Title : The histidine composition of the amyloid-β domain, but not the E1 copper binding domain, modulates β-secretase processing of amyloid-β protein precursor in Alzheimer's disease.

Pub. Date : 2015

PMID : 25171714






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 The histidine composition of the amyloid-beta domain, but not the E1 copper binding domain, modulates beta-secretase processing of amyloid-beta protein precursor in Alzheimer"s disease. Histidine amyloid beta precursor protein Homo sapiens
2 The histidine composition of the amyloid-beta domain, but not the E1 copper binding domain, modulates beta-secretase processing of amyloid-beta protein precursor in Alzheimer"s disease. Histidine amyloid beta precursor protein Homo sapiens
3 We have investigated the role of histidine residues within the extracellular E1 copper binding and Abeta domains of AbetaPP in its proteolysis. Histidine amyloid beta precursor protein Homo sapiens
4 Mutation of histidine 14 within the Abeta-domain specifically down-regulated beta-secretase processing without impacting on non-amyloidogenic proteolysis. Histidine amyloid beta precursor protein Homo sapiens
5 Understanding how histidine 14 participates in AbetaPP proteolysis may reveal new intervention points for AD treatments. Histidine amyloid beta precursor protein Homo sapiens