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Literature summary for 3.4.23.46 extracted from

  • Hamada, Y.; Suzuki, K.; Nakanishi, T.; Sarma, D.; Ohta, H.; Yamaguchi, R.; Yamasaki, M.; Hidaka, K.; Ishiura, S.; Kiso, Y.
    Structure-activity relationship study of BACE1 inhibitors possessing a chelidonic or 2,6-pyridinedicarboxylic scaffold at the P(2) position (2014), Bioorg. Med. Chem. Lett., 24, 618-623.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with inhibitor 6-[(3R,4S)-3-benzyl-4-hydroxy-5-oxo-5-[[3-(2H-tetrazol-5-yl)phenyl]amino]pentanoyl]-N-[(1R)-1-(4-fluorophenyl)ethyl]-4-oxo-4H-pyran-2-carboxamide. The P3 benzene ring tightly occupies the S3 sub-pocket of BACE1. Particularly, the fluorine atom of the compound seems to interact with the side chains of the hydrophobic amino acids Ala335 and Tyr14 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
6-[(3R,4S)-3-benzyl-4-hydroxy-5-oxo-5-[[3-(2H-tetrazol-5-yl)phenyl]amino]pentanoyl]-N-[(1R)-1-(4-fluorophenyl)ethyl]-4-oxo-4H-pyran-2-carboxamide 76% inhibition at 2 microM Homo sapiens
additional information BACE1 inhibitors possessing a chelidonic or 2,6-pyridinedicarboxylic scaffold at the P2 position. Small-sized and hydrophobic residues at the P2 and P3 positions are preferable for BACE1 inhibition. The membrane permeability of these non-peptidic BACE1 inhibitors is similar to that of peptidic compounds Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P56817
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