Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Binyuan, Sun"'
Autor:
Prasanthi Geda, Mark A. McCoy, Liping Yang, Chaomin Li, Armetta D. Hill, Xavier Fradera, Marianne L. Spatz, Matthew Ernst Voss, Carolyn Michele Cammarano, Pierre Daublain, Xiao Wang, Christopher F. Thompson, B. Wesley Trotter, C. Gary Marshall, Michael H. Reutershan, Peter Goldenblatt, Latha G. Nair, Manami Shizuka, Tammie C. Yeh, John G. Cryan, Isabelle Dussault, Michelle Martinez, Mingmei Cai, Raymond A. Kemper, Binyuan Sun, Michelle R. Machacek, Dietrich Steinhuebel, Giovanna Scapin, Michael D. Altman, Stephane L. Bogen, Matthew Christopher, Dapeng Chen, Victoria Kutilek, Weidong Pan
Publikováno v:
Journal of Medicinal Chemistry. 64:16213-16241
Identification of low-dose, low-molecular-weight, drug-like inhibitors of protein-protein interactions (PPIs) is a challenging area of research. Despite the challenges, the therapeutic potential of PPI inhibition has driven significant efforts toward
Autor:
Michael H, Reutershan, Michelle R, Machacek, Michael D, Altman, Stephane, Bogen, Mingmei, Cai, Carolyn, Cammarano, Dapeng, Chen, Matthew, Christopher, John, Cryan, Pierre, Daublain, Xavier, Fradera, Prasanthi, Geda, Peter, Goldenblatt, Armetta D, Hill, Raymond A, Kemper, Victoria, Kutilek, Chaomin, Li, Michelle, Martinez, Mark, McCoy, Latha, Nair, Weidong, Pan, Christopher F, Thompson, Giovanna, Scapin, Manami, Shizuka, Marianne L, Spatz, Dietrich, Steinhuebel, Binyuan, Sun, Matthew E, Voss, Xiao, Wang, Liping, Yang, Tammie C, Yeh, Isabelle, Dussault, C Gary, Marshall, B Wesley, Trotter
Publikováno v:
Journal of medicinal chemistry. 64(21)
Identification of low-dose, low-molecular-weight, drug-like inhibitors of protein-protein interactions (PPIs) is a challenging area of research. Despite the challenges, the therapeutic potential of PPI inhibition has driven significant efforts toward
Publikováno v:
Tetrahedron Letters. 54:6373-6377
Acid-mediated cyclizations of SEM-protected heterocyclic anilines and adjacent hydroxyls or enol ethers during SEM deprotection are reported. Strategies to suppress these side reactions and their potential synthetic utilities are also described.
Autor:
Sheila M. Galloway, Binyuan Sun, Nancy Kelly, John W. Butcher, Grace H. C. Woo, Kerrie Spencer, J. Michael Ellis, Ryan D. Otte, Ekundayo Osimboni, Alan S. Bass, Sandra Lee, J. Richard Miller, Chiming Yang, Erica Leccese, Andrew M. Haidle, Alan B. Northrup, Lily Y. Moy, James P. Jewell, Alan Byford, Hani Houshyar, Gwendolyn J. Ward, Anthony Donofrio, Matthew L. Maddess, Michael D. Altman, M. Vijay Reddy, Stella H. Vincent
Publikováno v:
Journal of medicinal chemistry. 58(4)
Development of a series of highly kinome-selective spleen tyrosine kinase (Syk) inhibitors with favorable druglike properties is described. Early leads were discovered through X-ray crystallographic analysis, and a systematic survey of cores within a
Publikováno v:
Proceedings of the National Academy of Sciences. 100:5658-5663
Bacterial transglycosylases are enzymes that couple the disaccharide subunits of peptidoglycan to form long carbohydrate chains. These enzymes are the target of the pentasaccharide antibiotic moenomycin as well as the proposed target of certain glyco
Autor:
Binyuan Sun, John V. LaTour, Daniel Kahne, Steven D Dong, Ulrike S. Eggert, Zhong Chen, Simon J. Shaw
Publikováno v:
Tetrahedron. 58:6585-6594
We have prepared several sets of glycopeptide analogues in order to probe the molecular basis for the activity of derivatives that overcome vanA resistance. The results described in this paper provide compelling evidence that good vanA activity is du
Publikováno v:
ChemInform. 45
Substrates (I) undergo unexpected acid mediated cyclization involving the Sem-protecting amino group and a neighboring enol ether moiety to produce tricyclic heterocycles (II).
Autor:
Binyuan Sun, Paul A. Mann, Peter Orth, Gerald W. Shipps, Li Xiao, Aileen Soriano, Kyle Ann Soucy, Todd A. Black, Noriyuki Kawahata, Zhiwei Yang, Cliff C. Cheng
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(23)
The biotin carboxylase (AccC) is part of the multi-component bacterial acetyl coenzyme-A carboxylase (ACCase) and is essential for pathogen survival. We describe herein the affinity optimization of an initial hit to give 2-(2-chlorobenzylamino)-1-(cy
Publikováno v:
Journal of the American Chemical Society. 128(43)
Moenomycin A is the only known natural product that inhibits peptidoglycan biosynthesis by binding the bacterial transglycosylases. We describe a degradation/reconstruction route to manipulate the reducing end of moenomycin A. A comparison of the bio
Autor:
Gianbattista Panzone, Markus Oberthür, Catherine Leimkuhler, Dianah Barrett, Daniel Kahne, Brian Falcone, Suzanne Walker, Lan Chen, Binyuan Sun, Stefano Donadio
Publikováno v:
Journal of the American Chemical Society. 127:3250-3251
The glycopeptide antibiotics prevent maturation of the bacterial cell wall by binding to the terminal d-alanyl-d-alanine moiety of peptidoglycan precursors, thereby inhibiting the enzymes involved in the final stages of peptidoglycan synthesis. Howev