{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Myers SL"],"funding":["Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["2311-21"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7618240"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["45(7)"],"pubmed_abstract":["Beta(2)-microglobulin (beta(2)m) forms amyloid fibrils that deposit in the musculo-skeletal system in patients undergoing long-term hemodialysis. How beta(2)m self-assembles in vivo is not understood, since the monomeric wild-type protein is incapable of forming fibrils in isolation in vitro at neutral pH, while elongation of fibril-seeds made from recombinant protein has only been achieved at low pH or at neutral pH in the presence of detergents or cosolvents. Here we describe a systematic study of the effect of 11 physiologically relevant factors on beta(2)m fibrillogenesis at pH 7.0 without denaturants. By comparing the results obtained for the wild-type protein with those of two variants (DeltaN6 and V37A), the role of protein stability in fibrillogenesis is explored. We show that Delt"],"journal":["Biochemistry"],"pubmed_title":["A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH."],"pmcid":["PMC7618240"],"funding_grant_id":["069064","SF16972"],"pubmed_authors":["Radford SE","Hewitt EW","Tennent GA","Morten IJ","Myers SL","Jones S","Jahn TR"],"additional_accession":[]},"is_claimable":false,"name":"A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH.","description":"Beta(2)-microglobulin (beta(2)m) forms amyloid fibrils that deposit in the musculo-skeletal system in patients undergoing long-term hemodialysis. How beta(2)m self-assembles in vivo is not understood, since the monomeric wild-type protein is incapable of forming fibrils in isolation in vitro at neutral pH, while elongation of fibril-seeds made from recombinant protein has only been achieved at low pH or at neutral pH in the presence of detergents or cosolvents. Here we describe a systematic study of the effect of 11 physiologically relevant factors on beta(2)m fibrillogenesis at pH 7.0 without denaturants. By comparing the results obtained for the wild-type protein with those of two variants (DeltaN6 and V37A), the role of protein stability in fibrillogenesis is explored. We show that Delt","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Feb","modification":"2026-06-04T09:46:21.256Z","creation":"2026-05-07T03:12:53.846Z"},"accession":"S-EPMC7618240","cross_references":{"pubmed":["16475820"],"doi":["10.1021/bi052434i"]}}