@article{discovery1472259, note = {{\copyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice-Final version full access. Creative Commons Attribution Unported License applies to Author Choice Articles}, month = {April}, pages = {9951--9958}, journal = {Journal of Biological Chemistry}, year = {2015}, volume = {290}, number = {16}, title = {Systemic amyloidosis: lessons from {\ensuremath{\beta}}2-microglobulin.}, abstract = {{\ensuremath{\beta}}2-Microglobulin is responsible for systemic amyloidosis affecting patients undergoing long-term hemodialysis. Its genetic variant D76N causes a very rare form of familial systemic amyloidosis. These two types of amyloidoses differ significantly in terms of the tissue localization of deposits and for major pathological features. Considering how the amyloidogenesis of the {\ensuremath{\beta}}2-microglobulin mechanism has been scrutinized in depth for the last three decades, the comparative analysis of molecular and pathological properties of wild type {\ensuremath{\beta}}2-microglobulin and of the D76N variant offers a unique opportunity to critically reconsider the current understanding of the relation between the protein's structural properties and its pathologic behavior.}, author = {Stoppini, M and Bellotti, V}, url = {http://dx.doi.org/10.1074/jbc.R115.639799}, issn = {1083-351X}, keywords = {Amyloid, Atomic Force Microscopy (AFM), Fibrillogenesis in Vitro, Genetic Variant Asp76Asn, Mechanism of Amyloidogenesis, Protein Aggregation, Protein Misfolding, Protein Structure, {\ensuremath{\beta}}2-Microglobulin, Amyloid, Amyloidosis, Doxycycline, Humans, Models, Molecular, Mutation, Protein Aggregation, Pathological, Protein Conformation, Renal Dialysis, Single-Chain Antibodies, beta 2-Microglobulin} }