Title : Yeast cell adhesion molecules have functional amyloid-forming sequences.

Pub. Date : 2010 Mar

PMID : 20038605






3 Functional Relationships(s)
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1 As examples of the amyloid-forming ability of the native proteins, soluble glycosylphosphatidylinositol (GPI)-less fragments of C. albicans Als5p and S. cerevisiae Muc1p also formed amyloids within a few days under native conditions at nM concentrations. Glycosylphosphatidylinositols Flo11p Saccharomyces cerevisiae S288C
2 As examples of the amyloid-forming ability of the native proteins, soluble glycosylphosphatidylinositol (GPI)-less fragments of C. albicans Als5p and S. cerevisiae Muc1p also formed amyloids within a few days under native conditions at nM concentrations. Glycosylphosphatidylinositols Flo11p Saccharomyces cerevisiae S288C
3 There was also evidence of amyloid formation in vivo: the surfaces of cells expressing wall-bound Als1p, Als5p, Muc1p, or Flo1p were birefringent and bound the fluorescent amyloid-reporting dye thioflavin T. thioflavin T Flo11p Saccharomyces cerevisiae S288C