4YE6
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4YE8
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4YE9
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6UAN
| B-Raf:14-3-3 complex | 分子名称: | 14-3-3 zeta, Serine/threonine-protein kinase B-raf | 著者 | Kondo, Y, Ognjenovic, J, Banerjee, S, Karandur, D, Merk, A, Kulhanek, K, Wong, K, Roose, J.P, Subramaniam, S, Kuriyan, J. | 登録日 | 2019-09-11 | 公開日 | 2019-09-25 | 最終更新日 | 2019-12-18 | 実験手法 | ELECTRON MICROSCOPY (3.9 Å) | 主引用文献 | Cryo-EM structure of a dimeric B-Raf:14-3-3 complex reveals asymmetry in the active sites of B-Raf kinases. Science, 366, 2019
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6X1Q
| 1.8 Angstrom resolution structure of b-galactosidase with a 200 kV cryoARM electron microscope | 分子名称: | Beta-galactosidase, MAGNESIUM ION, SODIUM ION | 著者 | Merk, A, Fukumura, T, Zhu, X, Darling, J, Grisshammer, R, Ognjenovic, J, Subramaniam, S. | 登録日 | 2020-05-19 | 公開日 | 2020-07-01 | 最終更新日 | 2024-03-06 | 実験手法 | ELECTRON MICROSCOPY (1.8 Å) | 主引用文献 | 1.8 angstrom resolution structure of beta-galactosidase with a 200 kV CRYO ARM electron microscope. Iucrj, 7, 2020
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8E20
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8EDM
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8EDO
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8EDN
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8EDL
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7SZ7
| Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha. "tips-juxtaposed" conformation | 分子名称: | Epidermal growth factor receptor, Transforming growth factor alpha | 著者 | Huang, Y, Ognjenovic, J, Karandur, D, Miller, K, Merk, A, Subramaniam, S, Kuriyan, J. | 登録日 | 2021-11-25 | 公開日 | 2021-12-15 | 最終更新日 | 2024-10-23 | 実験手法 | ELECTRON MICROSCOPY (3.4 Å) | 主引用文献 | A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. Elife, 10, 2021
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7SZ1
| Cryo-EM structure of the extracellular module of the full-length EGFR L834R bound to EGF. "tips-separated" conformation | 分子名称: | Epidermal growth factor, Epidermal growth factor receptor | 著者 | Huang, Y, Ognjenovic, J, Karandur, D, Miller, K, Merk, A, Subramaniam, S, Kuriyan, J. | 登録日 | 2021-11-25 | 公開日 | 2021-12-22 | 実験手法 | ELECTRON MICROSCOPY (3.4 Å) | 主引用文献 | A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. Elife, 10, 2021
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7SZ0
| Cryo-EM structure of the extracellular module of the full-length EGFR L834R bound to EGF. "tips-juxtaposed" conformation | 分子名称: | Epidermal growth factor, Epidermal growth factor receptor | 著者 | Huang, Y, Ognjenovic, J, Karandur, D, Miller, K, Merk, A, Subramaniam, S, Kuriyan, J. | 登録日 | 2021-11-25 | 公開日 | 2021-12-22 | 実験手法 | ELECTRON MICROSCOPY (3.3 Å) | 主引用文献 | A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. Elife, 10, 2021
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7SYD
| Cryo-EM structure of the extracellular module of the full-length EGFR bound to EGF "tips-juxtaposed" conformation | 分子名称: | Epidermal growth factor, Epidermal growth factor receptor | 著者 | Huang, Y, Ognjenovic, J, Karandur, D, Miller, K, Merk, A, Subramaniam, S, Kuriyan, J. | 登録日 | 2021-11-24 | 公開日 | 2021-12-22 | 最終更新日 | 2024-10-23 | 実験手法 | ELECTRON MICROSCOPY (3.1 Å) | 主引用文献 | A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. Elife, 10, 2021
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7SZ5
| Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha "tips-separated" conformation | 分子名称: | Epidermal growth factor receptor, Transforming growth factor alpha | 著者 | Huang, Y, Ognjenovic, J, Karandur, D, Miller, K, Merk, A, Subramaniam, S, Kuriyan, J. | 登録日 | 2021-11-25 | 公開日 | 2021-12-22 | 最終更新日 | 2024-10-23 | 実験手法 | ELECTRON MICROSCOPY (3.6 Å) | 主引用文献 | A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. Elife, 10, 2021
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7SYE
| Cryo-EM structure of the extracellular module of the full-length EGFR bound to EGF. "tips-separated" conformation | 分子名称: | Epidermal growth factor, Epidermal growth factor receptor | 著者 | Huang, Y, Ognjenovic, J, Karandur, D, Miller, K, Merk, A, Subramaniam, S, Kuriyan, J. | 登録日 | 2021-11-24 | 公開日 | 2021-12-22 | 最終更新日 | 2024-10-16 | 実験手法 | ELECTRON MICROSCOPY (3.3 Å) | 主引用文献 | A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor. Elife, 10, 2021
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