Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Chiehying Y, Chang"'
Autor:
Mian Gao, David J. Shuster, Hai-Yun Xiao, Christine B. Goldstine, Jing Chen, Zhonghui Lu, Victor R. Guarino, Khehyong Ngu, Lisa M. Kopcho, Deepa Calambur, Kurt R. Gregor, Andrew J. Tebben, Jingwu Duan, Luisa Salter-Cid, Hao Lu, Joseph A. Tino, Ning Li, John Hynes, James R. Burke, Joseph Yanchunas, John E. Macor, Steven Sheriff, Dauh-Rurng Wu, Bin Jiang, Patrick J. Shaw, ChiehYing Y. Chang, Jenny Xie, Vojkan Susulic, T. G. Murali Dhar
Publikováno v:
Journal of Medicinal Chemistry. 63:15050-15071
Scaffold hopping and structure-based drug design were employed to identify substituted 4-aminoquinolines and 4-aminonaphthyridines as potent, small molecule inhibitors of tumor necrosis factor alpha (TNFα). Structure-activity relationships in both t
Autor:
John S. Sack, Dianlin Xie, Andrew J. Tebben, James R. Burke, Jodi K. Muckelbauer, Mian Gao, Joseph A. Tino, ChiehYing Y. Chang, Nazia Ahmed
Publikováno v:
Chemical Biology & Drug Design. 78:739-748
Bone marrow kinase in the X chromosome, a member of the Tec family of tyrosine kinases, plays a role in both monocyte/macrophage trafficking as well as cytokine secretion. Although the structures of Tec family kinases Bruton's tyrosine kinase and IL-
Autor:
Andrew J. Tebben, Wayne Vaccaro, Xiaoxia Yang, Kim W. McIntyre, Steven Sheriff, Nelly Aranibar, Dharmpal S. Dodd, Stacey Skala, Zheng Yang, Dawn K. Stetsko, Patric M Davis, Theresa Ziemba, Suzanne J. Suchard, Dominique Potin, Karishma Patel, Bang-Chi Chen, Joel C. Barrish, Zili Xiao, Albert J. DelMonte, Scott H. Watterson, Murray McKinnon, David R. Tortolani, Praveen Balimane, Pathanjali Kadiyala, Punit Marathe, Huiping Zhang, Michele Launay, Deborah Lee, ChiehYing Y. Chang, T. G. Murali Dhar
Publikováno v:
Journal of Medicinal Chemistry. 53:3814-3830
Leukocyte function-associated antigen-1 (LFA-1), also known as CD11a/CD18 or alpha(L)beta(2), belongs to the beta(2) integrin subfamily and is constitutively expressed on all leukocytes. The major ligands of LFA-1 include three intercellular adhesion
Autor:
Peiying Liu, Yax Sun, Xiaopeng Sang, Upender Velaparthi, Joan M. Carboni, Ann Greer, Dolatrai M. Vyas, Ricardo M. Attar, David R. Langley, ChiehYing Y. Chang, Stoffan Karen M, Kurt Zimmermann, Aixin Li, Balu Balasubramanian, Mark D. Wittman, John S. Sack, Bruce L. Jacobsen, Marco M. Gottardis
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 17:2317-2321
The discovery and synthesis of 3-(1H-benzo[d]imidazol-2-yl)pyridin-2(1H)-one inhibitors of insulin-like growth factor 1-receptor (IGF-1R) are presented. Installing amine containing side chains at the 4-position of pyridone ring significantly improved
Autor:
Joseph J. Villafranca, Bruce L. Jacobson, John J. Emanuele, Chiehying Y. Chang, Howard Einspahr, Haiyong Jin
Publikováno v:
Protein Science. 5:2566-2574
Uridine diphosphate-N-acetylmuramate:L-alanine ligase (EC 6.3.2.8, UNAM:L-Ala ligase or MurC gene product) catalyzes the ATP-dependent ligation of the first amino acid to the sugar moiety of the peptidoglycan precursor. This is an essential step in c
Publikováno v:
Journal of Molecular Biology. 259:938-946
The X-ray structure of the uncomplexed human chimeric Fab′ of the anti-tumor antibody BR96 has been determined at 2.6 A resolution. The structure has been compared with Lewis Y antigen-complexed structures of BR96 which were determined previously.
Autor:
Jagabandhu Das, Daniel G.M. Roberts, ChiehYing Y. Chang, Lydia Tabernero, Mary F. Malley, S. L. Ohringer, John S. Sack
Publikováno v:
Protein Science. 5:221-228
The crystallographic structures of the ternary complexes of human alpha-thrombin with hirugen (a sulfated hirudin fragment) and the small-molecule active site thrombin inhibitors BMS-186282 and BMS-189090 have been determined at 2.6 and 2.8 A. In bot
Autor:
ChiehYing Y. Chang, Steven Sheriff, Patricia Bossart-Whitaker, Jiri Novotny, David C. Benjamin
Publikováno v:
Journal of Molecular Biology. 253:559-575
The three-dimensional structure of the antibody N10 Fab fragment complexed with staphylococcal nuclease (SNase) has been determined to 2.9 A resolution. Eighteen residues from six complementarity-determining regions (CDR) recognize an epitope of five
Autor:
Steven M. Seiler, Daniel G.M. Roberts, John S. Sack, Tammy C. Wang, ChiehYing Y. Chang, Edwin J. Iwanowicz, S. L. Ohringer, Wan F. Lau, Wen-Ching Han, Lydia Tabernero
Publikováno v:
Journal of Molecular Biology. 246:14-20
The crystallographic structure of the ternary complex between human alpha-thrombin, hirugen and the peptidyl inhibitor Phe-alloThr-Phe-O-CH3, which is acylated at its N terminus with 4-guanidino butanoic acid (BMS-183507), has been determined at 2.6
Autor:
Philip D. Jeffrey, ChiehYing Y. Chang, Joel F. Schildbach, Steven Sheriff, Michael N. Margolies, P. H. Kussie
Publikováno v:
Journal of Molecular Biology. 248:344-360
We determined the sequence, specificity for structurally related cardenolides, and three-dimensional structure of the anti-digoxin antibody 40-50 Fab in complex with ouabain. The 40-50 antibody does not share close sequence homology with other high-a