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","1766"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","1779"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Kaczmarek, Karina"],["dc.contributor.author","Studencka, Maja"],["dc.contributor.author","Meinhardt, Andreas"],["dc.contributor.author","Wieczerzak, Krzysztof"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Engel, Wolfgang"],["dc.contributor.author","Grzmil, Pawel"],["dc.date.accessioned","2018-11-07T08:56:09Z"],["dc.date.available","2018-11-07T08:56:09Z"],["dc.date.issued","2011"],["dc.description.abstract","Peroxisomal testis-specific 1 gene (Pxt1) is the only male germ cell-specific gene that encodes a peroxisomal protein known to date. To elucidate the role of Pxt1 in spermatogenesis, we generated transgenic mice expressing a c-MYC-PXT1 fusion protein under the control of the PGK2 promoter. Overexpression of Pxt1 resulted in induction of male germ cells' apoptosis mainly in primary spermatocytes, finally leading to male infertility. This prompted us to analyze the proapoptotic character of mouse PXT1, which harbors a BH3-like domain in the N-terminal part. In different cell lines, the overexpression of PXT1 also resulted in a dramatic increase of apoptosis, whereas the deletion of the BH3-like domain significantly reduced cell death events, thereby confirming that the domain is functional and essential for the proapoptotic activity of PXT1. Moreover, we demonstrated that PXT1 interacts with apoptosis regulator BAT3, which, if overexpressed, can protect cells from the PXT1-induced apoptosis. The PXT1-BAT3 association leads to PXT1 relocation from the cytoplasm to the nucleus. In summary, we demonstrated that PXT1 induces apoptosis via the BH3-like domain and that this process is inhibited by BAT3."],["dc.identifier.doi","10.1091/mbc.E09-12-0993"],["dc.identifier.isi","000290515600012"],["dc.identifier.pmid","21460186"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8147"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23074"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Overexpression of peroxisomal testis-specific 1 protein induces germ cell apoptosis and leads to infertility in male mice"],["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","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","38"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Communications Biology"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Oleksiievets, Nazar"],["dc.contributor.author","Sargsyan, Yelena"],["dc.contributor.author","Thiele, Jan Christoph"],["dc.contributor.author","Mougios, Nikolaos"],["dc.contributor.author","Sograte-Idrissi, Shama"],["dc.contributor.author","Nevskyi, Oleksii"],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Tsukanov, Roman"],["dc.date.accessioned","2022-01-13T06:27:32Z"],["dc.date.available","2022-01-13T06:27:32Z"],["dc.date.issued","2022-01-11"],["dc.description.abstract","DNA point accumulation for imaging in nanoscale topography (DNA-PAINT) is a powerful super-resolution technique highly suitable for multi-target (multiplexing) bio-imaging. However, multiplexed imaging of cells is still challenging due to the dense and sticky environment inside a cell. Here, we combine fluorescence lifetime imaging microscopy (FLIM) with DNA-PAINT and use the lifetime information as a multiplexing parameter for targets identification. In contrast to Exchange-PAINT, fluorescence lifetime PAINT (FL-PAINT) can image multiple targets simultaneously and does not require any fluid exchange, thus leaving the sample undisturbed and making the use of flow chambers/microfluidic systems unnecessary. We demonstrate the potential of FL-PAINT by simultaneous imaging of up to three targets in a cell using both wide-field FLIM and 3D time-resolved confocal laser scanning microscopy (CLSM). FL-PAINT can be readily combined with other existing techniques of multiplexed imaging and is therefore a perfect candidate for high-throughput multi-target bio-imaging."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s42003-021-02976-4"],["dc.identifier.pmid","35017652"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98096"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/392"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/415"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A10: Peroxisomen als modulatorische Einheiten im Herzstoffwechsel und bei Herzinsuffizienz"],["dc.relation.issn","2399-3642"],["dc.relation.orgunit","III. Physikalisches Institut - Biophysik"],["dc.relation.workinggroup","RG Enderlein"],["dc.relation.workinggroup","RG Thoms (Biochemistry and Molecular Medicine)"],["dc.rights","CC BY 4.0"],["dc.title","Fluorescence lifetime DNA-PAINT for multiplexed super-resolution imaging of cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["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.artnumber","7809"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.lastpage","13"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Soliman, Kareem"],["dc.contributor.author","Göttfert, Fabian"],["dc.contributor.author","Rosewich, Hendrik"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Gärtner, Jutta"],["dc.date.accessioned","2019-02-27T10:14:35Z"],["dc.date.available","2019-02-27T10:14:35Z"],["dc.date.issued","2018"],["dc.description.abstract","Peroxisomes are ubiquitous cell organelles involved in many metabolic and signaling functions. Their assembly requires peroxins, encoded by PEX genes. Mutations in PEX genes are the cause of Zellweger Syndrome spectrum (ZSS), a heterogeneous group of peroxisomal biogenesis disorders (PBD). The size and morphological features of peroxisomes are below the diffraction limit of light, which makes them attractive for super-resolution imaging. We applied Stimulated Emission Depletion (STED) microscopy to study the morphology of human peroxisomes and peroxisomal protein localization in human controls and ZSS patients. We defined the peroxisome morphology in healthy skin fibroblasts and the sub-diffraction phenotype of residual peroxisomal structures (‘ghosts’) in ZSS patients that revealed a relation between mutation severity and clinical phenotype. Further, we investigated the 70 kDa peroxisomal membrane protein (PMP70) abundance in relationship to the ZSS sub-diffraction phenotype. This work improves the morphological definition of peroxisomes. It expands current knowledge about peroxisome biogenesis and ZSS pathoethiology to the sub-diffraction phenotype including key peroxins and the characteristics of ghost peroxisomes."],["dc.identifier.doi","10.1038/s41598-018-24119-2"],["dc.identifier.pmid","29773809"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15261"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/57637"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/210"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A10: Peroxisomen als modulatorische Einheiten im Herzstoffwechsel und bei Herzinsuffizienz"],["dc.relation.issn","2045-2322"],["dc.relation.workinggroup","RG Thoms (Biochemistry and Molecular Medicine)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Super-resolution imaging reveals the sub-diffraction phenotype of Zellweger Syndrome ghosts and wild-type peroxisomes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]