| Reaction Details |
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 | Report a problem with these data |
| Target | Histone deacetylase 8 |
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| Ligand | BDBM50595954 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_2218705 (CHEMBL5132039) |
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| IC50 | 273±n/a nM |
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| Citation |  Toutah, K; Nawar, N; Timonen, S; Sorger, H; Raouf, YS; Bukhari, S; von Jan, J; Ianevski, A; Gawel, JM; Olaoye, OO; Geletu, M; Abdeldayem, A; Israelian, J; Radu, TB; Sedighi, A; Bhatti, MN; Hassan, MM; Manaswiyoungkul, P; Shouksmith, AE; Neubauer, HA; de Araujo, ED; Aittokallio, T; Krämer, OH; Moriggl, R; Mustjoki, S; Herling, M; Gunning, PT Development of HDAC Inhibitors Exhibiting Therapeutic Potential in T-Cell Prolymphocytic Leukemia. J Med Chem64:8486-8509 (2021) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Histone deacetylase 8 |
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| Name: | Histone deacetylase 8 |
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| Synonyms: | HD8 | HDAC8 | HDAC8_HUMAN | HDACL1 | Histone deacetylase 8 (HDAC-8) | Human HDAC8 |
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| Type: | Enzyme |
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| Mol. Mass.: | 41749.60 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Q9BY41 |
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| Residue: | 377 |
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| Sequence: | MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPK
VASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATI
TAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLH
HGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKY
YQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI
LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPH
RIQQILNYIKGNLKHVV
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| BDBM50595954 |
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| n/a |
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| Name | BDBM50595954 |
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| Synonyms: | CHEMBL5201529 |
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| Type | Small organic molecule |
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| Emp. Form. | C17H15F3N2O4S |
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| Mol. Mass. | 400.372 |
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| SMILES | ONC(=O)c1ccc(CN(C2CC2)S(=O)(=O)c2cc(F)c(F)c(F)c2)cc1 |
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| Structure | 
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