Title : Aggregation state-dependent activation of the classical complement pathway by the amyloid beta peptide.

Pub. Date : 1997 Jul

PMID : 9202333






2 Functional Relationships(s)
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1 In this report, we show that the fibrillar aggregation state of A beta, as determined by thioflavin T fluorometry, electron microscopy, and staining with Congo red and thioflavine S, is precisely correlated with the ability of the peptide to induce the formation of activated fragments of the complement proteins C4 and C3. thioflavin T amyloid beta precursor protein Homo sapiens
2 In this report, we show that the fibrillar aggregation state of A beta, as determined by thioflavin T fluorometry, electron microscopy, and staining with Congo red and thioflavine S, is precisely correlated with the ability of the peptide to induce the formation of activated fragments of the complement proteins C4 and C3. thioflavin T amyloid beta precursor protein Homo sapiens