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Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations.
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Antigenicity and cross-reactivity of denatured fibril proteins of primary, secondary, and myeloma associated amyloids.
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Tissue-based diagnosis of systemic amyloidosis: Experience of the informal diagnostic center at Uppsala University Hospital.
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Phage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitope.
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Antibody-mediated resolution of light chain-associated amyloid deposits.
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Serum amyloid A (SAA) in viral infection: rubella, measles and subacute sclerosing panencephalitis (SSPE).
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[Electron microscopic studies of neutrophils during phagocytosis of amyloid fibrils in the mouse].
Blut. 1971 Jul;23(1):14-20. doi: 10.1007/BF01815129.
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Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations.
J Exp Med. 1969 Oct 1;130(4):777-96. doi: 10.1084/jem.130.4.777.
8
Individual antigenic specificity and cross-reactions among amyloid preparations from different individuals.
Clin Exp Immunol. 1972 Apr;10(4):635-47.
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Detection of a specific antigen of amyloid fibrils in mice.
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Immunological characterization of amyloid fibrils in tissue sections.
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The localization of in vivo bound complement in tissue section.
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Immunohistochemical analysis of amyloid by the fluorescence technique.
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High-resolution electron microscopic analysis of the amyloid fibril.
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Amyloid. VI. A comparison of two morphologic components of human amyloid deposits.
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The characterization of soluble amyloid prepared in water.
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Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations.
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Studies on antigenic composition of amyloid.
J Immunol. 1966 Feb;96(2):245-52.
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Amyloid. IV. Is human amyloid immunogenic?
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High specific activity labeling of protein with I-131 by the iodine monochloride method.
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Plasma protein constituents of amyloid fibrils.
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