{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fang Z"],"funding":["Cancer Research Society","Princess Margaret Cancer Foundation","Canadian Cancer Society Research Institute"],"pagination":["15641-52"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4957048"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["291(30)"],"pubmed_abstract":["RAS-like protein expressed in many tissues 1 (RIT1) is a disease-associated RAS subfamily small guanosine triphosphatase (GTPase). Recent studies revealed that germ-line and somatic RIT1 mutations can cause Noonan syndrome (NS), and drive proliferation of lung adenocarcinomas, respectively, akin to RAS mutations in these diseases. However, the locations of these RIT1 mutations differ significantly from those found in RAS, and do not affect the three mutational \"hot spots\" of RAS. Moreover, few studies have characterized the GTPase cycle of RIT1 and its disease-associated mutants. Here we developed a real-time NMR-based GTPase assay for RIT1 and investigated the effect of disease-associated mutations on GTPase cycle. RIT1 exhibits an intrinsic GTP hydrolysis rate similar to that of H-RAS, b"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Biochemical Classification of Disease-associated Mutants of RAS-like Protein Expressed in Many Tissues (RIT1)."],"pmcid":["PMC4957048"],"funding_grant_id":["703209","14014"],"pubmed_authors":["Yin JC","Smith MJ","Fang Z","Mazhab-Jafari MT","Nishikawa T","Gasmi-Seabrook GM","Neel BG","Ikura M","Marshall CB","Xu Y"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical Classification of Disease-associated Mutants of RAS-like Protein Expressed in Many Tissues (RIT1).","description":"RAS-like protein expressed in many tissues 1 (RIT1) is a disease-associated RAS subfamily small guanosine triphosphatase (GTPase). Recent studies revealed that germ-line and somatic RIT1 mutations can cause Noonan syndrome (NS), and drive proliferation of lung adenocarcinomas, respectively, akin to RAS mutations in these diseases. However, the locations of these RIT1 mutations differ significantly from those found in RAS, and do not affect the three mutational \"hot spots\" of RAS. Moreover, few studies have characterized the GTPase cycle of RIT1 and its disease-associated mutants. Here we developed a real-time NMR-based GTPase assay for RIT1 and investigated the effect of disease-associated mutations on GTPase cycle. RIT1 exhibits an intrinsic GTP hydrolysis rate similar to that of H-RAS, b","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jul","modification":"2025-04-22T18:43:02.084Z","creation":"2019-03-27T02:18:56Z"},"accession":"S-EPMC4957048","cross_references":{"pubmed":["27226556"],"doi":["10.1074/jbc.M116.714196","10.1074/jbc.m116.714196"]}}