Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Joseph T. Tsay"'
Autor:
Xin Chen, Poli Gregory B, Joseph T. Tsay, Jiesheng Kang, Ying Zhang, Anne Minnich, Keith Sides, Qingping Wang, Yong Mi Choi-Sledeski, Patrick Wai-Kwok Shum, Guyan Liang, Vasant Kumar
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 22:1606-1610
Tropanylamide was investigated as a possible scaffold for β-tryptase inhibitors with a basic benzylamine P1 group and a substituted thiophene P4 group. Comparing to piperidinylamide, the tropanylamide scaffold is much more rigid, which presents less
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11005196f65f43ed0cb5d4f3f5282312
https://doi.org/10.1016/j.bmcl.2011.12.127
https://doi.org/10.1016/j.bmcl.2011.12.127
Autor:
Keith Sides, James Pribish, Magali Mathieu, Sam Rebello, Gregory H. Merriman, Henry W. Pauls, Guyan Liang, Xin Chen, Julian Levell, Jennifer Cairns, Isabelle Morize, Brian Whitely, Joseph T. Tsay, Aldous Suzanne C, Sébastien Maignan
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 22:1049-1054
A solid phase combinatorial library was designed based on X-ray structures and in-silico models to explore an inducible S4+ pocket, which is formed by a simple side-chain rotation of Tyr95. This inducible S4+ pocket is unique to β-tryptase and does
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f671f9914d4892d516d5bdd70e540e8f
https://doi.org/10.1016/j.bmcl.2011.11.119
https://doi.org/10.1016/j.bmcl.2011.11.119
Autor:
William Degnen, Dasha Cabel, Jane Peppard, Ying Zhang, Roy J. Vaz, Larry R. McLean, Joseph T. Tsay, Arun Subramaniam, Chao Zou, Yi Li
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 20:1981-1984
Amino-benzoic acid derivatives 1-4 were found to be inhibitors for DHODH by virtual screening, biochemical, and X-ray crystallographic studies. X-ray structures showed that 1 and 2 bind to DHODH as predicted by virtual screening, but 3 and 4 were fou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c49cd17806183304defbfb07d986a306
https://doi.org/10.1016/j.bmcl.2010.01.115
https://doi.org/10.1016/j.bmcl.2010.01.115
Autor:
Michael Gardyan, Mathew Rose M, Jane Davidson, Joseph Romano, Alain Dupuy, Aldous Suzanne C, Jennifer Kwong, Sam S. Rebello, Jennifer Cairns, Odessa Giardino, Yongyi Luo, Sébastien Maignan, Andrew David Morley, Clive Mccarthy, Joseph T. Tsay, Darren Engers, Guyan Liang, Houille Olivier, Julian Levell, Pribish James R, Jean-Pierre Guilloteau, Garry Fenton, Simon Watson, Trevor K.P. Harrison, Peter C. Astles, Liduo Shen, Mark Czekaj, Gregory H. Merriman, Keith Sides, Pauls Henry W, Keith Smith, Jie Wang, Heng-Keang Lim, Paul R. Eastwood, Brian Whiteley
Publikováno v:
Bioorganic & Medicinal Chemistry. 13:2859-2872
Tryptase is a serine protease found almost exclusively in mast cells. It has trypsin-like specificity, favoring cleavage of substrates with an arginine (or lysine) at the P1 position, and has optimal catalytic activity at neutral pH. Current evidence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abef3005a193e13656a4c8e845e1b9b8
https://doi.org/10.1016/j.bmc.2005.02.014
https://doi.org/10.1016/j.bmc.2005.02.014
Autor:
Xin Chen, Eric W. MacMillan, Guyan Liang, Isabelle Morize, Yong Gong, Yong Mi Choi-Sledeski, Joseph T. Tsay, David J. Aldous, Berndt Kulitzscher, Jennifer Cairns, Keith Sides, Pauls Henry W
Publikováno v:
Bioorganicmedicinal chemistry letters. 22(9)
The tetrameric folding of β-tryptase and the pair-wise distribution of its substrate binding sites offer a unique opportunity for development of inhibitors that span two adjacent binding sites. A series of dimeric inhibitors with two basic P1 moieti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31394b151f2999474eaac65e9c8c912d
https://pubmed.ncbi.nlm.nih.gov/22483389
https://pubmed.ncbi.nlm.nih.gov/22483389
Autor:
Jie Wang, Qingping Wang, Roy J. Vaz, Guyan Liang, Jennifer Cairns, Keith Sides, Joseph T. Tsay, Zhicheng Zhao, Gregory T Stoklosa, Yong Mi Choi-Sledeski, Patrick Wai-Kwok Shum, Xin Chen, Anne Minnich, Gregory B. Poli, Thaddeus R. Nieduzak
Publikováno v:
Bioorganicmedicinal chemistry letters. 20(22)
A novel β-tryptase inhibitor with a basic benzylamine P1 group, a piperidine-amide linker, and a substituted indole P4 group was discovered. A substitution at 4-indole position was introduced to constrain the conformational flexibility of the inhibi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5de7864d6da9350249661c5c64ee07b6
https://pubmed.ncbi.nlm.nih.gov/20855210
https://pubmed.ncbi.nlm.nih.gov/20855210
Autor:
Roy J. Vaz, Larry R. McLean, Ying Zhang, Hua Li, Yi Li, Joy Prisco, Ziyu Li, Choi Yong-Mi, Joseph T. Tsay, Zuoning Han, Stephan Reiling, Ulrike Lukasczyk, Jeremy Fordham
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(23)
Biochemical and X-ray crystallographic studies confirmed that hydroxyquinoline derivatives identified by virtual screening were actually covalent inhibitors of the MIF tautomerase. Adducts were formed by N-alkylation of the Pro-1 at the catalytic sit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbd383e8d558cc5b0cf5ee20754de94e
https://pubmed.ncbi.nlm.nih.gov/19836948
https://pubmed.ncbi.nlm.nih.gov/19836948
Autor:
Guyan Liang, Xin Chen, Gregory B. Poli, Qingping Wang, Yong Mi Choi-Sledeski, Roy J. Vaz, Joseph T. Tsay, Anne Minnich, Keith Sides
Publikováno v:
MedChemComm. 2:794
A β-tryptase inhibitor with a basic benzylamine P1 group, a substituted indole P4 group, and a spiro-piperidineamide scaffold linker was designed, synthesized, and tested for its β-tryptase potency and ADMET properties. Comparing to its non-spiro a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a756fce5d94f38069ed857e17eefa56c
https://doi.org/10.1039/c1md00104c
https://doi.org/10.1039/c1md00104c