Zobrazeno 1 - 10
of 235
pro vyhledávání: '"Michael J. Eck"'
Autor:
Zhengnian Li, Jie Jiang, Scott B. Ficarro, Tyler S. Beyett, Ciric To, Isidoro Tavares, Yingde Zhu, Jiaqi Li, Michael J. Eck, Pasi A. Jänne, Jarrod A. Marto, Tinghu Zhang, Jianwei Che, Nathanael S. Gray
Publikováno v:
ACS Central Science, Vol 10, Iss 6, Pp 1156-1166 (2024)
Externí odkaz:
https://doaj.org/article/d5c6dbf338584d8bbd4b0121b594a89f
Autor:
Florian Wittlinger, Blessing C. Ogboo, Ekaterina Shevchenko, Tahereh Damghani, Calvin D. Pham, Ilse K. Schaeffner, Brandon T. Oligny, Surbhi P. Chitnis, Tyler S. Beyett, Alexander Rasch, Brian Buckley, Daniel A. Urul, Tatiana Shaurova, Earl W. May, Erik M. Schaefer, Michael J. Eck, Pamela A. Hershberger, Antti Poso, Stefan A. Laufer, David E. Heppner
Publikováno v:
Communications Chemistry, Vol 7, Iss 1, Pp 1-14 (2024)
Abstract Bivalent molecules consisting of groups connected through bridging linkers often exhibit strong target binding and unique biological effects. However, developing bivalent inhibitors with the desired activity is challenging due to the dual mo
Externí odkaz:
https://doaj.org/article/4d98b317db4743c79540cdb1697614f4
Autor:
Eunyoung Park, Shaun Rawson, Anna Schmoker, Byeong-Won Kim, Sehee Oh, Kangkang Song, Hyesung Jeon, Michael J. Eck
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract RAF-family kinases are activated by recruitment to the plasma membrane by GTP-bound RAS, whereupon they initiate signaling through the MAP kinase cascade. Prior structural studies of KRAS with RAF have focused on the isolated RAS-binding and
Externí odkaz:
https://doaj.org/article/024f9e85bb9c4c38ad6050e31be70692
Autor:
Tyler S. Beyett, Ciric To, David E. Heppner, Jaimin K. Rana, Anna M. Schmoker, Jaebong Jang, Dries J. H. De Clercq, Gabriel Gomez, David A. Scott, Nathanael S. Gray, Pasi A. Jänne, Michael J. Eck
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
Acquired drug resistance is common during chemotherapy. Here, the authors describe the structural basis and molecular mechanism by which allosteric and clinically approved, ATP-competitive inhibitors of EGFR synergize to overcome resistance in lung c
Externí odkaz:
https://doaj.org/article/b71e888015d54f3e90272f29edf5c334
Autor:
Eunyoung Park, Shaun Rawson, Anna Schmoker, Byeong-Won Kim, Sehee Oh, Kangkang Song, Hyesung Jeon, Michael J. Eck
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-1 (2023)
Externí odkaz:
https://doaj.org/article/f878864051f7492aada23cea4aaae674
Comprehensive functional evaluation of variants of fibroblast growth factor receptor genes in cancer
Autor:
Ikuko Takeda Nakamura, Shinji Kohsaka, Masachika Ikegami, Hiroshi Ikeuchi, Toshihide Ueno, Kunhua Li, Tyler S. Beyett, Takafumi Koyama, Toshio Shimizu, Noboru Yamamoto, Fumiyuki Takahashi, Kazuhisa Takahashi, Michael J. Eck, Hiroyuki Mano
Publikováno v:
npj Precision Oncology, Vol 5, Iss 1, Pp 1-14 (2021)
Abstract Various genetic alterations of the fibroblast growth factor receptor (FGFR) family have been detected across a wide range of cancers. However, inhibition of FGFR signaling by kinase inhibitors demonstrated limited clinical effectiveness. Her
Externí odkaz:
https://doaj.org/article/1eb0d4f54965435d896fb494c2235251
Autor:
Jing Zhang, Xueliang Gao, Fabienne Schmit, Guillaume Adelmant, Michael J. Eck, Jarrod A. Marto, Jean J. Zhao, Thomas M. Roberts
Publikováno v:
Cell Reports, Vol 20, Iss 3, Pp 549-557 (2017)
The p110β isoform of PI3K is preferentially activated in many tumors deficient in the phosphatase and tensin homolog (PTEN). However, the mechanism(s) linking PTEN loss to p110β activation remain(s) mysterious. Here, we identify CRKL as a member of
Externí odkaz:
https://doaj.org/article/3c7f2758514b4e9ca685e4628d81a820
Autor:
Weikang Cai, Masaji Sakaguchi, Andre Kleinridders, Gonzalo Gonzalez-Del Pino, Jonathan M. Dreyfuss, Brian T. O’Neill, Alfred K. Ramirez, Hui Pan, Jonathon N. Winnay, Jeremie Boucher, Michael J. Eck, C. Ronald Kahn
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
Despite being structurally similar, the insulin receptor (IR) and insulin growth factor I receptor (IGF1R) elicit distinct signalling pathways. Here the authors use receptor chimeras to unveil that IR and IGF1R signalling is related primarily to diff
Externí odkaz:
https://doaj.org/article/c27316e5cd6942f09a89e65936cda8b3
Autor:
Peter A. Meyer, Stephanie Socias, Jason Key, Elizabeth Ransey, Emily C. Tjon, Alejandro Buschiazzo, Ming Lei, Chris Botka, James Withrow, David Neau, Kanagalaghatta Rajashankar, Karen S. Anderson, Richard H. Baxter, Stephen C. Blacklow, Titus J. Boggon, Alexandre M. J. J. Bonvin, Dominika Borek, Tom J. Brett, Amedeo Caflisch, Chung-I Chang, Walter J. Chazin, Kevin D. Corbett, Michael S. Cosgrove, Sean Crosson, Sirano Dhe-Paganon, Enrico Di Cera, Catherine L. Drennan, Michael J. Eck, Brandt F. Eichman, Qing R. Fan, Adrian R. Ferré-D'Amaré, J. Christopher Fromme, K. Christopher Garcia, Rachelle Gaudet, Peng Gong, Stephen C. Harrison, Ekaterina E. Heldwein, Zongchao Jia, Robert J. Keenan, Andrew C. Kruse, Marc Kvansakul, Jason S. McLellan, Yorgo Modis, Yunsun Nam, Zbyszek Otwinowski, Emil F. Pai, Pedro José Barbosa Pereira, Carlo Petosa, C. S. Raman, Tom A. Rapoport, Antonina Roll-Mecak, Michael K. Rosen, Gabby Rudenko, Joseph Schlessinger, Thomas U. Schwartz, Yousif Shamoo, Holger Sondermann, Yizhi J. Tao, Niraj H. Tolia, Oleg V. Tsodikov, Kenneth D. Westover, Hao Wu, Ian Foster, James S. Fraser, Filipe R. N C. Maia, Tamir Gonen, Tom Kirchhausen, Kay Diederichs, Mercè Crosas, Piotr Sliz
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
The validation and analysis of X-ray crystallographic data is essential for reproducibility and the development of crystallographic methods. Here, the authors describe a repository for crystallographic datasets and demonstrate some of the ways it cou
Externí odkaz:
https://doaj.org/article/72383da3679147f9a2668c703d709d2e
Autor:
Daqi Tu, Zehua Zhu, Alicia Y. Zhou, Cai-hong Yun, Kyung-Eun Lee, Angela V. Toms, Yiqun Li, Gavin P. Dunn, Edmond Chan, Tran Thai, Shenghong Yang, Scott B. Ficarro, Jarrod A. Marto, Hyesung Jeon, William C. Hahn, David A. Barbie, Michael J. Eck
Publikováno v:
Cell Reports, Vol 3, Iss 3, Pp 747-758 (2013)
Upon stimulation by pathogen-associated inflammatory signals, TANK-binding kinase 1 (TBK1) induces type I interferon expression and modulates nuclear factor κB (NF-κB) signaling. Here, we describe the 2.4 Å-resolution crystal structure of nearly f
Externí odkaz:
https://doaj.org/article/994a8e3a594e4cb5822df3147232d8d4