Unfolding, Aggregation, and Seeded Amyloid Formation of Lysine-58-Cleaved β2-Microglobulin

Autor: Dorthe B. Corlin, Mogens H. Nissen, Anna G. Tempesta, Thomas J. D. Jørgensen, Rogert Bauer, Jesper S. Pedersen, Peter Roepstorff, Noemi Rozlosnik, Niels H. H. Heegaard

Publikováno v: Pedersen, J S, Heegaard, N H H, Jørgensen, T D, Rozlosnik, N, Corlin, D B, Tempesta, A G, Roepstorff, P, Bauer, R & Nissen, M H 2005, ' Unfolding, aggregation, and seeded amyloid formation of lysine-58-cleaved beta(2)-microglobulin ', Biochemistry, vol. 44, no. 11, pp. 4397-4407 . https://doi.org/10.1021/bi047594t

Beta(2)-microglobulin (beta(2)m) is the amyloidogenic protein in dialysis-related amyloidosis, but the mechanisms underlying beta(2)m fibrillogenesis in vivo are largely unknown. We study a structural variant of beta(2)m that has been linked to cance

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https://doi.org/10.1021/bi047594t