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- W2024151718 abstract "The Ras proteins have been repeatedly identified as key components in a wide range of cell signalling networks. The classical Ras proteins all have at least one C-terminal lipid anchor which is essential for both their membrane localisation within the cell and their biological activity. Coarse-grained molecular dynamics simulations have, over the past few years, been established as a reliable technique for examining protein-lipid interactions, both for integral and more recently for peripheral membrane proteins. We have used this technique to examine how Ras proteins bind to a model phase-separated membrane containing cholesterol. In particular, we wish to explore how Ras proteins may cluster and what effect they have on the nature and size of lipid domains. Each of the classical Ras proteins has a farnesyl lipid anchor, but HRas and NRas may also be (reversibly) palmitoylated. We have therefore examined the effect of removing one (or in the case of HRas, both) palmitoyl tails upon their interactions with membranes." @default.
- W2024151718 created "2016-06-24" @default.
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- W2024151718 date "2013-01-01" @default.
- W2024151718 modified "2023-09-29" @default.
- W2024151718 title "Ras Proteins, Lipid Domains and Palmitoylation: Modelling the Complex Interactions between Ras Proteins and Cell Membranes" @default.
- W2024151718 doi "https://doi.org/10.1016/j.bpj.2012.11.688" @default.
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