Immunohistochemical detection of advanced glycation end products in dialysis-related amyloidosis

This publication has 23 references indexed in Scilit:

• Involvement of beta 2-microglobulin modified with advanced glycation end products in the pathogenesis of hemodialysis-associated amyloidosis. Induction of human monocyte chemotaxis and macrophage secretion of tumor necrosis factor-alpha and interleukin-1.
  Journal of Clinical Investigation, 1994
• beta 2-Microglobulin modified with advanced glycation end products is a major component of hemodialysis-associated amyloidosis.
  Journal of Clinical Investigation, 1993
• Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.
  Proceedings of the National Academy of Sciences, 1986
• β2-microglobulin: A new form of amyloid protein associated with chronic hemodialysis
  Kidney International, 1986
• Serum Levels of β₂-Microglobulin as a New Form of Amyloid Protein in Patients Undergoing Long-Term Hemodialysis
  New England Journal of Medicine, 1986
• Beta-2 microglobulin is an amyloidogenic protein in man.
  Journal of Clinical Investigation, 1985
• High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules.
  Proceedings of the National Academy of Sciences, 1985
• A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin
  Biochemical and Biophysical Research Communications, 1985
• Nonenzymatic Glycosylation and the Pathogenesis of Diabetic Complications
  Annals of Internal Medicine, 1984
• Accelerated age-related browning of human collagen in diabetes mellitus.
  Proceedings of the National Academy of Sciences, 1984