Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Darcy, Kohls"'
Autor:
Dean F. Rigel, Hidetomo Imase, Kayo Yasoshima, Darcy Kohls, Toshio Kawanami, Yukiko I. Yagi, Jun Yuan, Monish Jain, Hyi-Man Park, Upendra A. Argikar, David Yowe, Paul Taslimi, Xiaoling Xie, Yuki Iwaki, Neeraja Idamakanti, Taeyong Yoon, Ken Yamada, Vidya Kunjathoor, Keith DiPetrillo, Lingfei Xu, Mitsunori Kato, Meicheng Zhu, Julian Levell, Zachary Robinson, Lauren G. Monovich
Publikováno v:
Journal of Medicinal Chemistry. 60:7099-7107
The observed structure-activity relationship of three distinct ATP noncompetitive With-No-Lysine (WNK) kinase inhibitor series, together with a crystal structure of a previously disclosed allosteric inhibitor bound to WNK1, led to an overlay hypothes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3d52943277800bc7194904670e9e1d7
https://doi.org/10.1021/acs.jmedchem.7b00708
https://doi.org/10.1021/acs.jmedchem.7b00708
Autor:
Mitsunori Kato, Jason Gunawan, Xiaoling Xie, Muneto Mogi, Neeraja Idamakanti, Waan-Jeng Huang, Daniel LaSala, Ken Yamada, Hajime Yoshisue, Hyi-Man Park, Zhan Deng, Darcy Kohls, Yukiko I. Yagi, David Yowe, Kayo Yasoshima, Amy Qiongshu Xie, Reinhardt Juergen, Debra Burdick, Natasha Kreder, Q. Kimberley Yue, Pramod Pandey, Peter Drueckes, Isabel Schmidt, Toshio Kawanami, Hiromichi Wakai, Ji-Hu Zhang
Publikováno v:
ACS Chemical Biology. 11:3338-3346
Protein kinases are known for their highly conserved adenosine triphosphate (ATP)-binding site, rendering the discovery of selective inhibitors a major challenge. In theory, allosteric inhibitors can achieve high selectivity by targeting less conserv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b363e34512a8c7147a1bb8f1b5e7f58f
https://doi.org/10.1021/acschembio.6b00511
https://doi.org/10.1021/acschembio.6b00511
Autor:
Fallon Lin, Ali Farsidjani, Daniel J. McKay, Darcy Kohls, Simon van der Plas, Lindsey Rodrigues, Ming Xu, Kirk Wright, Jinyun Chen, Raviraj Kulathila, Daniel Baird, Pascal D. Fortin, YoungShin Cho, Xiaoling Xie, Julian Levell, Raymond Pagliarini, Vladimir Capka, Kimberly E. Bowen, B. Barry Touré, Gregg Chenail, David Sage, Julia Dooley, Hong Yin
Publikováno v:
Structure (London, England : 1993). 25(3)
Oncogenic IDH1 and IDH2 mutations contribute to cancer via production of R-2-hydroxyglutarate (2-HG). Here, we characterize two structurally distinct mutant- and isoform-selective IDH1 inhibitors that inhibit 2-HG production. Both bind to an alloster
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e323c04dbdcb84f8a485fd20732ee01
https://pubmed.ncbi.nlm.nih.gov/28132785
https://pubmed.ncbi.nlm.nih.gov/28132785
Autor:
Darcy Kohls, Simon Low, Glen Rennie, Yuan-Hua Ding, Cyrille Kuhn, Frederic Feru, Michael Kothe, Rocco Coli
Publikováno v:
Chemical Biology & Drug Design. 70:540-546
Polo-like kinase 1 is an important regulator of cell cycle progression whose over-expression is often associated with oncogenesis. Polo-like kinase 1 hence represents an attractive target for cancer intervention. BI 2536 (Boehringer Ingelheim, Ingelh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70f56f22404ef9e96e6c481d195548de
https://doi.org/10.1111/j.1747-0285.2007.00594.x
https://doi.org/10.1111/j.1747-0285.2007.00594.x
Autor:
Simon Low, Rocco Coli, Yuan-Hua Ding, Alan C. Cheng, Alissa L. Sheils, Cyrille Kuhn, Thomas A. Wynn, Theresa L. Johnson, Jim Nonomiya, Suzanne L. Jacques, Darcy Kohls, Cristina Lewis, Michael Kothe, Kimberly A. Verdries, Christine Loh
Publikováno v:
Biochemistry. 46:5960-5971
Polo-like kinase 1 (Plk1) is an attractive target for the development of anticancer agents due to its importance in regulating cell-cycle progression. Overexpression of Plk1 has been detected in a variety of cancers, and expression levels often corre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cb7b5150b3f78f35926d557efc4acae
https://doi.org/10.1021/bi602474j
https://doi.org/10.1021/bi602474j
Autor:
Ken Yamada, Hyi-Man Park, Dean F Rigel, Keith DiPetrillo, Erin J Whalen, Anthony Anisowicz, Michael Beil, James Berstler, Cara Emily Brocklehurst, Debra A Burdick, Shari L Caplan, Michael P Capparelli, Guanjing Chen, Wei Chen, Bethany Dale, Lin Deng, Fumin Fu, Norio Hamamatsu, Kouki Harasaki, Tracey Herr, Peter Hoffmann, Qi-Ying Hu, Waan-Jeng Huang, Neeraja Idamakanti, Hidetomo Imase, Yuki Iwaki, Monish Jain, Jey Jeyaseelan, Mitsunori Kato, Virendar K Kaushik, Darcy Kohls, Vidya Kunjathoor, Daniel LaSala, Jongchan Lee, Jing Liu, Yang Luo, Fupeng Ma, Ruowei Mo, Sarah Mowbray, Muneto Mogi, Flavio Ossola, Pramod Pandey, Sejal J Patel, Swetha Raghavan, Bahaa Salem, Yuka H Shanado, Gary M Trakshel, Gordon Turner, Hiromichi Wakai, Chunhua Wang, Stephen Weldon, Jennifer B Wielicki, Xiaoling Xie, Lingfei Xu, Yukiko I Yagi, Kayo Yasoshima, Jianning Yin, David Yowe, Ji-Hu Zhang, Gang Zheng, Lauren Monovich
Publikováno v:
Nature chemical biology. 12(11)
The With-No-Lysine (K) (WNK) kinases play a critical role in blood pressure regulation and body fluid and electrolyte homeostasis. Herein, we introduce the first orally bioavailable pan-WNK-kinase inhibitor, WNK463, that exploits unique structural fe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78087a9853125909a6b388fbc86c95c9
https://pubmed.ncbi.nlm.nih.gov/27595330
https://pubmed.ncbi.nlm.nih.gov/27595330
Autor:
Qing Cao, Yuan-Hua Ding, Yan Zhang, Michael Kothe, Tom Ellenberger, Andre Iffland, Simon Low, Darcy Kohls, Ajith V. Kamath, Jing Luan
Publikováno v:
Biochemistry. 44:8312-8325
Phosphodiesterases (PDEs) modulate signaling by cyclic nucleotides in diverse processes such as cardiac contractility, platelet aggregation, lipolysis, glycogenolysis, and smooth muscle contraction. Cyclic guanosine monophosphate (cGMP) stimulated hu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6331c53507f8f9ce83242e98058692f
https://doi.org/10.1021/bi047313h
https://doi.org/10.1021/bi047313h
Autor:
Yuan-Hua Ding, Brendan Connolly, Alissa L. Sheils, Michael Kothe, Alan C. Cheng, Ajith V. Kamath, Darcy Kohls, Maura E. Charlton, Laura Weibley, Lily Yang, Qing Cao, Brian J. Stockman
Publikováno v:
Chemical biologydrug design. 73(2)
Aberrant activation of the phosphoinositide 3-kinase pathway because of genetic mutations of essential signalling proteins has been associated with human diseases including cancer and diabetes. The pivotal role of 3-phosphoinositide-dependent kinase-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::902bb0578fd6ff04c7f3b02c2a32a510
https://pubmed.ncbi.nlm.nih.gov/19207420
https://pubmed.ncbi.nlm.nih.gov/19207420
Autor:
H. James Harwood, R. Kirk McPherson, Susan Tapley, Leanne M. Buzon, Kevin Daniel Freeman-Cook, Steven B. Coffey, Richard L. Elliott, Darcy Kohls, Liang Tong, Felix Vajdos, Meihua Tu, Eliot Sugarman, Shawn D. Doran, Francis Rajamohan, Eric S. Marr, Hailong Zhang, Wei Song, Kenneth J. DiRico, Jeffrey W. Corbett, Janet A. Houser, Sharad B. Murdande, William P. Esler, Martha L. Minich, Christopher J. Jones
Publikováno v:
Bioorganicmedicinal chemistry letters. 20(7)
Screening Pfizer's compound library resulted in the identification of weak acetyl-CoA carboxylase inhibitors, from which were obtained rACC1 CT-domain co-crystal structures. Utilizing HTS hits and structure-based drug discovery, a more rigid inhibito
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c15f1a6bcbbc031e2169b1cbccc4dfb
https://pubmed.ncbi.nlm.nih.gov/20219367
https://pubmed.ncbi.nlm.nih.gov/20219367
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 55:1206-1208
Formiminotransferase–cyclodeaminase (E.C. 2.1.2.5–E.C. 4.3.1.4) is a bifunctional enzyme involved in the histidine-degradation pathway which exhibits specificity for polyglutamylated folate substrates. The first function of the enzyme transfers t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be0efafe2c85a758975ac0456aa0d18f
https://doi.org/10.1107/s0907444999003601
https://doi.org/10.1107/s0907444999003601