Amyloid precursor proteins form ordered fibrils

Stable Identifier
R-HSA-977136
Type
Reaction [Polymerisation]
Species
Homo sapiens
Compartment
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Amyloid fibril formation is associated with a wide range of diseases (Chiti & Dobson 2006), though the accumulation and deposition of fibrillar material does not correlate well with disease pathogenesis and it is now widely believed that oligomeric amyloid forms are largely responsible for the cytotoxic effects of amyloid (Glabe 2009). Fibrils have been described as more like crystalline polymer structures than the protein monomers they are derived from (Wetzel et al. 2007). In vitro, fibril formation is usually preceded by the association of monomers into oligomeric structures (Kodali & Wetzel 2007), though this remains to be established in vivo. Amyloid-beta forms spherical structures with around 12 units (Bernstein et al. 2005). Larger structures called protofibrils are also observed, non-spherical filamentous structures lacking a periodic substructure (Goldsbury 2005).

Literature References
PubMed ID Title Journal Year
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Proc Natl Acad Sci U S A 1994
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Kidney Int 2008
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Biochem Biophys Res Commun 2001
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Amyloid 2008
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J Lab Clin Med 2005
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Nature 1999
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Nature 1993
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Lancet 1988
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J Immunol 1976
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Proc Natl Acad Sci U S A 1990
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Proc Natl Acad Sci U S A 1987
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Nat Genet 1997
Participants
Participant Of
Disease
Name Identifier Synonyms
Amyloidosis 9120
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