{"entity": "researcher", "timestamp": "2026-09-23T17:10:28.528Z", "family": "Rosenberger", "given": "Florian A", "initials": "FA", "orcid": "0000-0003-4604-6170", "affiliations": ["Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.", "Department of Molecular Medicine and Surgery, Karolinska Institutet, Stockholm, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/e526ebcc7b834f9a89e41542b5feeac1.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/e526ebcc7b834f9a89e41542b5feeac1"}}, "publications": [{"entity": "publication", "iuid": "b0fd2096917f468b844d001b7cba9a1b", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/b0fd2096917f468b844d001b7cba9a1b.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/b0fd2096917f468b844d001b7cba9a1b"}}, "title": "The mitochondrial methylation potential gates mitoribosome assembly.", "authors": [{"family": "Glasgow", "given": "Ruth I C", "initials": "RIC"}, {"family": "Singh", "given": "Vivek", "initials": "V", "orcid": "0000-0003-4656-3362", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fae8ba5c9d2d4a6ab32734ed7deaa7c3.json"}}, {"family": "Pe\u00f1a-P\u00e9rez", "given": "Luc\u00eda", "initials": "L", "orcid": "0000-0002-5044-7754", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/588586bc4a6b4b9ab13e10d0b83cfe53.json"}}, {"family": "Wilhalm", "given": "Alissa", "initials": "A"}, {"family": "Moedas", "given": "Marco F", "initials": "MF"}, {"family": "Moore", "given": "David", "initials": "D"}, {"family": "Rosenberger", "given": "Florian A", "initials": "FA", "orcid": "0000-0003-4604-6170", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e526ebcc7b834f9a89e41542b5feeac1.json"}}, {"family": "Li", "given": "Xinping", "initials": "X"}, {"family": "Atanassov", "given": "Ilian", "initials": "I", "orcid": "0000-0001-8259-2545", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d8192a12252842d3bb11cc553bc4d546.json"}}, {"family": "Saba", "given": "Mira", "initials": "M"}, {"family": "Cipullo", "given": "Miriam", "initials": "M"}, {"family": "Rorbach", "given": "Joanna", "initials": "J", "orcid": "0000-0002-2891-2840", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0a00abe0efcc458d8879f14186202a63.json"}}, {"family": "Wedell", "given": "Anna", "initials": "A"}, {"family": "Freyer", "given": "Christoph", "initials": "C", "orcid": "0000-0003-0418-1673", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fba742fee9324f4ba469cc84a6bfd9c6.json"}}, {"family": "Amunts", "given": "Alexey", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6c79bee23e114906bc847dfbd0975139.json"}}, {"family": "Wredenberg", "given": "Anna", "initials": "A", "orcid": "0000-0002-2500-6121", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1bd991602b184ab48a4dca93b7901466.json"}}], "type": "journal article", "published": "2025-06-25", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "16", "issue": "1", "pages": "5388", "issn-l": "2041-1723"}, "abstract": "S-adenosylmethionine (SAM) is the principal methyl donor in cells and is essential for mitochondrial gene expression, influencing RNA modifications, translation, and ribosome biogenesis. Using direct long-read RNA sequencing in mouse tissues and embryonic fibroblasts, we show that processing of the mitochondrial ribosomal gene cluster fails in the absence of mitochondrial SAM, leading to an accumulation of unprocessed precursors. Proteomic analysis of ribosome fractions revealed these precursors associated with processing and assembly factors, indicating stalled biogenesis. Structural analysis by cryo-electron microscopy demonstrated that SAM-dependent methylation is required for peptidyl transferase centre formation during mitoribosome assembly. Our findings identify a critical role for SAM in coordinating mitoribosomal RNA processing and large subunit maturation, linking cellular methylation potential to mitochondrial translation capacity.", "doi": "10.1038/s41467-025-60977-x", "pmid": "40562754", "labels": {"SciLifeLab Fellow": "", "Alexey Amunts": ""}, "xrefs": [{"db": "pmc", "key": "PMC12198368"}, {"db": "pii", "key": "10.1038/s41467-025-60977-x"}], "notes": [], "created": "2026-09-23T11:28:46.433Z", "modified": "2026-09-23T11:28:46.598Z"}, {"entity": "publication", "iuid": "1f8a79ceab774d4ab2dbc31a933e7740", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1f8a79ceab774d4ab2dbc31a933e7740.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1f8a79ceab774d4ab2dbc31a933e7740"}}, "title": "Severe congenital lactic acidosis and hypertrophic cardiomyopathy caused by an intronic variant in NDUFB7.", "authors": [{"family": "Correia", "given": "Sandrina P", "initials": "SP"}, {"family": "Moedas", "given": "Marco F", "initials": "MF"}, {"family": "Naess", "given": "Karin", "initials": "K"}, {"family": "Bruhn", "given": "Helene", "initials": "H"}, {"family": "Maffezzini", "given": "Camilla", "initials": "C"}, {"family": "Calvo-Garrido", "given": "Javier", "initials": "J"}, {"family": "Lesko", "given": "Nicole", "initials": "N"}, {"family": "Wibom", "given": "Rolf", "initials": "R"}, {"family": "Schober", "given": "Florian A", "initials": "FA", "orcid": "0000-0003-4604-6170", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e526ebcc7b834f9a89e41542b5feeac1.json"}}, {"family": "Jemt", "given": "Anders", "initials": "A"}, {"family": "Stranneheim", "given": "Henrik", "initials": "H"}, {"family": "Freyer", "given": "Christoph", "initials": "C", "orcid": "0000-0003-0418-1673", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fba742fee9324f4ba469cc84a6bfd9c6.json"}}, {"family": "Wedell", "given": "Anna", "initials": "A"}, {"family": "Wredenberg", "given": "Anna", "initials": "A", "orcid": "0000-0002-2500-6121", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1bd991602b184ab48a4dca93b7901466.json"}}], "type": "case reports", "published": "2021-04-00", "journal": {"title": "Hum. Mutat.", "issn": "1098-1004", "volume": "42", "issue": "4", "pages": "378-384", "issn-l": "1059-7794"}, "abstract": "Mutations in structural subunits and assembly factors of complex I of the oxidative phosphorylation system constitute the most common cause of mitochondrial respiratory chain defects. Such mutations can present a wide range of clinical manifestations, varying from mild deficiencies to severe, lethal disorders. We describe a patient presenting intrauterine growth restriction and anemia, which displayed postpartum hypertrophic cardiomyopathy, lactic acidosis, encephalopathy, and a severe complex I defect with fatal outcome. Whole genome sequencing revealed an intronic biallelic mutation in the NDUFB7 gene (c.113-10C>G) and splicing pattern alterations in NDUFB7 messenger RNA were confirmed by RNA Sequencing. The detected variant resulted in a significant reduction of the NDUFB7 protein and reduced complex I activity. Complementation studies with expression of wild-type NDUFB7 in patient fibroblasts normalized complex I function. Here we report a case with a primary complex I defect due to a homozygous mutation in an intron region of the NDUFB7 gene.", "doi": "10.1002/humu.24173", "pmid": "33502047", "labels": [], "xrefs": [], "notes": [], "created": "2026-09-23T11:56:37.171Z", "modified": "2026-09-23T11:56:37.240Z"}, {"entity": "publication", "iuid": "e0818dac40b84474a47730a2afbddbb6", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/e0818dac40b84474a47730a2afbddbb6.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/e0818dac40b84474a47730a2afbddbb6"}}, "title": "Novel Mutation m.10372A>G in MT-ND3 Causing Sensorimotor Axonal Polyneuropathy.", "authors": [{"family": "Bruhn", "given": "Helene", "initials": "H"}, {"family": "Samuelsson", "given": "Kristin", "initials": "K"}, {"family": "Schober", "given": "Florian A", "initials": "FA", "orcid": "0000-0003-4604-6170", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e526ebcc7b834f9a89e41542b5feeac1.json"}}, {"family": "Engvall", "given": "Martin", "initials": "M"}, {"family": "Lesko", "given": "Nicole", "initials": "N"}, {"family": "Wibom", "given": "Rolf", "initials": "R"}, {"family": "Nennesmo", "given": "Inger", "initials": "I"}, {"family": "Calvo-Garrido", "given": "Javier", "initials": "J"}, {"family": "Press", "given": "Rayomand", "initials": "R"}, {"family": "Stranneheim", "given": "Henrik", "initials": "H"}, {"family": "Freyer", "given": "Christoph", "initials": "C"}, {"family": "Wedell", "given": "Anna", "initials": "A"}, {"family": "Wredenberg", "given": "Anna", "initials": "A"}], "type": "journal article", "published": "2021-04-00", "journal": {"title": "Neurol Genet", "issn": "2376-7839", "volume": "7", "issue": "2", "pages": "e566", "issn-l": null}, "abstract": "To investigate the pathogenicity of a novel MT-ND3 mutation identified in a patient with adult-onset sensorimotor axonal polyneuropathy and report the clinical, morphologic, and biochemical findings.\n\nClinical assessments and morphologic and biochemical investigations of skeletal muscle and cultured myoblasts from the patient were performed. Whole-genome sequencing (WGS) of DNA from skeletal muscle and Sanger sequencing of mitochondrial DNA (mtDNA) from both skeletal muscle and cultured myoblasts were performed. Heteroplasmic levels of mutated mtDNA in different tissues were quantified by last-cycle hot PCR.\n\nMuscle showed ragged red fibers, paracrystalline inclusions, a significant reduction in complex I (CI) respiratory chain (RC) activity, and decreased adenosine triphosphate (ATP) production for all substrates used by CI. Sanger sequencing of DNA from skeletal muscle detected a unique previously unreported heteroplasmic mutation in mtDNA encoded MT-ND3, coding for a subunit in CI. WGS confirmed the mtDNA mutation but did not detect any other mutation explaining the disease. Cultured myoblasts, however, did not carry the mutation, and RC activity measurements in myoblasts were normal.\n\nWe report a case with adult-onset sensorimotor axonal polyneuropathy caused by a novel mtDNA mutation in MT-ND3. Loss of heteroplasmy in blood, cultured fibroblasts and myoblasts from the patient, and normal measurement of RC activity of the myoblasts support pathogenicity of the mutation. These findings highlight the importance of mitochondrial investigations in patients presenting with seemingly idiopathic polyneuropathy, especially if muscle also is affected.", "doi": "10.1212/NXG.0000000000000566", "pmid": "33732874", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC7962437"}, {"db": "pii", "key": "NG2020014720"}], "notes": [], "created": "2026-09-23T12:57:20.594Z", "modified": "2026-09-23T12:57:20.652Z"}]}