{"entity": "researcher", "timestamp": "2026-07-22T17:41:16.093Z", "family": "Anan", "given": "Intissar", "initials": "I", "orcid": "0000-0003-2874-7643", "affiliations": [], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/923515859dae4f16ae6f4cee53515f98.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/923515859dae4f16ae6f4cee53515f98"}}, "publications": [{"entity": "publication", "iuid": "0acc2048f2074e63bddc5c1c8e0bc768", "links": {"self": {"href": "https://publications.scilifelab.se/publication/0acc2048f2074e63bddc5c1c8e0bc768.json"}, "display": {"href": "https://publications.scilifelab.se/publication/0acc2048f2074e63bddc5c1c8e0bc768"}}, "title": "Structural basis for transthyretin amyloid formation in vitreous body of the eye.", "authors": [{"family": "Iakovleva", "given": "Irina", "initials": "I", "orcid": "0000-0002-9500-5917", "researcher": {"href": "https://publications.scilifelab.se/researcher/b5fd05e56e164227b137bac9a879af58.json"}}, {"family": "Hall", "given": "Michael", "initials": "M", "orcid": "0000-0003-0864-9798", "researcher": {"href": "https://publications.scilifelab.se/researcher/7489a92a241f4d0d9f8ef6eb4fcb3858.json"}}, {"family": "Oelker", "given": "Melanie", "initials": "M", "orcid": "0000-0001-7301-8445", "researcher": {"href": "https://publications.scilifelab.se/researcher/0d4b43ce3822421e998c7ecead0f2e1a.json"}}, {"family": "Sandblad", "given": "Linda", "initials": "L", "orcid": "0000-0003-3492-3287", "researcher": {"href": "https://publications.scilifelab.se/researcher/070825e0190a4e9a932e79663d2bc89f.json"}}, {"family": "Anan", "given": "Intissar", "initials": "I", "orcid": "0000-0003-2874-7643", "researcher": {"href": "https://publications.scilifelab.se/researcher/923515859dae4f16ae6f4cee53515f98.json"}}, {"family": "Sauer-Eriksson", "given": "A Elisabeth", "initials": "AE", "orcid": "0000-0003-0124-0199", "researcher": {"href": "https://publications.scilifelab.se/researcher/9435049fbe2745b59e04558cc5201f95.json"}}], "type": "journal article", "published": "2021-12-08", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "12", "issue": "1", "pages": "7141", "issn-l": "2041-1723"}, "abstract": "Amyloid transthyretin (ATTR) amyloidosis is characterized by the abnormal accumulation of ATTR fibrils in multiple organs. However, the structure of ATTR fibrils from the eye is poorly understood. Here, we used cryo-EM to structurally characterize vitreous body ATTR fibrils. These structures were distinct from previously characterized heart fibrils, even though both have the same mutation and type A pathology. Differences were observed at several structural levels: in both the number and arrangement of protofilaments, and the conformation of the protein fibril in each layer of protofilaments. Thus, our results show that ATTR protein structure and its assembly into protofilaments in the type A fibrils can vary between patients carrying the same mutation. By analyzing and matching the interfaces between the amino acids in the ATTR fibril with those in the natively folded TTR, we are able to propose a mechanism for the structural conversion of TTR into a fibrillar form.", "doi": "10.1038/s41467-021-27481-4", "pmid": "34880242", "labels": {"Cryo-EM": "Collaborative", "Structural Proteomics": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-021-27481-4"}, {"db": "pmc", "key": "PMC8654999"}], "notes": [], "created": "2021-12-09T13:57:20.280Z", "modified": "2022-01-03T10:03:27.020Z"}, {"entity": "publication", "iuid": "f59ae4f4ba0c42cda3fce4888d703552", "links": {"self": {"href": "https://publications.scilifelab.se/publication/f59ae4f4ba0c42cda3fce4888d703552.json"}, "display": {"href": "https://publications.scilifelab.se/publication/f59ae4f4ba0c42cda3fce4888d703552"}}, "title": "Metabolomics analysis for diagnosis and biomarker discovery of transthyretin amyloidosis.", "authors": [{"family": "Olsson", "given": "Malin", "initials": "M"}, {"family": "Hellman", "given": "Urban", "initials": "U"}, {"family": "Wixner", "given": "Jonas", "initials": "J"}, {"family": "Anan", "given": "Intissar", "initials": "I", "orcid": "0000-0003-2874-7643", "researcher": {"href": "https://publications.scilifelab.se/researcher/923515859dae4f16ae6f4cee53515f98.json"}}], "type": "journal article", "published": "2021-07-28", "journal": {"title": "Amyloid", "issn": "1744-2818", "pages": "1-9", "issn-l": null}, "abstract": "Untargeted metabolomics is a well-established technique and a powerful tool to find potential plasma biomarkers for early diagnosing hereditary transthyretin amyloidosis. Hereditary transthyretin amyloidosis (ATTRv) is a disabling and fatal disease with different clinical features such as polyneuropathy, cardiomyopathy, different gastrointestinal symptoms and renal failure. Plasma specimens collected from 27 patients with ATTRv (ATTRV30M), 26 asymptomatic TTRV30M carriers and 26 control individuals were subjected to gas chromatography (GC)- and liquid chromatography (LC)-mass spectrometry (MS)-based metabolomics analysis. Partial least squares discriminant and univariate analysis was used to analyse the data. The models constructed by Partial least squares-discriminant analysis (PLS-DA) could clearly discriminate ATTRV30M patients from controls and asymptomatic TTRV30M carriers. In total, 24 plasma metabolites (VIP > 1.0 and p < .05) were significantly altered in ATTRV30M patient group (6 increased and 18 decreased). Eleven of these distinguished the ATTRV30M group from both controls and TTRV30M carriers. Plasma metabolomics analysis revealed marked changes in several pathways in patients with ATTRV30M amyloidosis. Statistical analysis identified a panel of biomarkers that could effectively separate controls/TTRV30M carriers from ATTRV30M patients. These biomarkers can potentially be used to diagnose patients at an early stage of the disease.", "doi": "10.1080/13506129.2021.1958775", "pmid": "34319177", "labels": {"Swedish Metabolomics Centre": "Service"}, "xrefs": [], "notes": [], "created": "2021-12-09T20:04:01.870Z", "modified": "2025-10-17T13:03:15.884Z"}]}