Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Marijane Russell"'
Autor:
Siegfried H. Reich, Stephen K. Burley, Spencer Emtage, Stephen R. Wasserman, Kevin Holme, Shane Atwell, Laura A. Pelletier, Lydia Smyth, Devon A. Thompson, Paul A. Sprengeler, Jeff M. Blaney, Tuan H. Do, Barbara C. Leon, Jason Adams, Isabelle A. Rooney, Marijane Russell, Kenneth D. Schwinn, J. Michael Sauder, Steve F. Gessert, Brandon E. Aubol, Marshall C. Peterman, Karen J. Froning, Jeremy D. Felce, Nanni H. Huser, Crystal M. Tang, Katti A. Jessen, Pierre-Yves Bounaud, Christopher R. Smith, Patrick S. Lee, Jorg Hendle, Sean G. Buchanan
Supplementary Tables 1-3, Figures 1-4 from SGX523 is an exquisitely selective, ATP-competitive inhibitor of the MET receptor tyrosine kinase with antitumor activity in vivo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b253da2b8af69b57f61a86d3221a13f9
https://doi.org/10.1158/1535-7163.22485138
https://doi.org/10.1158/1535-7163.22485138
Autor:
Siegfried H. Reich, Stephen K. Burley, Spencer Emtage, Stephen R. Wasserman, Kevin Holme, Shane Atwell, Laura A. Pelletier, Lydia Smyth, Devon A. Thompson, Paul A. Sprengeler, Jeff M. Blaney, Tuan H. Do, Barbara C. Leon, Jason Adams, Isabelle A. Rooney, Marijane Russell, Kenneth D. Schwinn, J. Michael Sauder, Steve F. Gessert, Brandon E. Aubol, Marshall C. Peterman, Karen J. Froning, Jeremy D. Felce, Nanni H. Huser, Crystal M. Tang, Katti A. Jessen, Pierre-Yves Bounaud, Christopher R. Smith, Patrick S. Lee, Jorg Hendle, Sean G. Buchanan
Supplementary Figure 1 from SGX523 is an exquisitely selective, ATP-competitive inhibitor of the MET receptor tyrosine kinase with antitumor activity in vivo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee53a296e3d5b8a6d460e10e97860b5a
https://doi.org/10.1158/1535-7163.22485141.v1
https://doi.org/10.1158/1535-7163.22485141.v1
Autor:
Siegfried H. Reich, Stephen K. Burley, Spencer Emtage, Stephen R. Wasserman, Kevin Holme, Shane Atwell, Laura A. Pelletier, Lydia Smyth, Devon A. Thompson, Paul A. Sprengeler, Jeff M. Blaney, Tuan H. Do, Barbara C. Leon, Jason Adams, Isabelle A. Rooney, Marijane Russell, Kenneth D. Schwinn, J. Michael Sauder, Steve F. Gessert, Brandon E. Aubol, Marshall C. Peterman, Karen J. Froning, Jeremy D. Felce, Nanni H. Huser, Crystal M. Tang, Katti A. Jessen, Pierre-Yves Bounaud, Christopher R. Smith, Patrick S. Lee, Jorg Hendle, Sean G. Buchanan
The MET receptor tyrosine kinase has emerged as an important target for the development of novel cancer therapeutics. Activation of MET by mutation or gene amplification has been linked to kidney, gastric, and lung cancers. In other cancers, such as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::265be7461b5631c4751aa9dac9de05d6
https://doi.org/10.1158/1535-7163.c.6531795.v1
https://doi.org/10.1158/1535-7163.c.6531795.v1
Autor:
Joey P Ting, Frances Tung, Stephen Antonysamy, Stephen Wasserman, Spencer B Jones, Feiyu F Zhang, Alfonso Espada, Howard Broughton, Michael J Chalmers, Michael E Woodman, Holly A Bina, Jeffrey A Dodge, Jordi Benach, Aiping Zhang, Christopher Groshong, Danalyn Manglicmot, Marijane Russell, Sepideh Afshar
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0190850 (2018)
To date, IL-17A antibodies remain the only therapeutic approach to correct the abnormal activation of the IL-17A/IL-17R signaling complex. Why is it that despite the remarkable success of IL-17 antibodies, there is no small molecule antagonist of IL-
Externí odkaz:
https://doaj.org/article/9c2e01bb6db44b01a1e0d014dd80e53b
Autor:
Stephen Antonysamy, Bradley Condon, Zhanna Druzina, Jeffrey B Bonanno, Tarun Gheyi, Feiyu Zhang, Iain MacEwan, Aiping Zhang, Sheela Ashok, Logan Rodgers, Marijane Russell, John Gately Luz
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e84147 (2013)
The enhancer-of-zeste homolog 2 (EZH2) gene product is an 87 kDa polycomb group (PcG) protein containing a C-terminal methyltransferase SET domain. EZH2, along with binding partners, i.e., EED and SUZ12, upon which it is dependent for activity forms
Externí odkaz:
https://doaj.org/article/d0efb2c872af40ed96f0cf32d3038efa
Autor:
Frances Lu, Bryan G. Johnson, Daniel Ursu, Joan H. Carter, Lisa M. Broad, Kofi Adragni, Shane Atwell, Jing Wang, David K. Clawson, Beverly A. Heinz, Steven P. Swanson, James A. Monn, Qi Chen, Helene E. Sanger, David B. Shaw, Steven Marc Massey, Xushan Wang, Marijane Russell, Steven S. Henry, Junliang Hao, Rajni M. Bhardwaj, Diseroad Benjamin Alan, David L. McKinzie, Brian G. Getman, John T. Catlow
Publikováno v:
Journal of Medicinal Chemistry. 61:2303-2328
Multiple therapeutic opportunities have been suggested for compounds capable of selective activation of metabotropic glutamate 3 (mGlu3) receptors, but small molecule tools are lacking. As part of our ongoing efforts to identify potent, selective, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::34fd3a986aac486e41e6ea738f1a4465
https://doi.org/10.1021/acs.jmedchem.7b01481
https://doi.org/10.1021/acs.jmedchem.7b01481
Autor:
Yilin Meng, Cen Gao, Michal Vieth, Shane Atwell, Marijane Russell, Benoît Roux, David K. Clawson
Understanding protein conformational variability remains a challenge in drug discovery. The issue arises in protein kinases, whose multiple conformational states can affect the binding of small-molecule inhibitors. To overcome this challenge, we prop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f561d0d49719d28f107f83c9e480c8e
https://europepmc.org/articles/PMC6317529/
https://europepmc.org/articles/PMC6317529/
Autor:
James A, Monn, Steven S, Henry, Steven M, Massey, David K, Clawson, Qi, Chen, Benjamin A, Diseroad, Rajni M, Bhardwaj, Shane, Atwell, Frances, Lu, Jing, Wang, Marijane, Russell, Beverly A, Heinz, Xu-Shan, Wang, Joan H, Carter, Brian G, Getman, Kofi, Adragni, Lisa M, Broad, Helene E, Sanger, Daniel, Ursu, John T, Catlow, Steven, Swanson, Bryan G, Johnson, David B, Shaw, David L, McKinzie, Junliang, Hao
Publikováno v:
Journal of medicinal chemistry. 61(6)
Multiple therapeutic opportunities have been suggested for compounds capable of selective activation of metabotropic glutamate 3 (mGlu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0b0a91b923b376e1620dd4223a841b23
https://pubmed.ncbi.nlm.nih.gov/29350927
https://pubmed.ncbi.nlm.nih.gov/29350927
Autor:
Mark G. Bures, David Edward Tupper, Joan H. Carter, James A. Monn, David L. McKinzie, Marijane Russell, Lourdes Prieto, Steven S. Henry, Reinhard Matthew Robert, Alicia Marcos, Lesley Walton, Christopher David Beadle, Bryan G. Johnson, Brian G. Getman, John T. Catlow, Frances Lu, Xushan Wang, Lorena Taboada, S. Richard Baker, Beverly A. Heinz, Helene Rudyk, David B. Shaw, Jaime Blanco, Carlos Lamas, Steven Swanson, David K. Clawson, Junliang Hao, Carlos Montero, Teresa Man, Shane Atwell, Barry Peter Clark, Jing Wang
Publikováno v:
Journal of Medicinal Chemistry. 58:7526-7548
Identification of orthosteric mGlu(2/3) receptor agonists capable of discriminating between individual mGlu2 and mGlu3 subtypes has been highly challenging owing to the glutamate-site sequence homology between these proteins. Herein we detail the pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13d4b305d2ec1acea2f3d473c73251c1
https://doi.org/10.1021/acs.jmedchem.5b01124
https://doi.org/10.1021/acs.jmedchem.5b01124
Autor:
Kuklish Steven Lee, Dagart Allison, Bradley Condon, Aiping Zhang, Anita K. Harvey, Ashley V. Sloan, Xiao-Peng Yu, Ryan Thomas Backer, Matthew R. Lee, John G. Luz, Marijane Russell, Srinivasan Chandrasekhar, Matthew Fisher, Shawn Chang, Stephen Antonysamy
Publikováno v:
Journal of Medicinal Chemistry. 58:4727-4737
Microsomal prostaglandin E synthase 1 (mPGES-1) is an α-helical homotrimeric integral membrane inducible enzyme that catalyzes the formation of prostaglandin E2 (PGE2) from prostaglandin H2 (PGH2). Inhibition of mPGES-1 has been proposed as a therap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52f51d736c36586dd49c583231b9633f
https://doi.org/10.1021/acs.jmedchem.5b00330
https://doi.org/10.1021/acs.jmedchem.5b00330