Structural and biophysical properties of farnesylated KRas interacting with the chaperone SmgGDS-558
Author:
Funder
National Institutes of Health
National Cancer Institute
U.S. Department of Commerce
Publisher
Elsevier BV
Subject
Biophysics
Reference76 articles.
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3. Blocking K-Ras interaction with the plasma membrane is a tractable therapeutic approach to inhibit oncogenic K-Ras activity;Henkels;Front. Mol. Biosci.,2021
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Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. GTPase splice variants RAC1 and RAC1B display isoform-specific differences in localization, prenylation, and interaction with the chaperone protein SmgGDS;Journal of Biological Chemistry;2023-06
2. Biophysics of cancer;Biophysical Journal;2022-10
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