Pub. Date : 2017 Mar 3
PMID : 28096459
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | We found that Zn2+ induces APP-C99 dimerization, which prevents its cleavage by gamma-secretase and Abeta production, with an IC50 value of 15 mum Importantly, at this concentration, Zn2+ also drastically raised the production of the aggregation-prone Abeta43 found in the senile plaques of AD brains and elevated the Abeta43:Abeta40 ratio, a promising biomarker for neurotoxicity and AD. | Zinc | amyloid beta precursor protein | Homo sapiens |
2 | We found that Zn2+ induces APP-C99 dimerization, which prevents its cleavage by gamma-secretase and Abeta production, with an IC50 value of 15 mum Importantly, at this concentration, Zn2+ also drastically raised the production of the aggregation-prone Abeta43 found in the senile plaques of AD brains and elevated the Abeta43:Abeta40 ratio, a promising biomarker for neurotoxicity and AD. | Zinc | amyloid beta precursor protein | Homo sapiens |
3 | We further demonstrate that the APP-C99 histidine residues His-6, His-13, and His-14 control the Zn2+-dependent APP-C99 dimerization and inhibition of Abeta production, whereas the increased Abeta43:Abeta40 ratio is substrate dimerization-independent and involves the known Zn2+ binding lysine Lys-28 residue that orientates the APP-C99 transmembrane domain within the lipid bilayer. | Zinc | amyloid beta precursor protein | Homo sapiens |
4 | We further demonstrate that the APP-C99 histidine residues His-6, His-13, and His-14 control the Zn2+-dependent APP-C99 dimerization and inhibition of Abeta production, whereas the increased Abeta43:Abeta40 ratio is substrate dimerization-independent and involves the known Zn2+ binding lysine Lys-28 residue that orientates the APP-C99 transmembrane domain within the lipid bilayer. | Zinc | amyloid beta precursor protein | Homo sapiens |