Proteins forming amyloids in diseases
To date, 37 human proteins have been found to form amyloid in pathology and be associated with well-defined diseases. The International Society of Amyloidosis classifies amyloid fibrils and their associated diseases based upon associated proteins (for example ATTR is the group of diseases and associated fibrils formed by TTR). A table is included below. Non-disease and functional amyloids
Many examples of non-pathological amyloid with a well-defined physiological role have been identified in various organisms, including human. These may be termed as functional or physiological or native amyloid. Functional amyloid in Homo sapiens:
Intralumenal domain of melanocyte protein PMEL
Peptide/protein hormones stored as amyloids within endocrine secretory granules
Receptor-interacting serine/threonine-protein kinase 1/3 (RIP1/RIP3)
Fragments of prostatic acid phosphatase and semenogelinsFunctional amyloid in other organisms:
Curli fibrils produced by E. coli, Salmonella, and a few other members of the Enterobacteriales (Csg). The genetic elements (operons) encoding the curli system are phylogenetic widespread and can be found in at least four bacterial phyla. This suggest that many more bacteria may express curli fibrils. GvpA, forming the walls of particular Gas vesicles, i.e. the buoyancy organelles of aquatic archaea and eubacteria
Fap fibrils in various species of Pseudomonas
Chaplins from Streptomyces coelicolor
Spidroin from Trichonephila edulis (spider) (Spider silk)
Hydrophobins from Neurospora crassa and other fungi
Fungal cell adhesion proteins forming cell surface amyloid regions with greatly increased binding strength
Environmental biofilms according to staining with amyloid specific dyes and antibodies. Tubular sheaths encasing Methanosaeta thermophila filamentsFunctional amyloid acting as prions
Several yeast prions are based on an infectious amyloid, e.g.
The general master equation approach to amyloid fibril formation with secondary pathways has been developed by Knowles, Vendruscolo, Cohen, Michaels and coworkers and considers the time evolution of the concentration 
  
    
      
        f
        (
        t
        ,
        j
        )
      
    
    {\displaystyle f(t,j)}
   of fibrils of length 
  
    
      
        j
      
    
    {\displaystyle j}
   (here 
  
    
      
        j
      
    
    {\displaystyle j}
   represents the number of monomers in an aggregate).