Reaction Details |
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Target | Beta-secretase 1 |
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Ligand | BDBM50231951 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_799824 (CHEMBL1941530) |
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IC50 | 4600±n/a nM |
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Citation | Bolognesi, ML; Chiriano, G; Bartolini, M; Mancini, F; Bottegoni, G; Maestri, V; Czvitkovich, S; Windisch, M; Cavalli, A; Minarini, A; Rosini, M; Tumiatti, V; Andrisano, V; Melchiorre, C Synthesis of monomeric derivatives to probe memoquin's bivalent interactions. J Med Chem54:8299-304 (2011) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Beta-secretase 1 |
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Name: | Beta-secretase 1 |
Synonyms: | ASP2 | Asp 2 | Aspartyl protease 2 | BACE | BACE1 | BACE1_HUMAN | Beta-secretase (BACE) | Beta-secretase 1 | Beta-secretase 1 (BACE 1) | Beta-secretase 1 (BACE-1) | Beta-secretase 1 (BACE1) | Beta-site APP cleaving enzyme 1 | Beta-site amyloid precursor protein cleaving enzyme 1 | KIAA1149 | Memapsin-2 | Membrane-associated aspartic protease 2 | beta-Secretase (BACE-1) | beta-Secretase (BACE1) |
Type: | Protein |
Mol. Mass.: | 55755.10 |
Organism: | Homo sapiens (Human) |
Description: | P56817 |
Residue: | 501 |
Sequence: | MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSF
VEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSST
YRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGIL
GLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGI
DHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKK
VFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRIT
ILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSAC
HVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQW
RCLRCLRQQHDDFADDISLLK
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BDBM50231951 |
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n/a |
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Name | BDBM50231951 |
Synonyms: | 2,5-bis(6-((2-methoxybenzyl)(ethyl)amino)hexylamino)cyclohexa-2,5-diene-1,4-dione | 2,5-bis(6-(ethyl(2-methoxybenzyl)amino)hexylamino)cyclohexa-2,5-diene-1,4-dione | CHEMBL231160 | memoquin |
Type | Small organic molecule |
Emp. Form. | C38H56N4O4 |
Mol. Mass. | 632.8756 |
SMILES | CCN(CCCCCCNc1cc(O)c(cc1O)N=CCCCCCN(CC)Cc1ccccc1OC)Cc1ccccc1OC |w:18.18| |
Structure |
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