Reaction Details |
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Target | Histone deacetylase 8 |
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Ligand | BDBM50595953 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_2218705 (CHEMBL5132039) |
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IC50 | 281±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 |
Synonyms: | HD8 | HDAC8 | HDAC8_HUMAN | HDACL1 | Histone deacetylase 8 (HDAC-8) | Human HDAC8 |
Type: | Enzyme |
Mol. Mass.: | 41749.60 |
Organism: | Homo sapiens (Human) |
Description: | Q9BY41 |
Residue: | 377 |
Sequence: | MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPK
VASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATI
TAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLH
HGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKY
YQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI
LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPH
RIQQILNYIKGNLKHVV
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BDBM50595953 |
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n/a |
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Name | BDBM50595953 |
Synonyms: | CHEMBL5193014 |
Type | Small organic molecule |
Emp. Form. | C17H17FN2O4S |
Mol. Mass. | 364.391 |
SMILES | ONC(=O)c1ccc(CN(C2CC2)S(=O)(=O)c2ccc(F)cc2)cc1 |
Structure |
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