Search results for ASL

Showing 5 results out of 5

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Species

Types

Compartments

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Protein (2 results from a total of 2)

ASL

Identifier: R-HSA-70570
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: ASL: P04424
Identifier: R-HSA-62504
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: ADSL: P30566

Complex (1 results from a total of 1)

Identifier: R-HSA-70571
Species: Homo sapiens
Compartment: cytosol

Reaction (2 results from a total of 2)

Identifier: R-HSA-977136
Species: Homo sapiens
Compartment: extracellular region
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).
Identifier: R-HSA-70573
Species: Homo sapiens
Compartment: cytosol
Cytosolic argininosuccinate lyase (ASL) catalyzes the reversible reaction of argininosuccinate to form fumarate and arginine. The enzyme is a homotetramer (Turner et al. 1997). The function of the human enzyme in vivo is inferred from the defective argininosuccinate lyase enzyme activity observed in patients with mutant forms of the ASL gene (e.g., Walker et al. 1990).
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