Thoms, Sven

[["dc.bibliographiccitation.firstpage","84"],["dc.bibliographiccitation.lastpage","85"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.editor","Schwab, Manfred"],["dc.date.accessioned","2020-08-10T06:10:25Z"],["dc.date.available","2020-08-10T06:10:25Z"],["dc.date.issued","2001"],["dc.identifier.doi","10.1007/3-540-30683-8_130"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67557"],["dc.language.iso","en"],["dc.relation.isbn","3-540-66527-7"],["dc.title","Autophagy"],["dc.type","encyclopedia_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","European Journal of Pediatrics"],["dc.bibliographiccitation.volume","168"],["dc.contributor.author","Klinge, Lars"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Cierny, Irmgard"],["dc.contributor.author","Straub, Volker"],["dc.contributor.author","Bushby, Kate"],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2018-11-07T08:31:59Z"],["dc.date.available","2018-11-07T08:31:59Z"],["dc.date.issued","2009"],["dc.identifier.isi","000262826600054"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17244"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.title","Defective membrane tubulation in dysferlin-deficient muscular dystrophy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","504"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The FEBS Journal"],["dc.bibliographiccitation.lastpage","514"],["dc.bibliographiccitation.volume","275"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Debelyy, Mykhaylo O."],["dc.contributor.author","Nau, Katja"],["dc.contributor.author","Meyer, Helmut E."],["dc.contributor.author","Erdmann, Ralf"],["dc.date.accessioned","2020-08-10T05:24:04Z"],["dc.date.available","2020-08-10T05:24:04Z"],["dc.date.issued","2008"],["dc.description.abstract","Lpx1p (systematic name: Yor084wp) is a peroxisomal protein from Saccharomyces cerevisiae with a peroxisomal targeting signal type 1 (PTS1) and a lipase motif. Using mass spectrometry, we have identified Lpx1p as present in peroxisomes, and show that Lpx1p import is dependent on the PTS1 receptor Pex5p. We provide evidence that Lpx1p is piggyback-transported into peroxisomes. We have expressed the Lpx1p protein in Escherichia coli, and show that the enzyme exerts acyl hydrolase and phospholipase A activity in vitro. However, the protein is not required for wild-type-like steady-state function of peroxisomes, which might be indicative of a metabolic rather than a biogenetic role. Interestingly, peroxisomes in deletion mutants of LPX1 have an aberrant morphology characterized by intraperoxisomal vesicles or invaginations."],["dc.identifier.doi","10.1111/j.1742-4658.2007.06217.x"],["dc.identifier.pmid","18199283"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67542"],["dc.language.iso","en"],["dc.relation.issn","1742-464X"],["dc.title","Lpx1p is a peroxisomal lipase required for normal peroxisome morphology"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e202000987"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Life Science Alliance"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Sargsyan, Yelena"],["dc.contributor.author","Bickmeyer, Uta"],["dc.contributor.author","Gibhardt, Christine S"],["dc.contributor.author","Streckfuss-Bömeke, Katrin"],["dc.contributor.author","Bogeski, Ivan"],["dc.contributor.author","Thoms, Sven"],["dc.date.accessioned","2021-08-12T07:45:41Z"],["dc.date.available","2021-08-12T07:45:41Z"],["dc.date.issued","2021"],["dc.description.abstract","Peroxisomes communicate with other cellular compartments by transfer of various metabolites. However, whether peroxisomes are sites for calcium handling and exchange has remained contentious. Here we generated sensors for assessment of peroxisomal calcium and applied them for single cell-based calcium imaging in HeLa cells and cardiomyocytes. We found that peroxisomes in HeLa cells take up calcium upon depletion of intracellular calcium stores and upon calcium influx across the plasma membrane. Furthermore, we show that peroxisomes of neonatal rat cardiomyocytes and human induced pluripotent stem cell–derived cardiomyocytes can take up calcium. Our results indicate that peroxisomal and cytosolic calcium signals are tightly interconnected both in HeLa cells and in cardiomyocytes. Cardiac peroxisomes take up calcium on beat-to-beat basis. Hence, peroxisomes may play an important role in shaping cellular calcium dynamics of cardiomyocytes."],["dc.description.abstract","Peroxisomes communicate with other cellular compartments by transfer of various metabolites. However, whether peroxisomes are sites for calcium handling and exchange has remained contentious. Here we generated sensors for assessment of peroxisomal calcium and applied them for single cell-based calcium imaging in HeLa cells and cardiomyocytes. We found that peroxisomes in HeLa cells take up calcium upon depletion of intracellular calcium stores and upon calcium influx across the plasma membrane. Furthermore, we show that peroxisomes of neonatal rat cardiomyocytes and human induced pluripotent stem cell–derived cardiomyocytes can take up calcium. Our results indicate that peroxisomal and cytosolic calcium signals are tightly interconnected both in HeLa cells and in cardiomyocytes. Cardiac peroxisomes take up calcium on beat-to-beat basis. Hence, peroxisomes may play an important role in shaping cellular calcium dynamics of cardiomyocytes."],["dc.identifier.doi","10.26508/lsa.202000987"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/88529"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-448"],["dc.relation.eissn","2575-1077"],["dc.title","Peroxisomes contribute to intracellular calcium dynamics in cardiomyocytes and non-excitable cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Neuropediatrics"],["dc.contributor.author","Nava, Esmeralda"],["dc.contributor.author","Hartmann, Britta"],["dc.contributor.author","Boxheimer, Larissa"],["dc.contributor.author","Capone Mori, Andrea"],["dc.contributor.author","Nuoffer, Jean-Marc"],["dc.contributor.author","Sargsyan, Yelena"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Rosewich, Hendrik"],["dc.contributor.author","Boltshauser, Eugen"],["dc.date.accessioned","2022-04-01T10:00:41Z"],["dc.date.available","2022-04-01T10:00:41Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract A 4-year-old boy presented with subacute onset of cerebellar ataxia. Neuroimaging revealed cerebellar atrophy. Metabolic screening tests aiming to detect potentially treatable ataxias showed an increased value (fourfold upper limit of normal) for phytanic acid and elevated very-long-chain fatty acid (VLCFA) ratios (C24:0/C22:0 and C26:0/C22:0), while absolute concentrations of VLCFA were normal. Genetic analysis identified biallelic variants in PEX10. Immunohistochemistry confirmed pathogenicity in the patients' cultured fibroblasts demonstrating peroxisomal mosaicism with a general catalase import deficiency as well as conspicuous peroxisome morphology as an expression of impaired peroxisomal function. We describe for the first time an elongated peroxisome morphology in a patient with PEX10-related cerebellar ataxia. A literature search yielded 14 similar patients from nine families with PEX10-related cerebellar ataxia, most of them presenting their first symptoms between 3 and 8 years of age. In 11/14 patients, the first and main symptom was cerebellar ataxia; in three patients, it was sensorineural hearing impairment. Finally, all 14 patients developed ataxia. Polyneuropathy (9/14) and cognitive impairment (9/14) were common associated findings. In 12/13 patients brain MRI showed cerebellar atrophy. Phytanic acid was elevated in 8/12 patients, while absolute concentrations of VLCFA levels were in normal limits in several patients. VLCFA ratios (C24:0/C22:0 and/or C26:0/C22:0), though, were elevated in 11/11 cases. We suggest including measurement of phytanic acid and VLCFA ratios in metabolic screening tests in unexplained autosomal recessive ataxias with cerebellar atrophy, especially when there is an early onset and symptoms are mild."],["dc.identifier.doi","10.1055/s-0041-1741383"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/105487"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1439-1899"],["dc.relation.issn","0174-304X"],["dc.title","How to Detect Isolated PEX10-Related Cerebellar Ataxia?"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","362"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Structural Biology"],["dc.bibliographiccitation.lastpage","371"],["dc.bibliographiccitation.volume","175"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Thoeing, Christian"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Niemann, Hartmut H."],["dc.date.accessioned","2017-09-07T11:43:25Z"],["dc.date.available","2017-09-07T11:43:25Z"],["dc.date.issued","2011"],["dc.description.abstract","The yeast peroxisomal hydrolase Lpx1 belongs to the alpha/beta-hydrolase superfamily. In the absence of Lpx1, yeast peroxisomes show an aberrant vacuolated morphology similar to what is found in peroxisomal disorder patients. Here, we present the crystal structure of Lpx1 determined at a resolution of 1.9 angstrom. The structure reveals the complete catalytic triad with an unusual location of the acid residue after strand beta 6 of the canonical alpha/beta-hydrolase fold. A four-helix cap domain covers the active site. The interface between the alpha/beta-hydrolase core and the cap domain forms the potential substrate binding site, which may also comprise the tunnel that leads into the protein interior and widens into a cavity. Two further tunnels connect the active site to the protein surface, potentially facilitating substrate access. Lpx1 is a homodimer. The alpha/beta-hydrolase core folds of the two protomers form the dimer contact site. Further dimerization contacts arise from the mutual embracement of the cap domain of one protomer by the non-canonical C-terminal helix of the other, resulting in a total buried surface area of some 6000 angstrom(2). The unusual C-terminal helix sticks out from the core fold to which it is connected by an extended flexible loop. We analyzed whether this helix is required for dimerization and for import of the dimer into peroxisomes using biochemical assays in vitro and a microscopy-based interaction assay in mammalian cells. Surprisingly, the C-terminal helix is dispensable for dimerization and dimer import. The unusually robust self-interaction suggests that Lpx1 is imported into peroxisomes as dimer. (C) 2011 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.jsb.2011.06.008"],["dc.identifier.gro","3142679"],["dc.identifier.isi","000293807000012"],["dc.identifier.pmid","21741480"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/109"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1047-8477"],["dc.title","The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]

[["dc.bibliographiccitation.firstpage","541"],["dc.bibliographiccitation.lastpage","572"],["dc.contributor.author","Platta, Harald W."],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Kunau, Wolf‐H."],["dc.contributor.author","Erdmann, Ralf"],["dc.contributor.editor","Dalbey, Ross E."],["dc.contributor.editor","Koehler, Carla M."],["dc.contributor.editor","Tamanoi, Fuyuhiko"],["dc.date.accessioned","2020-08-10T06:04:52Z"],["dc.date.available","2020-08-10T06:04:52Z"],["dc.date.issued","2007"],["dc.description.abstract","This chapter discusses the enzymatically catalyzed mechanisms underlying the transport of matrix proteins across the peroxisomal membrane into the lumen of the organelle, a process that involves most of the known peroxins. The chapter focuses on the basic experimental evidence concerning the functional roles of Pex4p and AAA peroxins in Pex5p recycling and matrix protein import to combine and discuss them in a unified model. Ubiquitin-conjugating enzymes play a central role in the process of ubiquitination and function to bridge the first, nonspecific step of ubiquitin activation by E1 with the transfer of activated ubiquitin to target-proteins by substrate-specific E3 enzymes. Pex4p/Ubc10p is a ubiquitin-conjugating enzyme essential for peroxisomal biogenesis. Pex4p contains the catalytically relevant active site Cys residue of ubiquitin-conjugating enzymes within the core Ubc fold, while AAAs are mechanoenzymes that manipulate the structure of substrate proteins, and thereby unfold them or disassemble protein complexes. The energy dependence of peroxisomal protein import is caused by the cycle of the peroxisomal targeting signal (PTS) receptors. A model is emerging in which the previously disparate roles of Pex4p and the AAA peroxins are combined in a concerted reaction sequence. However, it will be a challenge to elucidate the way ATP-dependent receptor dislocation is mechanistically linked to the import of folded proteins."],["dc.identifier.doi","10.1016/S1874-6047(07)25021-8"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67555"],["dc.language.iso","en"],["dc.publisher","Elsevier"],["dc.relation.isbn","9780123739162"],["dc.relation.ispartof","Molecular Machines Involved in Protein Transport across Cellular Membranes"],["dc.title","Function of the Ubiquitin‐Conjugating Enzyme Pex4p and the AAA Peroxin Complex Pex1p/Pex6p in Peroxisomal Matrix Protein Transport"],["dc.type","book_chapter"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","599"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","609"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Harms, Imke"],["dc.contributor.author","Kalies, Kai-Uwe"],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2017-09-07T11:48:55Z"],["dc.date.available","2017-09-07T11:48:55Z"],["dc.date.issued","2011"],["dc.description.abstract","In peroxisome formation, models of near-autonomous peroxisome biogenesis with membrane protein integration directly from the cytosol into the peroxisomal membrane are in direct conflict with models whereby peroxisomes bud from the endoplasmic reticulum and receive their membrane proteins through a branch of the secretory pathway. We therefore reinvestigated the role of the Sec61 complex, the protein-conducting channel of the endoplasmic reticulum (ER) in peroxisome formation. We found that depletion or partial inactivation of Sec61 in yeast disables peroxisome formation. The ER entry of the early peroxisomal membrane protein Pex3 engineered with a glycosylation tag is reduced in sec61 mutant cells. Moreover, we were able to reconstitute Pex3 import into ER membranes in vitro, and we identified a variant of a signal anchor sequence for ER translocation at the Pex3 N-terminus. Our findings are consistent with a Sec61 requirement for peroxisome formation and a fundamental role of the ER in peroxisome biogenesis."],["dc.identifier.doi","10.1111/j.1600-0854.2011.01324.x"],["dc.identifier.gro","3142559"],["dc.identifier.isi","000301347800010"],["dc.identifier.pmid","22212716"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8923"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [Ga354/5-2, Ga354/7-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1398-9219"],["dc.title","Peroxisome Formation Requires the Endoplasmic Reticulum Channel Protein Sec61"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]

[["dc.bibliographiccitation.firstpage","1119"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Europace"],["dc.bibliographiccitation.lastpage","1131"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Bersch, Kristina"],["dc.contributor.author","Wagner, Stefan"],["dc.contributor.author","Molina, Cristina Espinosa"],["dc.contributor.author","Fakuade, Funsho E."],["dc.contributor.author","Iyer, Lavanya M."],["dc.contributor.author","Streckfuß-Bömeke, Katrin"],["dc.contributor.author","Toischer, Karl"],["dc.contributor.author","Zelarayan, Laura Cecilia"],["dc.contributor.author","Voigt, Niels"],["dc.contributor.author","Nikolaev, Viacheslav O."],["dc.contributor.author","Maier, Lars Siegfried"],["dc.contributor.author","Klinge, Lars"],["dc.contributor.author","Thoms, Sven"],["dc.date.accessioned","2020-08-10T05:34:04Z"],["dc.date.available","2020-08-10T05:34:04Z"],["dc.date.issued","2020"],["dc.description.abstract","The multi-C2 domain protein dysferlin localizes to the T-Tubule system of skeletal and heart muscles. In skeletal muscle, dysferlin is known to play a role in membrane repair and in T-tubule biogenesis and maintenance. Dysferlin deficiency manifests as muscular dystrophy of proximal and distal muscles. Cardiomyopathies have been also reported, and some dysferlinopathy mouse models develop cardiac dysfunction under stress. Generally, the role and functional relevance of dysferlin in the heart is not clear. The aim of this study was to analyse the effect of dysferlin deficiency on the transverse-axial tubule system (TATS) structure and on Ca2+ homeostasis in the heart."],["dc.identifier.doi","10.1093/europace/euaa093"],["dc.identifier.pmid","32572487"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67547"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/360"],["dc.language.iso","en"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A10: Peroxisomen als modulatorische Einheiten im Herzstoffwechsel und bei Herzinsuffizienz"],["dc.relation","SFB 1002 | C07: Kardiomyozyten Wnt/β-catenin Komplex Aktivität im pathologischen Herz-Remodeling - als gewebespezifischer therapeutischer Ansatz"],["dc.relation","SFB 1002 | D04: Bedeutung der Methylierung von RNA (m6A) und des Histons H3 (H3K4) in der Herzinsuffizienz"],["dc.relation","SFB 1002 | S01: In vivo und in vitro Krankheitsmodelle"],["dc.relation","SFB 1002 | A13: Bedeutung einer gestörten zytosolischen Calciumpufferung bei der atrialen Arrhythmogenese bei Patienten mit Herzinsuffizienz (HF)"],["dc.relation.eissn","1532-2092"],["dc.relation.issn","1099-5129"],["dc.relation.workinggroup","RG L. Maier (Experimentelle Kardiologie)"],["dc.relation.workinggroup","RG Nikolaev (Cardiovascular Research Center)"],["dc.relation.workinggroup","RG Thoms (Biochemistry and Molecular Medicine)"],["dc.relation.workinggroup","RG Toischer (Kardiales Remodeling)"],["dc.relation.workinggroup","RG Voigt (Molecular Pharmacology)"],["dc.relation.workinggroup","RG Zelarayán-Behrend (Developmental Pharmacology)"],["dc.title","Dysferlin links excitation-contraction coupling to structure and maintenance of the cardiac transverse-axial tubule system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["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"]]