Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Elizabeth M. Turner"'
Autor:
Christian Voitenleitner, Huichang Zhang, Renae M. Crosby, Kirsten M. Kahler, Feng Wang, John F. Miller, Elizabeth M. Turner, Daniel J. Price, Jing Fang, Andrew Maynard, Vincent W.-F. Tai, Katrina L. Creech, Andrew J. Peat, J. Brad Shotwell, Shawn P. Williams, Amanda Mathis, Jeffrey J. Pouliot, Pek Yoke Chong
Publikováno v:
Journal of Medicinal Chemistry. 62:3254-3267
[Image: see text] We previously described the discovery of GSK5852 (1), a non-nucleoside polymerase (NS5B) inhibitor of hepatitis C virus (HCV), in which an N-benzyl boronic acid was essential for potent antiviral activity. Unfortunately, facile benz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0813e0ff593055c94f6a8f690744f127
https://doi.org/10.1021/acs.jmedchem.8b01719
https://doi.org/10.1021/acs.jmedchem.8b01719
Autor:
Chenguang Zhao, Morven Graham, Ethan Laudermilch, Elizabeth M. Turner, Christian Schlieker, Pei-Ling Tsai
Publikováno v:
Molecular Biology of the Cell
Torsins are essential, disease-relevant ATPases, but their function is unknown. Monitoring of nuclear envelope morphology after deletion of multiple Torsins or their cofactors reveals a robust inner nuclear membrane–blebbing phenotype in HeLa cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c498d906d633a793ba1e6d30dfa3d1a9
http://europepmc.org/articles/PMC5156537
http://europepmc.org/articles/PMC5156537
Autor:
Christian Schlieker, Rebecca S. H. Brown, Pei-Ling Tsai, Elizabeth M. Turner, Ethan Laudermilch
Publikováno v:
Journal of Virology. 89:8444-8452
TorsinA is a membrane-tethered AAA+ ATPase implicated in nuclear envelope dynamics as well as the nuclear egress of herpes simplex virus 1 (HSV-1). The activity of TorsinA and the related ATPase TorsinB strictly depends on LAP1 and LULL1, type II tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a20991a17d953fe9ed69630d4aaeb340
https://doi.org/10.1128/jvi.01143-15
https://doi.org/10.1128/jvi.01143-15
Publikováno v:
Journal of Biological Chemistry. 289:552-564
Torsins are membrane-tethered AAA+ ATPases residing in the nuclear envelope (NE) and endoplasmic reticulum (ER). Here, we show that the induction of a conditional, dominant-negative TorsinB variant provokes a profound reorganization of the endomembra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bfb8dcafb5b777cdf84502542945726
https://doi.org/10.1074/jbc.m113.515791
https://doi.org/10.1074/jbc.m113.515791
Autor:
Amanda Mathis, Wenyan Mo, Susan Long, Stephanie Anna Chan, Jill Walker, Ryan Lauchli, Martin Robert Leivers, Elizabeth M. Turner, Tony Ton, Sebastian Liehr, J. Greg Falls, John F. Miller, Michael Youngman
Publikováno v:
Journal of Medicinal Chemistry. 57:1964-1975
By reducing the basicity of the core heterocycle in a series of HCV NS5B inhibitors, the hERG liability was reduced. The SAR was then systematically explored in order to increase solubility and enable dose escalation while retaining potency. During t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac356040e8f55946d9a047bcc57f508d
https://doi.org/10.1021/jm401337x
https://doi.org/10.1021/jm401337x
Autor:
Andrew Maynard, Renae M. Crosby, Byron Ellis, Robert Hamatake, Zhi Hong, Brian A. Johns, Kirsten M. Kahler, Cecilia Koble, Anna Leivers, Martin R. Leivers, Amanda Mathis, Andrew J. Peat, Jeffrey J. Pouliot, Christopher D. Roberts, Vicente Samano, Rachel M. Schmidt, Gary K. Smith, Andrew Spaltenstein, Eugene L. Stewart, Pia Thommes, Elizabeth M. Turner, Christian Voitenleitner, Jill T. Walker, Greg Waitt, Jason Weatherhead, Kurt Weaver, Shawn Williams, Lois Wright, Zhiping Z. Xiong, David Haigh, J. Brad Shotwell
Publikováno v:
Journal of Medicinal Chemistry. 57:1902-1913
A boronic acid moiety was found to be a critical pharmacophore for enhanced in vitro potency against wild-type hepatitis C replicons and known clinical polymorphic and resistant HCV mutant replicons. The synthesis, optimization, and structure-activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6ce7599d644e69b47104c8ac1a7db2e
https://doi.org/10.1021/jm400317w
https://doi.org/10.1021/jm400317w
Publikováno v:
Rare Diseases
Lamin B Receptor (LBR) is an inner nuclear membrane protein associated with the rare human diseases Pelger-Huët anomaly and Greenberg skeletal dysplasia. A new study has used CRISPR/Cas9-mediated genetic manipulations in a human cell system to deter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38569876d2c058a407efa760884f5c49
http://europepmc.org/articles/PMC5077067
http://europepmc.org/articles/PMC5077067
Publikováno v:
eLife
eLife, Vol 5 (2016)
eLife, Vol 5 (2016)
Lamin B receptor (LBR) is a polytopic membrane protein residing in the inner nuclear membrane in association with the nuclear lamina. We demonstrate that human LBR is essential for cholesterol synthesis. LBR mutant derivatives implicated in Greenberg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d40a325ba0a704220708834cc164f41
https://doi.org/10.7554/elife.16011
https://doi.org/10.7554/elife.16011
Autor:
Michael Thomson, John F. Miller, Kristjan S. Gudmundsson, Elizabeth M. Turner, Stephen Jenkinson, Pat Wheelan, Andrew Spaltenstein
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 20:2125-2128
The lead optimization of a series of N-substituted benzimidazole CXCR4 antagonists is described. Side chain modifications and stereochemical optimization led to substantial improvements in potency and protein shift to afford compounds with low nanomo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88af6326d71661a8731afe3cb94e4f83
https://doi.org/10.1016/j.bmcl.2010.02.053
https://doi.org/10.1016/j.bmcl.2010.02.053