Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Michael H, Reutershan"'
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:
Catherine White, Michael H. Reutershan, Elisabeth LaBlue, Bridget A. Becker, Katrina M. Mennie, Kaila Margrey, James Z. Deng, Jason D. Katz, Josep Saurí, Bruce Adams
Publikováno v:
Organic Letters. 23:4694-4698
Nitrogenous heterocycles are ubiquitous in pharmaceuticals and drug-like compounds; however, regioselective synthesis has proved challenging. Herein we report our efforts to develop a regioselective method for the synthesis of pyrazolo[1,5-a]pyridine
Autor:
David A Candito, David J. Witter, Josep Saurí, Yu-hong Lam, Surendra B Gadamsetty, Michael H. Reutershan, Yingchun Ye, Ryan V Quiroz, Sebastian Schneider, Rachel L. Palte, Hongming Li
Publikováno v:
The Journal of Organic Chemistry. 86:5142-5151
In the context of a PRMT5 inhibitor program, we describe our efforts to develop a flexible and robust strategy to access tetrahydrofuro[3,4-b]furan nucleoside analogues. Ultimately, it was found that a Wolfe type carboetherification from an alkenol d
Autor:
Chunhui Huang, Christian Fischer, Michelle R. Machacek, Stephane Bogen, Tesfaye Biftu, Xianhai Huang, Michael H. Reutershan, Ryan Otte, Qingmei Hong, Zhicai Wu, Yang Yu, Min Park, Lei Chen, Purakkattle Biju, Ian Knemeyer, Ping Lu, Christopher J. Kochansky, Michael Brendan Hicks, Yong Liu, Roy Helmy, Xavier Fradera, Anthony Donofrio, Josh Close, Matthew L. Maddess, Catherine White, David L. Sloman, Nunzio Sciammetta, Jun Lu, Craig Gibeau, Vladimir Simov, Hongjun Zhang, Peter Fuller, David Witter
Publikováno v:
ACS Med Chem Lett
[Image: see text] Mutant isocitrate dehydrogenase 1 (IDH1) has been identified as an attractive oncology target for which >70% of grade II and III gliomas and ∼10% of acute myeloid leukemia (AML) harbor somatic IDH1 mutations. These mutations confe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13ecfd534a4182e5c705a82b16c3ffcc
https://europepmc.org/articles/PMC9014435/
https://europepmc.org/articles/PMC9014435/
Autor:
Xavier Fradera, Michael H. Reutershan, Michelle R. Machacek, B. Wesley Trotter, Mark A. McCoy
Publikováno v:
Chembiochem : a European journal of chemical biology. 23(6)
We present an automated NMR-guided docking workflow that can be used to generate models of protein-ligand complexes based on data from NOE NMR experiments. The first step is to generate a number of intermolecular distance constraints from experimenta
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
Autor:
Katrina M, Mennie, Michael H, Reutershan, Catherine, White, Bruce, Adams, Bridget, Becker, James, Deng, Jason D, Katz, Elisabeth, LaBlue, Kaila, Margrey, Josep, Saurí
Publikováno v:
Organic letters. 23(12)
Nitrogenous heterocycles are ubiquitous in pharmaceuticals and drug-like compounds; however, regioselective synthesis has proved challenging. Herein we report our efforts to develop a regioselective method for the synthesis of pyrazolo[1,5
Autor:
David A, Candito, Yingchun, Ye, Ryan V, Quiroz, Michael H, Reutershan, David, Witter, Surendra B, Gadamsetty, Hongming, Li, Josep, Saurí, Sebastian E, Schneider, Yu-Hong, Lam, Rachel L, Palte
Publikováno v:
The Journal of organic chemistry. 86(7)
In the context of a PRMT5 inhibitor program, we describe our efforts to develop a flexible and robust strategy to access tetrahydrofuro[3,4
Autor:
My Sam Mansueto, Brooke M Swalm, Patrick S. Fier, Rachel L. Palte, Sandra Lee, Kristin Geddes, Josep Saurí, Michael H. Reutershan, Charles S. Yeung, Benjamin Nicholson, David J. Witter, Murray Wan, Robert P Hayes, Haiyan Xu, David L. Sloman, Nicole Follmer, Daniel S. Spellman, Danica A. Rankic, Pierre Daublain, Timothy J. Henderson, Jongwon Lim, Dapeng Chen, Erik Munsell, Guo Feng, Steven M. Silverman, Ryan V Quiroz, Doug Linn, Sulagna Sanyal, Michelle R. Machacek, Craig R. Gibeau, Shuhei Kawamura, Yuanwei Gao, Jonathan M E Hughes, Sebastian Schneider, Phieng Siliphaivanh, Yingchun Ye, Brian M. Lacey
Publikováno v:
Journal of medicinal chemistry. 64(7)
Protein arginine methyltransferase 5 (PRMT5) is a type II arginine methyltransferase that catalyzes the post-translational symmetric dimethylation of protein substrates. PRMT5 plays a critical role in regulating biological processes including transcr
Autor:
Christopher Sondey, Michael D. Altman, Sebastian Schneider, Michelle R. Machacek, Yingchun Ye, Robert P Hayes, Zangwei Xu, Phieng Siliphaivanh, Brian M. Lacey, Shuhei Kawamura, Haiyan Xu, Michael H. Reutershan, Rachel L. Palte, My Sam Mansueto
Publikováno v:
ACS Med Chem Lett
[Image: see text] Protein arginine methyltransferase 5 (PRMT5) belongs to a family of enzymes that regulate the posttranslational modification of histones and other proteins via methylation of arginine. Methylation of histones is linked to an increas