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Literature summary for 1.2.1.12 extracted from

  • Naletova, I.; Schmalhausen, E.; Kharitonov, A.; Katrukha, A.; Saso, L.; Caprioli, A.; Muronetz, V.
    Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures (2008), Biochim. Biophys. Acta, 1784, 2052-2058.
    View publication on PubMed

Application

Application Comment Organism
medicine non-native forms of GAPDH may be involved in the formation of amyloid structures during Alzheimer's disease, binding to soluble amyloid-beta peptide Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
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Oryctolagus cuniculus
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Subunits

Subunits Comment Organism
More non-native forms of GAPDH obtained by cold denaturation, oxidation of the enzyme, or its unfolding in guanidine hydrochloride efficiently bind to soluble amyloid-beta peptide (1-42) yielding a stable complex. Native tetrameric GAPDH does not interact with soluble amyloid-beta peptide (1-42), neither non-native forms of GAPDH interact with aggregated amyloid-beta peptide (1-42) Oryctolagus cuniculus