BETA-2-MICROGLOBULIN AMYLOIDOSIS - AN OVERVIEW

[81] Dinarello CHA, Cannon JG, Wolff SHM, Bernheim HA, Beutler B, Cerami A, Figari IS, Palladino MA, O'Connor JV, Tumor necrosis factor (Cachectin) is an endogenous pyrogen and induces production of interleukin 1, J Exp Med, 163, pp. 1433-1450, (1986)

[82] Tielmans C, Dratwa M, Bergmann P, Goldman M, Flamion B, Collart F, Wens R, Continuous ambulatory peritoneal dialysis, protective against developing dialysis‐associated amyloid, Nephron, 53, pp. 174-175, (1989)

[83] Cornellis F, Bardin T, Zingraff J, Drueke T, β ₂‐Microglobulin amyloidosis and peritoneal dialysis, Dialysis Amyloidosis, pp. 119-122, (1989)

[84] Becker JW, Reeke GN, Three‐dimensional structures of β₂‐microglobulin, Proc Natl Acad Sci USA, 82, pp. 4225-4229, (1985)

[85] Berggard B, Bjorck L, Cigen R, Logdberg L, β ₂‐Microglobulin, Scand J Clin Lab Invest, 40, pp. 13-25, (1980)

[86] D'Urso CM, Wang Z, Cao Y, Tatake R, Zeff RA, Ferrone S, Lack of HLA class I antigen expression by cultured melanoma cells FO‐1 due to a defect in β₂‐M gene expression, J Clin Invest, 87, pp. 284-292, (1991)

[87] 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, 36, pp. 675-681, (1989)

[88] Connors LH, Shirahama T, Sipe JD, Skinner M, Fenves A, Cohen AS, Formation of amyloid fibrils from intact β₂‐microglobulin, Biochem Biophys Res Commun, 131, pp. 1063-1068, (1985)

[89] Campistol JM, Sole M, Bombi JA, Rodriguez R, Mirapeix E, Munoz-Gomez J, Revert, In vitro spontaneous synthesis of β₂‐microglobulin amyloid fibrils, Am J Pathol, 141, pp. 241-248, (1992)

[90] Ogawa H, Saito A, Hirabayashi N, Hara K, Amyloid deposition in systemic organs in long‐term hemodialysis patients, Clin Nephrol, 28, pp. 199-204, (1987)

[81] Dinarello CHA, Cannon JG, Wolff SHM, Bernheim HA, Beutler B, Cerami A, Figari IS, Palladino MA, O'Connor JV, Tumor necrosis factor (Cachectin) is an endogenous pyrogen and induces production of interleukin 1, J Exp Med, 163, pp. 1433-1450, (1986)

[82] Tielmans C, Dratwa M, Bergmann P, Goldman M, Flamion B, Collart F, Wens R, Continuous ambulatory peritoneal dialysis, protective against developing dialysis‐associated amyloid, Nephron, 53, pp. 174-175, (1989)

[83] Cornellis F, Bardin T, Zingraff J, Drueke T, β ₂‐Microglobulin amyloidosis and peritoneal dialysis, Dialysis Amyloidosis, pp. 119-122, (1989)

[84] Becker JW, Reeke GN, Three‐dimensional structures of β₂‐microglobulin, Proc Natl Acad Sci USA, 82, pp. 4225-4229, (1985)

[85] Berggard B, Bjorck L, Cigen R, Logdberg L, β ₂‐Microglobulin, Scand J Clin Lab Invest, 40, pp. 13-25, (1980)

[86] D'Urso CM, Wang Z, Cao Y, Tatake R, Zeff RA, Ferrone S, Lack of HLA class I antigen expression by cultured melanoma cells FO‐1 due to a defect in β₂‐M gene expression, J Clin Invest, 87, pp. 284-292, (1991)

[87] 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, 36, pp. 675-681, (1989)

[88] Connors LH, Shirahama T, Sipe JD, Skinner M, Fenves A, Cohen AS, Formation of amyloid fibrils from intact β₂‐microglobulin, Biochem Biophys Res Commun, 131, pp. 1063-1068, (1985)

[89] Campistol JM, Sole M, Bombi JA, Rodriguez R, Mirapeix E, Munoz-Gomez J, Revert, In vitro spontaneous synthesis of β₂‐microglobulin amyloid fibrils, Am J Pathol, 141, pp. 241-248, (1992)

[90] Ogawa H, Saito A, Hirabayashi N, Hara K, Amyloid deposition in systemic organs in long‐term hemodialysis patients, Clin Nephrol, 28, pp. 199-204, (1987)