In-Depth Study of Tripeptide-Based α-Ketoheterocycles as Inhibitors of Thrombin. Effective Utilization of the S1‘ Subsite and Its Implications to Structure-Based Drug Design-Reference-Cited by-同舟云学术

In-Depth Study of Tripeptide-Based α-Ketoheterocycles as Inhibitors of Thrombin. Effective Utilization of the S1‘ Subsite and Its Implications to Structure-Based Drug Design

Published:2004-10-09 Issue:6 Volume:48 Page:1984-2008
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Costanzo Michael J.¹,Almond Harold R.¹,Hecker Leonard R.¹,Schott Mary R.¹,Yabut Stephen C.¹,Zhang Han-Cheng¹,Andrade-Gordon Patricia¹,Corcoran Thomas W.¹,Giardino Edward C.¹,Kauffman Jack A.¹,Lewis Joan M.¹,de Garavilla Lawrence¹,Haertlein Barbara J.¹,Maryanoff Bruce E.¹

Affiliation:

1. Drug Discovery, Johnson & Johnson Pharmaceutical Research & Development, Spring House, Pennsylvania 19477-0776

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm0303857

Reference93 articles.

1. The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.

2. The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited humanα-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

3. Thrombin

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