| Reaction Details |
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 | Report a problem with these data |
| Target | Membrane primary amine oxidase |
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| Ligand | BDBM50341613 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_742890 (CHEMBL1769940) |
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| IC50 | 280±n/a nM |
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| Citation |  Nurminen, EM; Pihlavisto, M; Lázár, L; Pentikäinen, U; Fülöp, F; Pentikäinen, OT Novel hydrazine molecules as tools to understand the flexibility of vascular adhesion protein-1 ligand-binding site: toward more selective inhibitors. J Med Chem54:2143-54 (2011) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Membrane primary amine oxidase |
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| Name: | Membrane primary amine oxidase |
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| Synonyms: | AOC3 | AOC3_HUMAN | Amine oxidase, copper containing | Semicarbazide-sensitive amine oxidase (SSAO) | Semicarbazide-sensitive amine oxidase/ Vascular adhesion protein 1 (SSAO/VAP-1) | VAP1 | Vascular adhesion protein 1 (VAP-1) |
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| Type: | Protein |
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| Mol. Mass.: | 84620.86 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Q16853 |
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| Residue: | 763 |
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| Sequence: | MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
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| BDBM50341613 |
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| n/a |
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| Name | BDBM50341613 |
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| Synonyms: | (1R,2S)-2-(1-Methylhydrazino)-1,2-diphenylethanol | CHEMBL1766384 |
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| Type | Small organic molecule |
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| Emp. Form. | C15H18N2O |
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| Mol. Mass. | 242.3162 |
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| SMILES | CN(N)[C@H]([C@H](O)c1ccccc1)c1ccccc1 |r| |
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| Structure | 
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