X-ray Structure of Citrate Bound to Src SH2 Leads to a High-Affinity, Bone-Targeted Src SH2 Inhibitor-Reference-Cited by-同舟云学术

X-ray Structure of Citrate Bound to Src SH2 Leads to a High-Affinity, Bone-Targeted Src SH2 Inhibitor

Published:2001-02-06 Issue:5 Volume:44 Page:660-663
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Bohacek Regine S.¹,Dalgarno David C.¹,Hatada Marcos¹,Jacobsen Virginia A.¹,Lynch Berkley A.¹,Macek Karina J.¹,Merry Taylor¹,Metcalf Chester A.¹,Narula Surinder S.¹,Sawyer Tomi K.¹,Shakespeare William C.¹,Violette Shelia M.¹,Weigele Manfred¹

Affiliation:

1. ARIAD Pharmaceuticals, Inc., 26 Landsdowne Street, Cambridge, Massachusetts 02139-4234

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm0002681

Reference14 articles.

1. Knockouts of Src-family kinases: stiff bones, wimpy T cells, and bad memories.

2. A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo

3. Rescue of osteoclast function by transgenic expression of kinase-deficient Src insrc−/− mutant mice

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