1. High level SAA expression induced amyloidosis in all mice after a short, slightly variable delay. PMID: 23959890
2. These results suggest that the carboxy terminus of SAA, which is highly conserved among SAA sequences in all vertebrates, might play important structural roles, including modulating the folding, oligomerization, misfolding, and fibrillation of SAA.(Saa2) PMID: 22448726
3. The nonpathogenic murine Saa2.2 spontaneously forms marginally stable amyloid fibrils at 37 degrees C that exhibit cross-beta structure, binding to thioflavin T, and fibrillation by a nucleation-dependent seeding mechanism. PMID: 21942925
4. The ability of SAA2.2 to form different oligomeric species in vitro along with its marginal stability, suggest that the structure of SAA might be modulated in vivo to form different biologically relevant species. PMID: 21439938
5. forms a hexamer containing a central channel in solution PMID: 12456883
6. Only liposomes containing intact SAA2.1 or its residues 1-20 or 74-103 promoted the efflux of cholesterol in vivo PMID: 12951366
7. SAA2.2 can form amyloid fibrils in vitro at physiological temperatures, which suggests that SAA2.2's inability to cause amyloidosis may be related to the stabilization of hexameric SAA2.2 and/or the slow kinetics of aberrant misfolding and self-assembly. PMID: 16194868
8. Many functional and pathological roles attributed to serum amyloid A may rely on its precarious structure, modulated by its interaction with ligands under homeostasis conditions and during the acute phase response. PMID: 17425332

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KEGG: mmu:20209

STRING: 10090.ENSMUSP00000075365

UniGene: Mm.200941