{"entity": "researcher", "timestamp": "2026-08-26T22:57:51.261Z", "family": "Hebert", "given": "Hans", "initials": "H", "orcid": "0000-0002-3220-9402", "affiliations": ["School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, Department of Biosciences and Nutrition, Karolinska Institutet, 141 52, Huddinge, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/651ca91cbe0348bdaf554a8a3167f9b5.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/651ca91cbe0348bdaf554a8a3167f9b5"}}, "publications": [{"entity": "publication", "iuid": "d9e3bdae31884d4d85906019fa98ed5b", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/d9e3bdae31884d4d85906019fa98ed5b.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/d9e3bdae31884d4d85906019fa98ed5b"}}, "title": "Augmentation of Bri2 molecular chaperone activity against amyloid-\u03b2 reduces neurotoxicity in mouse hippocampus in vitro.", "authors": [{"family": "Chen", "given": "Gefei", "initials": "G"}, {"family": "Andrade-Talavera", "given": "Yuniesky", "initials": "Y", "orcid": "0000-0002-5295-0169", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/54ebe4d6cc4d4fe0b550cb1b15b9196b.json"}}, {"family": "Tambaro", "given": "Simone", "initials": "S"}, {"family": "Leppert", "given": "Axel", "initials": "A", "orcid": "0000-0001-6223-3350", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e0ca2c7662be40c68b0585acb903e90d.json"}}, {"family": "Nilsson", "given": "Harriet E", "initials": "HE"}, {"family": "Zhong", "given": "Xueying", "initials": "X"}, {"family": "Landreh", "given": "Michael", "initials": "M", "orcid": "0000-0002-7958-4074", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fccd56038e8a4c2992ed2b49f3d8d2bd.json"}}, {"family": "Nilsson", "given": "Per", "initials": "P", "orcid": "0000-0001-6450-0870", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6188d879ab214c3c8ec274f110d4d037.json"}}, {"family": "Hebert", "given": "Hans", "initials": "H", "orcid": "0000-0002-3220-9402", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/651ca91cbe0348bdaf554a8a3167f9b5.json"}}, {"family": "Biverst\u00e5l", "given": "Henrik", "initials": "H", "orcid": "0000-0002-2097-7658", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/603a87443b7b4315b6331a51e8103fb5.json"}}, {"family": "Fisahn", "given": "Andr\u00e9", "initials": "A"}, {"family": "Abelein", "given": "Axel", "initials": "A", "orcid": "0000-0002-8079-3017", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f708fb9956444ba89ba3bdaececa14a5.json"}}, {"family": "Johansson", "given": "Jan", "initials": "J"}], "type": "journal article", "published": "2020-01-20", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "3", "issue": "1", "pages": "32", "issn-l": "2399-3642"}, "abstract": "Molecular chaperones play important roles in preventing protein misfolding and its potentially harmful consequences. Deterioration of molecular chaperone systems upon ageing are thought to underlie age-related neurodegenerative diseases, and augmenting their activities could have therapeutic potential. The dementia relevant domain BRICHOS from the Bri2 protein shows qualitatively different chaperone activities depending on quaternary structure, and assembly of monomers into high-molecular weight oligomers reduces the ability to prevent neurotoxicity induced by the Alzheimer-associated amyloid-\u03b2 peptide 1-42 (A\u03b242). Here we design a Bri2 BRICHOS mutant (R221E) that forms stable monomers and selectively blocks a main source of toxic species during A\u03b242 aggregation. Wild type Bri2 BRICHOS oligomers are partly disassembled into monomers in the presence of the R221E mutant, which leads to potentiated ability to prevent A\u03b242 toxicity to neuronal network activity. These results suggest that the activity of endogenous molecular chaperones may be modulated to enhance anti-A\u03b242 neurotoxic effects.", "doi": "10.1038/s42003-020-0757-z", "pmid": "31959875", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6971075"}, {"db": "pii", "key": "10.1038/s42003-020-0757-z"}], "notes": [], "created": "2026-08-21T11:54:31.270Z", "modified": "2026-08-21T11:54:31.548Z"}]}