Title : Gly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics.

Pub. Date : 2014 Jun 26

PMID : 24735871






2 Functional Relationships(s)
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1 These results emphasize the importance of the Gly25-Ser26 dipeptide in organizing Abeta42 monomer structure and thus suggest that drugs altering the interactions of this dipeptide with neighboring side-chain atoms or with the peptide backbone could be useful in therapeutic strategies targeting formation of Abeta oligomers and higher-order assemblies. Dipeptides amyloid beta precursor protein Homo sapiens
2 These results emphasize the importance of the Gly25-Ser26 dipeptide in organizing Abeta42 monomer structure and thus suggest that drugs altering the interactions of this dipeptide with neighboring side-chain atoms or with the peptide backbone could be useful in therapeutic strategies targeting formation of Abeta oligomers and higher-order assemblies. Dipeptides amyloid beta precursor protein Homo sapiens