New Insights into the Pathogenesis of Hemodialysis‐Associated Amyloidosis
- 1 July 1990
- journal article
- Published by Wiley in Seminars in Dialysis
- Vol. 3 (3) , 149-151
- https://doi.org/10.1111/j.1525-139x.1990.tb00032.x
Abstract
No abstract availableThis publication has 50 references indexed in Scilit:
- Primary structure of duck amyloid protein A The form deposited in tissues may be identical to its serum precursorFEBS Letters, 1987
- Amyloid kidney stone of uremic patients consist of Beta2-microglobulin fragmentsBiochemical and Biophysical Research Communications, 1986
- Serum Levels of β2-Microglobulin as a New Form of Amyloid Protein in Patients Undergoing Long-Term HemodialysisNew England Journal of Medicine, 1986
- In vitro formation of amyloid fibrils from intact β2-microglobulinBiochemical and Biophysical Research Communications, 1985
- A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulinBiochemical and Biophysical Research Communications, 1985
- Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of jewish originBiochemical and Biophysical Research Communications, 1984
- Amyloid Deposits and AmyloidosisNew England Journal of Medicine, 1980
- N-Terminal Amino Acid Sequence of Amyloid Fibril Protein AR, Prototype of a New lamba-Variable Subgroup, VlambaVScandinavian Journal of Immunology, 1974
- Immunglobulin origin of localized nodular pulmonary amyloidosisZeitschrift für Die Gesamte Experimentelle Medizin, 1972
- An amyloid protein: The amino-terminal variable fragment of an immunoglobulin light chainBiochemical and Biophysical Research Communications, 1970