier.gro","3142406"],["dc.identifier.isi","000313909100042"],["dc.identifier.pmid","23277578"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7930"],["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","0027-8424"],["dc.title","Structural basis for cooperativity of CRM1 export complex formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Metje-Sprink, Janina"],["dc.contributor.author","Groffmann, Johannes"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Barg-Kues, Brigitte"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Kühnel, Karin"],["dc.contributor.author","Schalk, Amanda M."],["dc.contributor.author","Binotti, Beyenech"],["dc.date.accessioned","2021-04-14T08:24:26Z"],["dc.date.available","2021-04-14T08:24:26Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41598-020-69637-0"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81283"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2045-2322"],["dc.title","Crystal structure of the Rab33B/Atg16L1 effector complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1502"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Montino, Alice"],["dc.contributor.author","Balakrishnan, Karthi"],["dc.contributor.author","Dippel, Stefan"],["dc.contributor.author","Trebels, Björn"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Wimmer, Ernst A."],["dc.date.accessioned","2021-12-01T09:22:46Z"],["dc.date.available","2021-12-01T09:22:46Z"],["dc.date.issued","2021"],["dc.description.abstract","Olfaction is crucial for insects to find food sources, mates, and oviposition sites. One of the initial steps in olfaction is facilitated by odorant-binding proteins (OBPs) that translocate hydrophobic odorants through the aqueous olfactory sensilla lymph to the odorant receptor complexes embedded in the dendritic membrane of olfactory sensory neurons. The Tribolium castaneum (Coleoptera, Tenebrionidae) OBPs encoded by the gene pair TcasOBP9A and TcasOBP9B represent the closest homologs to the well-studied Drosophila melanogaster OBP Lush (DmelOBP76a), which mediates pheromone reception. By an electroantennographic analysis, we can show that these two OBPs are not pheromone-specific but rather enhance the detection of a broad spectrum of organic volatiles. Both OBPs are expressed in the antenna but in a mutually exclusive pattern, despite their homology and gene pair character by chromosomal location. A phylogenetic analysis indicates that this gene pair arose at the base of the Cucujiformia, which dates the gene duplication event to about 200 Mio years ago. Therefore, this gene pair is not the result of a recent gene duplication event and the high sequence conservation in spite of their expression in different sensilla is potentially the result of a common function as co-OBPs."],["dc.description.abstract","Olfaction is crucial for insects to find food sources, mates, and oviposition sites. One of the initial steps in olfaction is facilitated by odorant-binding proteins (OBPs) that translocate hydrophobic odorants through the aqueous olfactory sensilla lymph to the odorant receptor complexes embedded in the dendritic membrane of olfactory sensory neurons. The Tribolium castaneum (Coleoptera, Tenebrionidae) OBPs encoded by the gene pair TcasOBP9A and TcasOBP9B represent the closest homologs to the well-studied Drosophila melanogaster OBP Lush (DmelOBP76a), which mediates pheromone reception. By an electroantennographic analysis, we can show that these two OBPs are not pheromone-specific but rather enhance the detection of a broad spectrum of organic volatiles. Both OBPs are expressed in the antenna but in a mutually exclusive pattern, despite their homology and gene pair character by chromosomal location. A phylogenetic analysis indicates that this gene pair arose at the base of the Cucujiformia, which dates the gene duplication event to about 200 Mio years ago. Therefore, this gene pair is not the result of a recent gene duplication event and the high sequence conservation in spite of their expression in different sensilla is potentially the result of a common function as co-OBPs."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/biom11101502"],["dc.identifier.pii","biom11101502"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94479"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2218-273X"],["dc.relation.orgunit","Johann-Friedrich-Blumenbach-Institut für Zoologie und Anthropologie"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Mutually Exclusive Expression of Closely Related Odorant-Binding Proteins 9A and 9B in the Antenna of the Red Flour Beetle Tribolium castaneum"],["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","102144"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.contributor.author","Heidemann, Jana L."],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Krüger, Larissa"],["dc.contributor.author","Wicke, Dennis"],["dc.contributor.author","Vinhoven, Liza"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-07-01T07:35:47Z"],["dc.date.available","2022-07-01T07:35:47Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.jbc.2022.102144"],["dc.identifier.pii","S0021925822005865"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112267"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.issn","0021-9258"],["dc.title","Structural basis for c-di-AMP-dependent regulation of the bacterial stringent response by receptor protein DarB"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","R780"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","CRITICAL CARE"],["dc.bibliographiccitation.lastpage","R789"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Wrigge, Hermann"],["dc.contributor.author","Zinserling, Jörg"],["dc.contributor.author","Neumann, P."],["dc.contributor.author","Muders, T."],["dc.contributor.author","Magnusson, A."],["dc.contributor.author","Putensen, Christian"],["dc.contributor.author","Hedenstierna, G."],["dc.date.accessioned","2018-11-07T10:53:47Z"],["dc.date.available","2018-11-07T10:53:47Z"],["dc.date.issued","2005"],["dc.description.abstract","Introduction Experimental and clinical studies have shown a reduction in intrapulmonary shunt with spontaneous breathing during airway pressure release ventilation (APRV) in acute lung injury. This reduction was related to reduced atelectasis and increased aeration. We hypothesized that spontaneous breathing will result in better ventilation and aeration of dependent lung areas and in less cyclic collapse during the tidal breath. Methods In this randomized controlled experimental trial, 22 pigs with oleic-acid-induced lung injury were randomly assigned to receive APRV with or without spontaneous breathing at comparable airway pressures. Four hours after randomization, dynamic computed tomography scans of the lung were obtained in an apical slice and in a juxtadiaphragmatic transverse slice. Analyses of regional attenuation were performed separately in nondependent and dependent halves of the lungs on end-expiratory scans and end-inspiratory scans. Tidal changes were assessed as differences between inspiration and expiration of the mechanical breaths. Results Whereas no differences were observed in the apical slices, spontaneous breathing resulted in improved tidal ventilation of dependent lung regions ( P < 0.05) and less cyclic collapse ( P < 0.05) in the juxtadiaphragmatic slices. In addition, with spontaneous breathing, the end-expiratory aeration increased and nonaerated tissue decreased in dependent lung regions close to the diaphragm ( P < 0.05 for the interaction ventilator mode and lung region). Conclusion Spontaneous breathing during APRV redistributes ventilation and aeration to dependent, usually well-perfused, lung regions close to the diaphragm, and may thereby contribute to improved arterial oxygenation. Spontaneous breathing also counters cyclic collapse, which is a risk factor for ventilation-associated lung injury."],["dc.identifier.doi","10.1186/cc3908"],["dc.identifier.isi","000235514400028"],["dc.identifier.pmid","16356227"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/1260"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49419"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1466-609X"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Spontaneous breathing with airway pressure release ventilation favors ventilation in dependent lung regions and counters cyclic alveolar collapse in oleic-acid-induced lung injury: a randomized controlled computed tomography trial"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","785"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","795.e4"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2020-12-10T15:21:31Z"],["dc.date.available","2020-12-10T15:21:31Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.str.2018.03.004"],["dc.identifier.issn","0969-2126"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73053"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Validating Resolution Revolution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","643"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","656"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Melin, Jonathan"],["dc.contributor.author","Chacinska, Agnieszka"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:43:19Z"],["dc.date.available","2017-09-07T11:43:19Z"],["dc.date.issued","2011"],["dc.description.abstract","N-terminal targeting signals (presequences) direct proteins across the TOM complex in the outer mitochondrial membrane and the TIM23 complex in the inner mitochondrial membrane. Presequences provide directionality to the transport process and regulate the transport machineries during translocation. However, surprisingly little is known about how presequence receptors interact with the signals and what role these interactions play during preprotein transport. Here, we identify signal-binding sites of presequence receptors through photo-affinity labeling. Using engineered presequence probes, photo cross-linking sites on mitochondrial proteins were mapped mass spectrometrically, thereby defining a presequence-binding domain of Tim50, a core subunit of the TIM23 complex that is essential for mitochondrial protein import. Our results establish Tim50 as the primary presequence receptor at the inner membrane and show that targeting signals and Tim50 regulate the Tim23 channel in an antagonistic manner."],["dc.identifier.doi","10.1083/jcb.201105098"],["dc.identifier.gro","3142630"],["dc.identifier.isi","000297206400012"],["dc.identifier.pmid","22065641"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8033"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55"],["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.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex"],["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.firstpage","s45"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations and Advances"],["dc.bibliographiccitation.lastpage","s45"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2018-05-30T11:09:47Z"],["dc.date.available","2018-05-30T11:09:47Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1107/S2053273316099307"],["dc.identifier.issn","2053-2733"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/14805"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","fcwi"],["dc.relation.eventend","2016-09-01"],["dc.relation.eventlocation","Basel, Switzerland"],["dc.relation.eventstart","2016-08-28"],["dc.relation.ispartof","Acta Crystallographica Section A, 72(Part a1)"],["dc.title","How reliable are atomic models based on cryo-EM reconstructions? Improvements in model fitting and validation"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1007141"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Heinrich, Gabriele"],["dc.contributor.author","Gross, Carina"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Braus, Gerhard H."],["dc.creator.editor","Brakhage, Axel A."],["dc.date.accessioned","2018-04-23T11:47:09Z"],["dc.date.available","2018-04-23T11:47:09Z"],["dc.date.issued","2018"],["dc.description.abstract","The transition from vegetative growth to multicellular development represents an evolutionary hallmark linked to an oxidative stress signal and controlled protein degradation. We identified the Sem1 proteasome subunit, which connects stress response and cellular differentiation. The sem1 gene encodes the fungal counterpart of the human Sem1 proteasome lid subunit and is essential for fungal cell differentiation and development. A sem1 deletion strain of the filamentous fungus Aspergillus nidulans is able to grow vegetatively and expresses an elevated degree of 20S proteasomes with multiplied ATP-independent catalytic activity compared to wildtype. Oxidative stress induces increased transcription of the genes sem1 and rpn11 for the proteasomal deubiquitinating enzyme. Sem1 is required for stabilization of the Rpn11 deubiquitinating enzyme, incorporation of the ubiquitin receptor Rpn10 into the 19S regulatory particle and efficient 26S proteasome assembly. Sem1 maintains high cellular NADH levels, controls mitochondria integrity during stress and developmental transition."],["dc.identifier.doi","10.1371/journal.pgen.1007141"],["dc.identifier.gro","3142187"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15668"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13306"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Sem1 links proteasome stability and specificity to multicellular development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]