{"entity": "researcher", "timestamp": "2026-09-27T17:02:45.728Z", "family": "Persson", "given": "Bengt", "initials": "B", "orcid": "0000-0003-3165-5344", "affiliations": ["Department of Cell and Molecular Biology, Science for Life Laboratory, Uppsala University, S-751 24, Uppsala, Sweden. bengt.persson@icm.uu.se.", "Department of Medical Biochemistry and Biophysics, Science for Life Laboratory, Karolinska Institutet, S-17177, Stockholm, Sweden. bengt.persson@icm.uu.se."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/1fe4432f839c482babc8e315458be763.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/1fe4432f839c482babc8e315458be763"}}, "publications": [{"entity": "publication", "iuid": "bbf55847dc1943de9b92f4ab7889dd33", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/bbf55847dc1943de9b92f4ab7889dd33.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/bbf55847dc1943de9b92f4ab7889dd33"}}, "title": "Transcriptomics of cardiac biopsies reveals differences in patients with or without diagnostic parameters for heart failure with preserved ejection fraction.", "authors": [{"family": "Das", "given": "Sarbashis", "initials": "S", "orcid": "0000-0001-8799-691X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7fd4a3d3b3574ecf8afb398dcd247004.json"}}, {"family": "Frisk", "given": "Christoffer", "initials": "C"}, {"family": "Eriksson", "given": "Maria J", "initials": "MJ"}, {"family": "Walentinsson", "given": "Anna", "initials": "A"}, {"family": "Corbascio", "given": "Matthias", "initials": "M"}, {"family": "Hage", "given": "Camilla", "initials": "C"}, {"family": "Kumar", "given": "Chanchal", "initials": "C"}, {"family": "Asp", "given": "Michaela", "initials": "M", "orcid": "0000-0001-5941-7220", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0a8f28391c524289bbcaf0a5d809b40c.json"}}, {"family": "Lundeberg", "given": "Joakim", "initials": "J", "orcid": "0000-0003-4313-1601", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d9fa47767cd14ef2b9528c8b998cf095.json"}}, {"family": "Maret", "given": "Eva", "initials": "E"}, {"family": "Persson", "given": "Hans", "initials": "H"}, {"family": "Linde", "given": "Cecilia", "initials": "C"}, {"family": "Persson", "given": "Bengt", "initials": "B", "orcid": "0000-0003-3165-5344", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1fe4432f839c482babc8e315458be763.json"}}], "type": "journal article", "published": "2019-02-28", "journal": {"title": "Sci Rep", "issn": "2045-2322", "volume": "9", "issue": "1", "pages": "3179", "issn-l": "2045-2322"}, "abstract": "Heart failure affects 2-3% of adult Western population. Prevalence of heart failure with preserved left ventricular (LV) ejection fraction (HFpEF) increases. Studies suggest HFpEF patients to have altered myocardial structure and functional changes such as incomplete relaxation and increased cardiac stiffness. We hypothesised that patients undergoing elective coronary bypass surgery (CABG) with HFpEF characteristics would show distinctive gene expression compared to patients with normal LV physiology. Myocardial biopsies for mRNA expression analysis were obtained from sixteen patients with LV ejection fraction \u226545%. Five out of 16 patients (31%) had echocardiographic characteristics and increased NTproBNP levels indicative of HFpEF and this group was used as HFpEF proxy, while 11 patients had Normal LV physiology. Utilising principal component analysis, the gene expression data clustered into two groups, corresponding to HFpEF proxy and Normal physiology, and 743 differentially expressed genes were identified. The associated top biological functions were cardiac muscle contraction, oxidative phosphorylation, cellular remodelling and matrix organisation. Our results also indicate that upstream regulatory events, including inhibition of transcription factors STAT4, SRF and TP53, and activation of transcription repressors HEY2 and KDM5A, could provide explanatory mechanisms to observed gene expression differences and ultimately cardiac dysfunction in the HFpEF proxy group.", "doi": "10.1038/s41598-019-39445-2", "pmid": "30816197", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6395693"}, {"db": "pii", "key": "10.1038/s41598-019-39445-2"}], "notes": [], "created": "2026-09-23T09:25:55.340Z", "modified": "2026-09-23T09:25:55.467Z"}, {"entity": "publication", "iuid": "c4a7c9b833194b5dbb772434858bf930", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c4a7c9b833194b5dbb772434858bf930.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c4a7c9b833194b5dbb772434858bf930"}}, "title": "Computational studies of human class V alcohol dehydrogenase - the odd sibling.", "authors": [{"family": "\u00d6stberg", "given": "Linus J", "initials": "LJ"}, {"family": "Persson", "given": "Bengt", "initials": "B", "orcid": "0000-0003-3165-5344", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1fe4432f839c482babc8e315458be763.json"}}, {"family": "H\u00f6\u00f6g", "given": "Jan-Olov", "initials": "JO"}], "type": "journal article", "published": "2016-07-25", "journal": {"title": "BMC Biochem.", "issn": "1471-2091", "volume": "17", "issue": "1", "pages": "16", "issn-l": "1471-2091"}, "abstract": "All known attempts to isolate and characterize mammalian class V alcohol dehydrogenase (class V ADH), a member of the large ADH protein family, at the protein level have failed. This indicates that the class V ADH protein is not stable in a non-cellular environment, which is in contrast to all other human ADH enzymes. In this report we present evidence, supported with results from computational analyses performed in combination with earlier in vitro studies, why this ADH behaves in an atypical way.\n\nUsing a combination of structural calculations and sequence analyses, we were able to identify local structural differences between human class V ADH and other human ADHs, including an elongated \u03b2-strands and a labile \u03b1-helix at the subunit interface region of each chain that probably disturb it. Several amino acid residues are strictly conserved in class I-IV, but altered in class V ADH. This includes a for class V ADH unique and conserved Lys51, a position directly involved in the catalytic mechanism in other ADHs, and nine other class V ADH-specific residues.\n\nIn this study we show that there are pronounced structural changes in class V ADH as compared to other ADH enzymes. Furthermore, there is an evolutionary pressure among the mammalian class V ADHs, which for most proteins indicate that they fulfill a physiological function. We assume that class V ADH is expressed, but unable to form active dimers in a non-cellular environment, and is an atypical mammalian ADH. This is compatible with previous experimental characterization and present structural modelling. It can be considered the odd sibling of the ADH protein family and so far seems to be a pseudoenzyme with another hitherto unknown physiological function.", "doi": "10.1186/s12858-016-0072-y", "pmid": "27455956", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC4960878"}, {"db": "pii", "key": "10.1186/s12858-016-0072-y"}], "notes": [], "created": "2018-12-05T12:16:28.928Z", "modified": "2026-09-23T12:40:04.631Z"}]}