Titlebook: KRAS; Methods and Protocol Andrew G. Stephen,Dominic Esposito Book 2024 Leios Biomedical Research, Inc. 2024 GTPase activity.mass spectrome

Pessimistic

書目名稱KRAS影響因子(影響力)




書目名稱KRAS影響因子(影響力)學(xué)科排名




書目名稱KRAS網(wǎng)絡(luò)公開度




書目名稱KRAS網(wǎng)絡(luò)公開度學(xué)科排名




書目名稱KRAS被引頻次




書目名稱KRAS被引頻次學(xué)科排名




書目名稱KRAS年度引用




書目名稱KRAS年度引用學(xué)科排名




書目名稱KRAS讀者反饋




書目名稱KRAS讀者反饋學(xué)科排名

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Book 2024 novel molecules that bind KRAS in live cells. Chapters focus on protein production and characterization, biochemical assays, cell-based assays, KRAS-membrane interactions, targeting KRAS, and cell models. Written in the highly successful?.Methods in Molecular Biology.?series format, chapters includ

向外

Book 2024d key tips on troubleshooting and avoiding known pitfalls...?..Authoritative and cutting-edge,?.KRAS: Methods and Protocols .aims to provide methods that will be instrumental in the development of future clinically approved KRAS therapeutics..

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草率女

Studying RAS Interactions in Live Cells with BRET,RAF1 binding to active RAS, exhibits nonspecific interactions. The assay exhibits remarkable signal-to-background ratios and is highly suitable for investigating the interactions of RAS with effectors, as well as for high-throughput screening assays.

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Considerations Around Structure-Based Drug Discovery for KRAS Using DOCK,for prosecuting a virtual screen: protein structure choice, pocket selection, optimization of the scoring function, modification of sampling spheres and sampling procedures, choosing an appropriate portion of chemical space to dock, and the choice of which top scoring molecules to pick for purchase.

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The Abundance of KRAS and RAS Gene Mutations in Cancer,imate . mutations occur in 11–14% of all human cancers. Although these estimates are lower than many commonly encountered values, these estimates continue to rank . and the ensemble of . oncogenes among the most common genetic drivers of cancer across all forms of malignancy.

哥哥噴涌而出

Measurement of KRAS-GTPase Activity,olysis. Here we describe a biochemical assay that measures the release of free phosphate upon hydrolysis of the GTP nucleotide and allows the measurement of intrinsic or GAP-stimulated GTP hydrolysis by KRAS. This assay can be used to measure GTPase activity under single turnover conditions.