Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Guanjing Chen"'
Autor:
Margaret E Brousseau, Kevin B Clairmont, Glen Spraggon, Alec N Flyer, Andrei A Golosov, Philipp Grosche, Jérôme André, Shari Caplan, Guanjing Chen, Li Fan, Raphael Gattlen, Alexander Koch, Ian Lewis, Jingzhou Li, Eugene Liu, Danuta Lubicka, Andreas Marzinzik, Katsumasa Nakajima, David Nettleton, Johannes Ottl, Meihui Pan, Tajesh Patel, Stephanie Pickett, Jennifer Poirier, Patrick C Reid, Xavier Pelle, Vanitha Subramanian, Victoria Vera, Mei Xu, Lihua Yang, Qing Yang, jinghua yu, Guoming Zhu, Lauren G Monovich
Publikováno v:
Circulation. 144
Elevated LDL-C is a major risk factor for atherosclerotic cardiovascular disease, the leading cause of death worldwide. Proprotein convertase subtilisin/kexin type 9 (PCSK9) has pronounced effects on LDL-C levels via its modulation of hepatic LDL rec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c41fa5183540594ef99cce950597f62
https://doi.org/10.1161/circ.144.suppl_1.10516
https://doi.org/10.1161/circ.144.suppl_1.10516
Autor:
Katsumasa Nakajima, David Nettleton, Guoming Zhu, Debra Burdick, Alexander W. Koch, Qing Yang, Glen Spraggon, Margaret E. Brousseau, Guanjing Chen, Lisa Ames, Raphael Gattlen, Flyer Alec, Jennifer Poirier, Jingzhou Li, Mohindra Seepersaud, Dawn Kelly-Sullivan, Stephanie Pickett, Xavier Pelle, Lauren Perry, Raj Chopra, Jakal Amin, Jerome Andre, Danuta Lubicka, Victoria Vera, Philipp Grosche, Patel Tajesh Jayprakash, Ian Lewis, Lihua Yang, Eugene Liu, Andrei Golosov, jinghua yu, Li Fan, Patrick C. Reid, Lauren G. Monovich, Shari L. Caplan, Meihui Pan, Diana Dubiel, Vanitha Subramanian, Kevin B. Clairmont, Johannes Ottl, Mei Xu, Andreas Marzinzik
Publikováno v:
Cell Chemical Biology. 29:249-258.e5
Summary Proprotein convertase subtilisin/kexin type 9 (PCSK9) regulates plasma low-density lipoprotein cholesterol (LDL-C) levels by promoting hepatic LDL receptor (LDLR) degradation. Therapeutic antibodies that disrupt PCSK9-LDLR binding reduce LDL-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9b646053b683b9aba0f84b9efef17df
https://doi.org/10.1016/j.chembiol.2021.08.012
https://doi.org/10.1016/j.chembiol.2021.08.012
Autor:
Diane M. Boucher, George Huang, Edward D. Ball, Guanjing Chen, David K. Heidary, Mark N. Namchuk, Jianguo Ma, Yung-Mae Yao, Jinwang Xu, Ron Grey, Forster Cornelia J, Greg Henkel, Jie-Hua Zhou, Michael J. Arnost, Robert J. Davies, Deborah Choquette
Publikováno v:
Journal of Medicinal Chemistry. 55:725-734
In acute myelogenous leukemia (AML), the FLT3 receptor tyrosine kinase (RTK) is highly expressed with 30% of patients expressing a mutated, constitutively active form of this protein. To inhibit this receptor, VX-322 was developed and found to be ver
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7846b2ba9ca36cd34cd88fe4b4e59f32
https://doi.org/10.1021/jm201198w
https://doi.org/10.1021/jm201198w
Autor:
Nigel Ewing, Judy Straub, Ursula A. Germann, James W. Janetka, Alex Aronov, Ernst ter Haar, Jeremy Green, Mark N. Namchuk, Guy W. Bemis, Xiaoling Xie, William Markland, Michael R. Hale, Pamella J. Ford, Gabriel Martinez-Botella, Guanjing Chen, Qing Tang, Francois Maltais, Marc Jacobs, Jingrong Cao, Srinivasu Poondru, Suganthini Nanthakumar
Publikováno v:
Journal of Medicinal Chemistry. 52:6362-6368
The Ras/Raf/MEK/ERK signal transduction, an oncogenic pathway implicated in a variety of human cancers, is a key target in anticancer drug design. A novel series of pyrimidylpyrrole ERK inhibitors has been identified. Discovery of a conformational ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4fa59a8f55914383a31fbef490e3a2
https://doi.org/10.1021/jm900630q
https://doi.org/10.1021/jm900630q
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:
Heidi Campbell, Alice Mitchell, Krzysztof P. Bzymek, Richard C. Holz, Ventris M. D'Souza, Guanjing Chen
Publikováno v:
Protein Expression and Purification. 37:294-305
The leucine aminopeptidase from Aeromonas proteolytica (also known as Vibrio proteolyticus) (AAP) is a metalloenzyme with broad substrate specificity. The open reading frame (ORF) for AAP encodes a 54 kDa enzyme, however, the extracellular enzyme has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2c8d5487b40cda286e865480a6b018d
https://doi.org/10.1016/j.pep.2004.05.004
https://doi.org/10.1016/j.pep.2004.05.004
Autor:
Richard C. Holz, Ventris M. D'Souza, Brian Bennett, William E. Antholine, Leila Ustinyuk, Guanjing Chen
Publikováno v:
Journal of the American Chemical Society. 124:13025-13034
The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which bound sequentially at two distinct sites. Both the mono- and disubstituted forms of AAP exhibited catalytic hyperactivity relative to the native dizinc enzyme. Monos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50ce17d85e66e81113da94b42470391e
https://doi.org/10.1021/ja026341p
https://doi.org/10.1021/ja026341p
Publikováno v:
Biochemistry. 39:2079-2087
p38 is a member of the mitogen-activated protein (MAP) kinase family. Activation (phosphorylation) of p38 acts as a switch for the transcriptional and translational regulation of a number of proteins, including the proinflammatory cytokines. Investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10efb67d81266e7d397e2a8c59086173
https://doi.org/10.1021/bi9919495
https://doi.org/10.1021/bi9919495
Publikováno v:
Journal of the American Chemical Society. 120:6329-6335
Proton NMR spectra of the hyperactive Cu(II)-substituted aminopeptidase from Aeromonas proteolytica (AAP) were recorded in both H2O and D2O buffered solution at pH 6.7. Several remarkably sharp, we...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cdb065def0d524519118005e20c254d0
https://doi.org/10.1021/ja971589d
https://doi.org/10.1021/ja971589d
Autor:
Cameron Stuver-Moody, David K. Heidary, Deborah Choquette, Greg Henkel, Jinwang Xu, Guanjing Chen, Shi-Kai Tian, Forster Cornelia J, Ron Grey, Joanne Ma, Albert C. Pierce, Michael J. Arnost, Mark N. Namchuk, Robert J. Davies, Vincent Galullo
Publikováno v:
Journal of medicinal chemistry. 54(20)
A high-throughput screen of our compound archive revealed a novel class of dual FMS-like tyrosine kinase 3 (FLT3)/c-KIT inhibitors. With the help of molecular modeling, this class was rapidly optimized for both potency against FLT3 and FLT3/c-KIT and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8199a06a85816672c917762c031052c0
https://pubmed.ncbi.nlm.nih.gov/21970471
https://pubmed.ncbi.nlm.nih.gov/21970471