Linked from

The 13 pages that link to Amyloid, each with the reason it gives.

• Protein foldingBroader topic: Amyloid formation is one outcome of certain protein-misfolding pathways.

• Protein denaturationRelated: Unfolded or misfolded proteins can assemble into amyloid structures linked to disease.

• Protein structureBroader topic: Amyloid demonstrates that protein chains can assemble into stable structures beyond individual folded proteins.

• PrionRelated: Many prion aggregates form amyloid fibrils that accumulate in tissue.

• Protein misfoldingBroader topic: Some misfolded proteins assemble into amyloid fibrils rather than being cleared.

• Beta sheetRelated: Misassembled beta sheets can form the core architecture of amyloid fibrils.

• Creutzfeldt–Jakob diseaseCompared with: Prion aggregates are amyloid-like, but not every amyloid disease is transmissible.

• Stanley B. PrusinerRelated: Amyloid aggregation resembles prion protein assembly, though amyloid is not necessarily infectious.

• Congo redRelated: Congo red binds amyloid deposits and produces the classic stain used to identify them.

• Transmissible spongiform encephalopathyRelated: Prion aggregates share amyloid-like structure and accumulate in affected nervous tissue.

• Aubrey de GreyRelated: Amyloid deposits illustrate the extracellular aggregates included in de Grey’s damage framework.

• Gerstmann–Sträussler–Scheinker syndromeNarrower topic: Gerstmann–Sträussler–Scheinker syndrome is notable for prion-protein amyloid plaques.

• Hyalin (pathology)Compared with: Amyloid can look hyaline on routine sections but has distinct fibrils and diagnostic staining.