Discovery of LB30057, a benzamidrazone-based selective oral thrombin inhibitor

Bioorganic and Medicinal Chemistry Letters

Volumn 8, Issue 6, 1998, Pages 631-634

  Oh, Yeong Soo ^a   Yun, Mikyung ^a   Hwang, Sang Yeul ^a   Hong, Seongwon ^a   Shin, Youseung ^a   Lee, Koo ^a   Yoon, Kyung Hee ^a   Yoo, Yung Joon ^a   Kim, Dong Soo ^a   Lee, Sun Hwa ^a   Lee, Yong Hee ^a   Park, Hee Dong ^a   Lee, Chang Ho ^a   Lee, Sang Koo ^a   Kim, Sangsoo ^a  

^a LG Chemical Ltd   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

LB 30057; THROMBIN; THROMBIN INHIBITOR; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BINDING AFFINITY; DOG; DRUG BIOAVAILABILITY; DRUG MECHANISM; DRUG SYNTHESIS; INTRAVENOUS DRUG ADMINISTRATION; NONHUMAN; ORAL DRUG ADMINISTRATION; RAT; STRUCTURE ACTIVITY RELATION; THROMBOSIS;

ANIMALS; BENZAMIDES; BIOLOGICAL AVAILABILITY; CATTLE; DISEASE MODELS, ANIMAL; DOGS; HALF-LIFE; HUMANS; MODELS, MOLECULAR; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; THROMBIN; THROMBOSIS;

ANIMALIA; BOVINAE; CANIS FAMILIARIS;

EID: 19244385909     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(98)00079-1     Document Type: Article

References (15)

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9. 5 Details of the enzyme inhibition kinetics will be published elsewhere.
10. sym = 6.5% using the Denzo package (Z. Otwinowski and W. Minor). The protein model was taken from the entry 1HGT of the Protein Data Bank (PDB) and refined using a simulated annealing protocol (Brünger, A.T.; Kuriyan, K.; Karplus, M. Science 1987, 235, 458). The inhibitor molecule was built into the subsequent difference density and the whole complex including 234 water molecules were refined to an R = 19.9%. The r.m.s. deviations of bond distances and angles from ideal values were 0.010Å and 1.9°, respectively.
11. sym = 6.5% using the Denzo package (Z. Otwinowski and W. Minor). The protein model was taken from the entry 1HGT of the Protein Data Bank (PDB) and refined using a simulated annealing protocol (Brünger, A.T.; Kuriyan, K.; Karplus, M. Science 1987, 235, 458). The inhibitor molecule was built into the subsequent difference density and the whole complex including 234 water molecules were refined to an R = 19.9%. The r.m.s. deviations of bond distances and angles from ideal values were 0.010Å and 1.9°, respectively.
12. sym = 6.5% using the Denzo package (Z. Otwinowski and W. Minor). The protein model was taken from the entry 1HGT of the Protein Data Bank (PDB) and refined using a simulated annealing protocol (Brünger, A.T.; Kuriyan, K.; Karplus, M. Science 1987, 235, 458). The inhibitor molecule was built into the subsequent difference density and the whole complex including 234 water molecules were refined to an R = 19.9%. The r.m.s. deviations of bond distances and angles from ideal values were 0.010Å and 1.9°, respectively.
13. 7. Millet, J.; Theveniaux, J.; Brown, N.L. Thromb. Haemost. 1992, 67, 176.
14. 8. Broersma, R.J.; Kutcher, L.W,; Heminger, E.F.; Thromb. Res. 1991, 64, 405.
15. 4, and the supernatant was quantitated using HPLC on a reversed-phase column at UV 231 nm.