References
- Stoppini M, Bellotti V, Mangione P, Merlini G, Ferri G. Use of anti-β2-microglobulin mAb to study formation of amyloid fibrils. Eur J Biochem 1997;249:1–26
- Motomiya Y, Ando Y, Haraoka K, Sun X, Morita H, Amano I, Uchimura T, et al. Studies on unfolded β2-microglobulin at C-terminal in dialysis-related amyloidosis. Kidney Int 2005;67:314–20
- Myers SL, Jones S, Jahn TR, Morten IJ, Tennent GA, Hewitt EW, Radford SE. A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH. Biochemistry 2006;45:2311–21
- Linke RP, Hampl H, Lobeck H, Ritz E, Bommer J, Waldherr R, Eulitz M. Lysine-specific cleavage of β2-microglobulin in amyloid deposits associated with hemodialysis. Kidney Int 1989;36:675–81
- Stoppini MS, Arcidiaco P, Mangione P, Giorgetti S, Brancaccio D, Bellotti V. Detection of fragments of β2-microglobulin in amyloid fibrils. Kidney Int 2000;57:349–50
- Esposito G, Michelutti R, Verdone G, Viglino P, Hernández H, Robinson CV, Amoresano A, et al. Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci 2000;9:831–45
- Güntert P, Mumenthaler C, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 1997;273:28398
- Uji Y, Motomiya Y, Ando Y. A circulating β2-microglobulin intermediate in hemodialysis patients. Nephron Clin Pract 2009;111:c173–81
- Heegaard NH, Sen JW, Nissen MH. Congophilicity (Congo red affinity) of different β2-microglobulin conformations characterized by dye affinity capillary electrophoresis. J Chromatogr A 2000;894:319–27
- Carson M, Johnson DH, McDonald H, Brouillette C, Delucas LJ. His-tag impact on structure. Acta Crystallogr D Biol Crystallogr 2007;63:295–301
- Borysik AJ, Morten IJ, Radford SE, Hewitt EW. Specific glycosaminoglycans promote unseeded amyloid formation from β2-microglobulin under physiological conditions. Kidney Int 2007;72:174–81
- Gejyo F, Odani S, Yamada T, Honma N, Saito H, Suzuki Y, Nakagawa Y, et al. β2-Microglobulin: a new form of amyloid protein associated with chronic hemodialysis. Kidney Int 1986;30:385–90
- Linke RP, Hampl H, Bartel-Schwarze S, Eulitz M. β2-Microglobulin, different fragments and polymers thereof in synovial amyloid in long-term hemodialysis. Biol Chem Hoppe Seyler 1987;368:137–44
- Heegaard NH. β2-Microglobulin: from physiology to amyloidosis. Amyloid 2009;16:151–73
- Stoppini M, Mangione P, Monti M, Giorgetti S, Marchese L, Arcidiaco P, Verga L, et al. Proteomics of β2-microglobulin amyloid fibrils. Biochim Biophys Acta 2005;1753:23–33
- Naiki H, Hashimoto N, Suzuki S, Kimura, H, Nakakuki K, Gejyo F. Establishment of a kinetic-model of dialysis-related amyloid fibril extension in-vitro. Amyloid 1997;4:223–32
- Domanska K, Vanderhaegen S, Srinivasan V, Pardon E, Dupeux F, Marquez JA, Giorgetti S, et al. Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic β2-microglobulin variant. Proc Natl Acad Sci USA 2011;108:1314–19
- Lakey JH, Raggett EM. Measuring protein-protein interactions. Curr Opin Struct Biol 1998;8:119–23
- Campbell CT, Kim G. SPR microscopy and its applications to high-throughput analyses of biomolecular binding events and their kinetics. Biomaterials 2007;28:2380–92
- Giorgetti S, Rossi A, Mangione P, Raimondi S, Marini S, Stoppini M, Corazza A, et al. β2-Microglobulin isoforms display an heterogeneous affinity for type I collagen. Protein Sci 2005;14:696–702
- McParland VJ, Kad NM, Kalverda AP, Brown A, Kirwin-Jones P, Hunter MG, Sunde M, et al. Partially unfolded states of β2-microglobulin and amyloid formation in vitro. Biochemistry 2000;39:8735–46
- Rennella E, Cutuil T, Schanda P, Ayala I, Gabel F, Forge V, Corazza A, et al. Oligomeric states along the folding pathways of β2-microglobulin: kinetics, thermodynamics, and structure. J Mol Biol 2013;425:2722–36
- Eichner T, Radford SE. Understanding the complex mechanisms of β2-microglobulin amyloid assembly. FEBS J 2011;278:3868–83