Discovery of 6-Fluoro-5-(R)-(3-(S)-(8-fluoro-1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)-2-methylphenyl)-2-(S)-(2-hydroxypropan-2-yl)-2,3,4,9-tetrahydro-1H-carbazole-8-carboxamide (BMS-986142): A Reversible Inhibitor of Bruton’s Tyrosine Kinase (BTK) Conformationally Constrained by Two Locked Atropisomers-Reference-Cited by-同舟云学术

Discovery of 6-Fluoro-5-(R)-(3-(S)-(8-fluoro-1-methyl-2,4-dioxo-1,2-dihydroquinazolin-3(4H)-yl)-2-methylphenyl)-2-(S)-(2-hydroxypropan-2-yl)-2,3,4,9-tetrahydro-1H-carbazole-8-carboxamide (BMS-986142): A Reversible Inhibitor of Bruton’s Tyrosine Kinase (BTK) Conformationally Constrained by Two Locked Atropisomers

Published:2016-09-19 Issue:19 Volume:59 Page:9173-9200
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Watterson Scott H.¹,De Lucca George V.¹,Shi Qing¹,Langevine Charles M.¹,Liu Qingjie¹,Batt Douglas G.¹,Beaudoin Bertrand Myra¹,Gong Hua¹,Dai Jun¹,Yip Shiuhang¹,Li Peng¹,Sun Dawn¹,Wu Dauh-Rurng¹,Wang Chunlei¹,Zhang Yingru¹,Traeger Sarah C.¹,Pattoli Mark A.¹,Skala Stacey¹,Cheng Lihong¹,Obermeier Mary T.¹,Vickery Rodney¹,Discenza Lorell N.¹,D’Arienzo Celia J.¹,Zhang Yifan¹,Heimrich Elizabeth¹,Gillooly Kathleen M.¹,Taylor Tracy L.¹,Pulicicchio Claudine¹,McIntyre Kim W.¹,Galella Michael A.¹,Tebben Andy J.¹,Muckelbauer Jodi K.¹,Chang ChiehYing¹,Rampulla Richard¹,Mathur Arvind¹,Salter-Cid Luisa¹,Barrish Joel C.¹,Carter Percy H.¹,Fura Aberra¹,Burke James R.¹,Tino Joseph A.¹

Affiliation:

1. Bristol-Myers Squibb Research and Development, P.O. Box 4000, Princeton, New Jersey 08543, United States

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.6b01088

Reference49 articles.

1. Bruton’s tyrosine kinase (Btk): function, regulation, and transformation with special emphasis on the PH domain

2. Signalling of Bruton's Tyrosine Kinase, Btk

3. A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma 2.