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  1. Article ; Online: Live-Cell Imaging of Peroxisomal Calcium Levels and Dynamics.

    Sargsyan, Yelena / Thoms, Sven

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2643, Page(s) 199–206

    Abstract: ... Calcium ( ... ...

    Abstract Calcium (Ca
    MeSH term(s) Calcium/metabolism ; Endoplasmic Reticulum/metabolism ; Calcium Channels/metabolism ; Calcium Signaling/physiology ; Cytosol/metabolism
    Chemical Substances Calcium (SY7Q814VUP) ; Calcium Channels
    Language English
    Publishing date 2023-03-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3048-8_14
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  2. Article ; Online: Tissue-specific roles of peroxisomes revealed by expression meta-analysis.

    Plessner, Matthias / Thiele, Leonie / Hofhuis, Julia / Thoms, Sven

    Biology direct

    2024  Volume 19, Issue 1, Page(s) 14

    Abstract: Peroxisomes are primarily studied in the brain, kidney, and liver due to the conspicuous tissue-specific pathology of peroxisomal biogenesis disorders. In contrast, little is known about the role of peroxisomes in other tissues such as the heart. In this ...

    Abstract Peroxisomes are primarily studied in the brain, kidney, and liver due to the conspicuous tissue-specific pathology of peroxisomal biogenesis disorders. In contrast, little is known about the role of peroxisomes in other tissues such as the heart. In this meta-analysis, we explore mitochondrial and peroxisomal gene expression on RNA and protein levels in the brain, heart, kidney, and liver, focusing on lipid metabolism. Further, we evaluate a potential developmental and heart region-dependent specificity of our gene set. We find marginal expression of the enzymes for peroxisomal fatty acid oxidation in cardiac tissue in comparison to the liver or cardiac mitochondrial β-oxidation. However, the expression of peroxisome biogenesis proteins in the heart is similar to other tissues despite low levels of peroxisomal fatty acid oxidation. Strikingly, peroxisomal targeting signal type 2-containing factors and plasmalogen biosynthesis appear to play a fundamental role in explaining the essential protective and supporting functions of cardiac peroxisomes.
    MeSH term(s) Humans ; Peroxisomes/genetics ; Peroxisomes/metabolism ; Fatty Acids/metabolism ; Peroxisomal Disorders/genetics ; Peroxisomal Disorders/metabolism ; Mitochondria/metabolism ; Oxidation-Reduction
    Chemical Substances Fatty Acids
    Language English
    Publishing date 2024-02-16
    Publishing country England
    Document type Meta-Analysis ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2221028-3
    ISSN 1745-6150 ; 1745-6150
    ISSN (online) 1745-6150
    ISSN 1745-6150
    DOI 10.1186/s13062-024-00458-1
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  3. Article ; Online: Systematic and quantitative analysis of stop codon readthrough in Rett syndrome nonsense mutations.

    Lebeda, Dennis / Fierenz, Adrian / Werfel, Lina / Rosin-Arbesfeld, Rina / Hofhuis, Julia / Thoms, Sven

    Journal of molecular medicine (Berlin, Germany)

    2024  Volume 102, Issue 5, Page(s) 641–653

    Abstract: Rett syndrome (RTT) is a neurodevelopmental disorder resulting from genetic mutations in the methyl CpG binding protein 2 (MeCP2) gene. Specifically, around 35% of RTT patients harbor premature termination codons (PTCs) within the MeCP2 gene due to ... ...

    Abstract Rett syndrome (RTT) is a neurodevelopmental disorder resulting from genetic mutations in the methyl CpG binding protein 2 (MeCP2) gene. Specifically, around 35% of RTT patients harbor premature termination codons (PTCs) within the MeCP2 gene due to nonsense mutations. A promising therapeutic avenue for these individuals involves the use of aminoglycosides, which stimulate translational readthrough (TR) by causing stop codons to be interpreted as sense codons. However, the effectiveness of this treatment depends on several factors, including the type of stop codon and the surrounding nucleotides, collectively referred to as the stop codon context (SCC). Here, we develop a high-content reporter system to precisely measure TR efficiency at different SCCs, assess the recovery of the full-length MeCP2 protein, and evaluate its subcellular localization. We have conducted a comprehensive investigation into the intricate relationship between SCC characteristics and TR induction, examining a total of 14 pathogenic MeCP2 nonsense mutations with the aim to advance the prospects of personalized therapy for individuals with RTT. Our results demonstrate that TR induction can successfully restore full-length MeCP2 protein, albeit to varying degrees, contingent upon the SCC and the specific position of the PTC within the MeCP2 mRNA. TR induction can lead to the re-establishment of nuclear localization of MeCP2, indicating the potential restoration of protein functionality. In summary, our findings underscore the significance of SCC-specific approaches in the development of tailored therapies for RTT. By unraveling the relationship between SCC and TR therapy, we pave the way for personalized, individualized treatment strategies that hold promise for improving the lives of individuals affected by this debilitating neurodevelopmental disorder. KEY MESSAGES: The efficiency of readthrough induction at MeCP2 premature termination codons strongly depends on the stop codon context. The position of the premature termination codon on the transcript influences the readthrough inducibility. A new high-content dual reporter assay facilitates the measurement and prediction of readthrough efficiency of specific nucleotide stop contexts. Readthrough induction results in the recovery of full-length MeCP2 and its re-localization to the nucleus. MeCP2 requires only one of its annotated nuclear localization signals.
    MeSH term(s) Codon, Nonsense ; Rett Syndrome/genetics ; Rett Syndrome/metabolism ; Methyl-CpG-Binding Protein 2/genetics ; Methyl-CpG-Binding Protein 2/metabolism ; Humans ; Codon, Terminator ; Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; HEK293 Cells
    Chemical Substances Codon, Nonsense ; Methyl-CpG-Binding Protein 2 ; Codon, Terminator ; MECP2 protein, human ; RNA, Messenger
    Language English
    Publishing date 2024-03-02
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1223802-8
    ISSN 1432-1440 ; 0946-2716
    ISSN (online) 1432-1440
    ISSN 0946-2716
    DOI 10.1007/s00109-024-02436-6
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    Ua VI Zs.36: Show issues Location:
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  4. Article: Calcium in peroxisomes: An essential messenger in an essential cell organelle.

    Sargsyan, Yelena / Kalinowski, Julia / Thoms, Sven

    Frontiers in cell and developmental biology

    2022  Volume 10, Page(s) 992235

    Abstract: Calcium is a central signal transduction element in biology. Peroxisomes are essential cellular organelles, yet calcium handling in peroxisomes has been contentious. Recent advances show that peroxisomes are part of calcium homeostasis in cardiac ... ...

    Abstract Calcium is a central signal transduction element in biology. Peroxisomes are essential cellular organelles, yet calcium handling in peroxisomes has been contentious. Recent advances show that peroxisomes are part of calcium homeostasis in cardiac myocytes and therefore may contribute to or even shape their calcium-dependent functionality. However, the mechanisms of calcium movement between peroxisomes and other cellular sites and their mediators remain elusive. Here, we review calcium handling in peroxisomes in concert with other organelles and summarize the most recent knowledge on peroxisomal involvement in calcium dynamics with a focus on mammalian cells.
    Language English
    Publishing date 2022-08-30
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2022.992235
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  5. Article ; Online: Functions of Vertebrate Ferlins.

    Bulankina, Anna V / Thoms, Sven

    Cells

    2020  Volume 9, Issue 3

    Abstract: Ferlins are multiple-C2-domain proteins involved in Ca2+-triggered membrane dynamics within the secretory, endocytic and lysosomal pathways. In bony vertebrates there are six ferlin genes encoding, in humans, dysferlin, otoferlin, myoferlin, Fer1L5 and 6 ...

    Abstract Ferlins are multiple-C2-domain proteins involved in Ca2+-triggered membrane dynamics within the secretory, endocytic and lysosomal pathways. In bony vertebrates there are six ferlin genes encoding, in humans, dysferlin, otoferlin, myoferlin, Fer1L5 and 6 and the long noncoding RNA Fer1L4. Mutations in
    MeSH term(s) Animals ; Humans ; Muscular Dystrophies, Limb-Girdle/metabolism ; Vertebrates/metabolism
    Language English
    Publishing date 2020-02-25
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells9030534
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  6. Article ; Online: Correction: Nonsense mutation suppression is enhanced by targeting different stages of the protein synthesis process.

    Wittenstein, Amnon / Caspi, Michal / Rippin, Ido / Elroy-Stein, Orna / Eldar-Finkelman, Hagit / Thoms, Sven / Rosin-Arbesfeld, Rina

    PLoS biology

    2024  Volume 22, Issue 2, Page(s) e3002524

    Abstract: This corrects the article DOI: 10.1371/journal.pbio.3002355.]. ...

    Abstract [This corrects the article DOI: 10.1371/journal.pbio.3002355.].
    Language English
    Publishing date 2024-02-14
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.3002524
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6193: Show issues Location:
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  7. Book ; Online ; Thesis: Peroxisomal calcium handling and homeostasis

    Sargsyan, Yelena [Verfasser] / Thoms, Sven [Akademischer Betreuer] / Thoms, Sven [Gutachter] / Rizzoli, Silvio [Gutachter]

    2022  

    Author's details Yelena Sargsyan ; Gutachter: Sven Thoms, Silvio Rizzoli ; Betreuer: Sven Thoms
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language English
    Publisher Niedersächsische Staats- und Universitätsbibliothek Göttingen
    Publishing place Göttingen
    Document type Book ; Online ; Thesis
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  8. Article ; Online: Import of proteins into peroxisomes: piggybacking to a new home away from home.

    Thoms, Sven

    Open biology

    2015  Volume 5, Issue 11

    Abstract: Peroxisomes are capable of importing folded and oligomeric proteins. However, it is a matter of dispute whether oligomer import by peroxisomes is the exception or the rule. Here, I argue for a clear distinction between homo-oligomeric proteins that are ... ...

    Abstract Peroxisomes are capable of importing folded and oligomeric proteins. However, it is a matter of dispute whether oligomer import by peroxisomes is the exception or the rule. Here, I argue for a clear distinction between homo-oligomeric proteins that are essentially peroxisomal, and dually localized hetero-oligomers that access the peroxisome by piggyback import, localizing there in limited number, whereas the majority remain in the cytosol. Homo-oligomeric proteins comprise the majority of all peroxisomal matrix proteins. There is evidence that binding by Pex5 in the cytosol can regulate their oligomerization state before import. The hetero-oligomer group is made up of superoxide dismutase and lactate dehydrogenase. These proteins have evolved mechanisms that render import inefficient and retain the majority of proteins in the cytosol.
    MeSH term(s) Amino Acid Sequence ; Animals ; Humans ; Molecular Sequence Data ; Peroxisome-Targeting Signal 1 Receptor ; Peroxisomes/metabolism ; Protein Multimerization ; Protein Transport ; Receptors, Cytoplasmic and Nuclear/chemistry ; Receptors, Cytoplasmic and Nuclear/metabolism
    Chemical Substances PEX5 protein, human ; Peroxisome-Targeting Signal 1 Receptor ; Receptors, Cytoplasmic and Nuclear
    Language English
    Publishing date 2015-11
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2630944-0
    ISSN 2046-2441 ; 2046-2441
    ISSN (online) 2046-2441
    ISSN 2046-2441
    DOI 10.1098/rsob.150148
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  9. Book ; Online ; Thesis: Mechanistic differences in mouse models of heart failure with preserved ejection fraction

    Swarnkar, Surabhi [Verfasser] / Katschinski, Dörthe [Akademischer Betreuer] / Thoms, Sven [Gutachter] / Meyer, Thomas [Gutachter] / Schnelle, Moritz Thomas [Gutachter]

    2024  

    Author's details Surabhi Swarnkar ; Gutachter: Sven Thoms, Thomas Meyer, Moritz Thomas Schnelle ; Betreuer: Dörthe Katschinski
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language English
    Publisher Niedersächsische Staats- und Universitätsbibliothek Göttingen
    Publishing place Göttingen
    Document type Book ; Online ; Thesis
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  10. Article ; Online: Calcium in peroxisomes

    Yelena Sargsyan / Julia Kalinowski / Sven Thoms

    Frontiers in Cell and Developmental Biology, Vol

    An essential messenger in an essential cell organelle

    2022  Volume 10

    Abstract: Calcium is a central signal transduction element in biology. Peroxisomes are essential cellular organelles, yet calcium handling in peroxisomes has been contentious. Recent advances show that peroxisomes are part of calcium homeostasis in cardiac ... ...

    Abstract Calcium is a central signal transduction element in biology. Peroxisomes are essential cellular organelles, yet calcium handling in peroxisomes has been contentious. Recent advances show that peroxisomes are part of calcium homeostasis in cardiac myocytes and therefore may contribute to or even shape their calcium-dependent functionality. However, the mechanisms of calcium movement between peroxisomes and other cellular sites and their mediators remain elusive. Here, we review calcium handling in peroxisomes in concert with other organelles and summarize the most recent knowledge on peroxisomal involvement in calcium dynamics with a focus on mammalian cells.
    Keywords peroxisomes ; calcium ; Ca2+ ; cell organelle ; cardiomyocyte ; FRET sensor ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2022-08-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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