Structural analysis of p185~c-neu and epidermal growth factor receptor tyrosine kinases: Oligomerization of kinase domains

Ramachandran Murali; Patrick J. Brennan; Thomas Kieber-Emmons

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Structural analysis of p185~c-neu and epidermal growth factor receptor tyrosine kinases: Oligomerization of kinase domains

机译：p185〜c-neu和表皮生长因子受体酪氨酸激酶的结构分析：激酶结构域的低聚

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摘要

The epidermal growth factor receptor (EGFR) and p185~c-neu proteins associate as dimers to create an efficient signaling assembly. Overexpression of these re- ceptors together enhances their intrinsic kinase activity and concomitantly results in oncogenic cellular transformation. The ectodomain is able to stabilize the dimer, whereas the kinase domain mediates biological activity.

机译：表皮生长因子受体（EGFR）和p185〜c-neu蛋白缔合为二聚体，从而形成有效的信号传导装配。这些受体的过表达共同增强了其内在的激酶活性，并随之导致致癌的细胞转化。胞外域能够稳定二聚体，而激酶域介导生物活性。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1996年第13期|p.6252-6257|共6页
作者
Ramachandran Murali; Patrick J. Brennan; Thomas Kieber-Emmons;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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1. Sensitivities to various epidermal growth factor receptor-tyrosine kinase inhibitors of uncommon epidermal growth factor receptor mutations L861Q and S768I: What is the optimal epidermal growth factor receptor-tyrosine kinase inhibitor? [J] . Banno Eri, Togashi Yosuke, Nakamura Yu, Cancer science. . 2016,第8期

机译：对不常见的表皮生长因子受体突变L861Q和S768I的各种表皮生长因子受体-酪氨酸激酶抑制剂的敏感性：最佳的表皮生长因子受体-酪氨酸激酶抑制剂是什么？
2. Sensitivities to various epidermal growth factor receptor‐tyrosine kinase inhibitors of uncommon epidermal growth factor receptor mutations L861Q and S768I: What is the optimal epidermal growth factor receptor‐tyrosine kinase inhibitor? [J] . Banno Eri, Togashi Yosuke, Nakamura Yu, Cancer science. . 2016,第8期

机译：对各种表皮生长因子受体酪氨酸激酶抑制剂的罕见表皮生长因子受体突变L861Q和S768I的敏感性：最佳的表皮生长因子受体酪氨酸激酶抑制剂是什么？
3. Sensitivities to various epidermal growth factor receptor-tyrosine kinase inhibitors of uncommon epidermal growth factor receptor mutations L861Q and S768I: What is the optimal epidermal growth factor receptor-tyrosine kinase inhibitor? [J] . Banno Eri, Togashi Yosuke, Nakamura Yu, Cancer science. . 2016,第8期

机译：对各种表皮生长因子受体 - 酪氨酸激酶抑制剂的敏感性罕见表皮生长因子受体突变L861Q和S768i：什么是最佳表皮生长因子受体 - 酪氨酸激酶抑制剂是什么？
4. QSAR Study of Quinazoline Derivatives as Inhibitor of Epidermal Growth Factor Receptor-Tyrosine Kinase (EGFR-TK) [C] . La Ode Aman, Widisusanti Abdulkadir, Julitha Geybie Rembet, International Conference on Computation for Science and Technology . 2015

机译：喹唑啉衍生物作为表皮生长因子受体 - 酪氨酸激酶（EGFR-TK）抑制剂的QSAR研究
5. Roles of the kinase domain in epidermal growth factor receptor signaling: Comparison of wild type and kinase-impaired mutant receptor function. [D] . Ewald, Jonathan Andrew. 2001

机译：激酶结构域在表皮生长因子受体信号传导中的作用：比较野生型和激酶受损的突变受体功能。
6. Structural analysis of p185c-neu and epidermal growth factor receptor tyrosine kinases: oligomerization of kinase domains. [O] . R Murali, P J Brennan, T Kieber-Emmons, 1996

机译：p185c-neu和表皮生长因子受体酪氨酸激酶的结构分析：激酶域的寡聚。
7. Structural analysis of p185c-neu and epidermal growth factor receptor tyrosine kinases: oligomerization of kinase domains. [O] . Murali, R, Brennan, P J, Kieber-Emmons, T, 1996

机译：p185c-neu和表皮生长因子受体酪氨酸激酶的结构分析：激酶域的寡聚。

Structural analysis of p185~c-neu and epidermal growth factor receptor tyrosine kinases: Oligomerization of kinase domains

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