General Information:

Id: 3,792 (click here to show other Interactions for entry)
Diseases: Alzheimer disease - [OMIM]
Mammalia
review
Reference: Srikanth V et al.(2011) Advanced glycation endproducts and their receptor RAGE in Alzheimers disease Neurobiol. Aging 32: 763-777 [PMID: 19464758]

Interaction Information:

Comment The formation of AGEs is accelerated by transition metals, such as copper and iron, which oxidize the protein-bound Amadori products or the monosaccharides directly in solution.
Formal Description
Interaction-ID: 37471

drug/chemical compound

Iron

increases_quantity of

drug/chemical compound

Advanced glycation end-product

Comment Formation of covalently crosslinked high molecular weight Abeta oligomers is accelerated by micromolar amounts of copper (Cu+, Cu2+) and iron (Fe2+, Fe3+) ions.
Formal Description
Interaction-ID: 37642

drug/chemical compound

Fe2+

increases_quantity of

complex/PPI

Amyloid beta peptide (oligomer)

The formation of covalently crosslinked high molecular weight Abeta oligomers is accelerated
Comment Formation of covalently crosslinked high molecular weight Abeta oligomers is accelerated by micromolar amounts of copper (Cu+, Cu2+) and iron (Fe2+, Fe3+) ions.
Formal Description
Interaction-ID: 37643

drug/chemical compound

Fe3+

increases_quantity of

complex/PPI

Amyloid beta peptide (oligomer)

The formation of covalently crosslinked high molecular weight Abeta oligomers is accelerated