ArticleGlycoconjugate journal2001
Glycosylated molecular variants of C-reactive proteins from the major carp Catla catla in fresh and polluted aquatic environments.
Article in Glycoconjugate journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- C-Reactive Protein: Friend or Foe? Phylogeny From Heavy Metals to Modified Lipoproteins and SARS-CoV-2.Frontiers in cardiovascular medicine · 2022Review
- Evolution of C-Reactive Protein.Frontiers in immunology · 2019Review
- C-reactive protein and the biology of disease.Immunologic research · 2013Review
- Disease-associated glycosylated molecular variants of human C-reactive protein activate complement-mediated hemolysis of erythrocytes in tuberculosis and Indian visceral leishmaniasis.Glycoconjugate journal · 2009Article
- Variations in binding characteristics of glycosylated human C-reactive proteins in different pathological conditions.Glycoconjugate journal · 2004Article
- Induction of glycosylation in human C-reactive protein under different pathological conditions.The Biochemical journal · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elevated level of pollutant specific glycosylated molecular variants of C-reactive protein have been purified to electrophoretic homogeneity from the sera of major carp, Catla catla confined in freshwater (CRP(N)) and water polluted with nonlethal doses of cadmium (CRP(Cd)), mercury (CRP(Hg)), phenol (CRP(Ph)) and hexachlorocyclohexane (CRP(Hex)). These CRPs differ amongst themselves in electrophoretic mobility, and in their carbohydrate content ranging from 20-50%. CRPs interact with pneumococcal C-polysaccharide (CPS) showing different binding constants. Both phosphorylcholine (PC) and calcium are indispensable for binding. Studies on amino acid compositions, electrophoretic analysis, isoelectric focusing, binding to PC & CPS and secondary structures of the purified CRPs indicate, that, they differ from each other. However, they share the common properties of a CRP, including pentraxin structure revealed by electron microscopy. Taken together, our results provide a new structural insight regarding the connection between the presence of unique molecular variants and probably the toxicity therein combated.
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Registered trials
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