Structures of the HER2–HER3–NRG1β complex reveal a dynamic dimer interface

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Structures of the active HER2/HER3 receptor complex reveal dynamics at the dimerization interface induced by binding of a single ligand

Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes - ScienceDirect

Her2 activation mechanism reflects evolutionary preservation of

Her2 activation mechanism reflects evolutionary preservation of

The fixed extended conformation of ErbB2 precludes formation of

Q-score analysis of the cryo-EM maps and a structural comparison

EMDB < EMD-23917

Purification, characterization, and reconstruction of the near

加州大学研究者首次解析HER2/HER3异源二聚体结构_北京华大蛋白质研发

Structures of the HER2–HER3–NRG1β complex reveal a dynamic dimer

The sErbB4:Nrg1β structure. Orthogonal views of a worm diagram of

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