{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Van QN"],"funding":["NCRR NIH HHS","DOE | NNSA | Los Alamos National Laboratory","HHS | National Institutes of Health","CCR NIH HHS","U.S. Department of Energy","DOE | LDRD | Oak Ridge National Laboratory","DOE | LDRD | Argonne National Laboratory","HHS | NIH | National Cancer Institute","DOE | LDRD | Lawrence Livermore National Laboratory","NCI NIH HHS","U.S. Department of Commerce","NIGMS NIH HHS","National Science Foundation"],"pagination":["24258-24268"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7533834"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["117(39)"],"pubmed_abstract":["The small GTPase KRAS is localized at the plasma membrane where it functions as a molecular switch, coupling extracellular growth factor stimulation to intracellular signaling networks. In this process, KRAS recruits effectors, such as RAF kinase, to the plasma membrane where they are activated by a series of complex molecular steps. Defining the membrane-bound state of KRAS is fundamental to understanding the activation of RAF kinase and in evaluating novel therapeutic opportunities for the inhibition of oncogenic KRAS-mediated signaling. We combined multiple biophysical measurements and computational methodologies to generate a consensus model for authentically processed, membrane-anchored KRAS. In contrast to the two membrane-proximal conformations previously reported, we identify a thi"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane."],"pmcid":["PMC7533834"],"funding_grant_id":["S10 RR028438","P50 GM085273","DE-AC52-07NA27344","JDACS4C","DE-AC05-00OR22725","S10 RR029220","S10RR023438","HHSN261200800001E","S10RR08438","S10 RR025062","DMB-8415048","HHSN261200800001C","P50GM085273","S10 RR002781","P41 GM103399","P41GM103399","S10RR025062","S10 RR023438","S10RR029220","OIA-9977486","DE-AC02-06-CH11357","S10RR02781","S10 RR008438","P41 GM103422","DE-AC5206NA25396","BIR-9214394","70NANB17H299","P41GM103422"],"pubmed_authors":["Ramanathan A","Scott D","Tonelli M","Taylor T","Alexander P","Ye X","Lopez CA","Chertov O","Van QN","Bhowmik D","Gillette WK","Losche M","Nissley DV","Stephen AG","Esposito D","Simanshu DK","Niu B","McCormick F","Gnanakaran S","Heinrich F","Messing S","Stanley CB","Drew M","Westler WM","Tran TH","Gross ML","Markley JL","Frank PH","Hengartner NW"],"additional_accession":[]},"is_claimable":false,"name":"Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane.","description":"The small GTPase KRAS is localized at the plasma membrane where it functions as a molecular switch, coupling extracellular growth factor stimulation to intracellular signaling networks. In this process, KRAS recruits effectors, such as RAF kinase, to the plasma membrane where they are activated by a series of complex molecular steps. Defining the membrane-bound state of KRAS is fundamental to understanding the activation of RAF kinase and in evaluating novel therapeutic opportunities for the inhibition of oncogenic KRAS-mediated signaling. We combined multiple biophysical measurements and computational methodologies to generate a consensus model for authentically processed, membrane-anchored KRAS. In contrast to the two membrane-proximal conformations previously reported, we identify a thi","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Sep","modification":"2026-04-29T06:26:07.526Z","creation":"2021-03-12T08:19:05Z"},"accession":"S-EPMC7533834","cross_references":{"pubmed":["32913056"],"doi":["10.1073/pnas.2006504117"]}}