Biochemical and Structural Studies of the Interaction between ARAP1 and CIN85.
Biochemistry. 2018 Apr 10;57(14):2132-2139. doi:10.1021/acs.biochem.8b00057. Epub 2018 Mar 28
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摘要
interaction were critical for ARAP1 binding specificity. Finally, our competitive analytical gel-filtration chromatography and isothermal titration calorimetry (ITC) results showed that ARAP1 could compete with Cbl for CIN85 binding, which provides a biochemical basis for the regulatory roles of ARAP1 in the CIN85-mediated EGFR internalizing process.
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基因功能
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原始数据
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文献解读
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