ArticleAnnals of the rheumatic diseases1991
High molecular weight glycosaminoglycans in AA type amyloid fibril extracts from human liver.
Article in Annals of the rheumatic diseases, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 14 citations in OpenAlex.
- On the association between amyloid fibrils and glycosaminoglycans; possible interactive role of Ca2+ and amyloid P-component.Clinical and experimental immunology · 1993Article
- Isolation and partial characterization of heparan sulphate proteoglycans from human hepatic amyloid.The Biochemical journal · 1992Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Glycosaminoglycans have previously been identified in extracts of AA type hepatic amyloid fibril from a patient with amyloidosis associated with juvenile rheumatoid arthritis. The macromolecular properties of these polysaccharides are described here in more detail. By gel filtration and ion exchange chromatography glycosaminoglycans in the form of high molecular weight free chains were shown to coisolate with water extracted amyloid fibrils. About 60% of these were characterised as galactosamines (chondroitin sulphate/dermatan sulphate), whereas the remaining 40% consisted of N-sulphated glucosamines (heparin/heparan sulphate). The amyloid associated glycosaminoglycans were not part of intact proteoglycans in the fibril extracts.
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