{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mavor D"],"funding":["National Institute of Neurological Disorders and Stroke","NIBIB NIH HHS","School of Pharmacy, University of California, San Francisco","Howard Hughes Medical Institute","NIAID NIH HHS","Paul F. Glenn Center for Aging Research","University of California, San Francisco","National Institutes of Health","Paul G. Allen Family Foundation","National Institute of General Medical Sciences","School of Medicine, University of California, San Francisco","Chan Zuckerberg Biohub","NCI NIH HHS","NINDS NIH HHS","NIGMS NIH HHS","National Institute of Biomedical Imaging and Bioengineering","NIH HHS","National Science Foundation"],"pagination":["bio036103"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6078352"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(7)"],"pubmed_abstract":["Although the primary protein sequence of ubiquitin (Ub) is extremely stable over evolutionary time, it is highly tolerant to mutation during selection experiments performed in the laboratory. We have proposed that this discrepancy results from the difference between fitness under laboratory culture conditions and the selective pressures in changing environments over evolutionary timescales. Building on our previous work (Mavor et al., 2016), we used deep mutational scanning to determine how twelve new chemicals (3-Amino-1,2,4-triazole, 5-fluorocytosine, Amphotericin B, CaCl<sub>2</sub>, Cerulenin, Cobalt Acetate, Menadione, Nickel Chloride, p-Fluorophenylalanine, Rapamycin, Tamoxifen, and Tunicamycin) reveal novel mutational sensitivities of ubiquitin residues. Collectively, our experiment"],"journal":["Biology open"],"pubmed_title":["Extending chemical perturbations of the ubiquitin fitness landscape in a classroom setting reveals new constraints on sequence tolerance."],"pmcid":["PMC6078352"],"funding_grant_id":["R01 AI100272","AI126726","R01 GM112844","GM008284","EB009383","NS100717","DP5 OD009180","R01 GM110089","AI120464","T32 EB009383","R56 AI126726","AI100272","R01 GM117189","K99 CA181494","R01 AI120464","DP2 GM119139","GM112844","R00 CA181494","GM119139","U54 NS100717","R01 GM071801","GM110089","T32-EB009383","GM064337","GM067547","OD009180","CA181494","GM071801","T32 AI060537","T32 GM064337","T32 GM008284","T32 GM067547","56005676","MCB-1615990","GM117189"],"pubmed_authors":["Khoroshkin MS","Myers-Turnbull D","Fraser JS","Chio CM","Elledge SK","Green EM","O'Conchuir S","Kang E","Dai SA","Kenner LR","Natale AM","Chen W","Tsai MK","Bergman ID","Tibble RW","Thorn KS","Bauer DP","Wu TS","Li J","Kern N","Rohweder PJ","Helsell CVM","Redding S","Tan SK","Arhar T","Birman Y","Reder GK","Nelson CA","Lou K","Madhani HD","Town JP","Brunetti RM","Marin WM","McTigue PF","Poss EM","Hendel NL","Thomas PV","Kampmann M","Barlow KA","Kirkemo LL","Morinishi LS","Schwarz DMC","Bolon DN","Lewis GR","Asarnow D","Rettko NJ","DeRisi JL","Ugur FS","Wolff AM","Wassarman DR","Maxwell AM","Kortemme T","Mavor D","Suresh P","Ary BE","Dickinson MS","Bogdanoff D","Oltion K","Swaney DL","Tian R","Mensa B","Pourmal S","Britain D","Nagy TL","Chow ED"],"additional_accession":[]},"is_claimable":false,"name":"Extending chemical perturbations of the ubiquitin fitness landscape in a classroom setting reveals new constraints on sequence tolerance.","description":"Although the primary protein sequence of ubiquitin (Ub) is extremely stable over evolutionary time, it is highly tolerant to mutation during selection experiments performed in the laboratory. We have proposed that this discrepancy results from the difference between fitness under laboratory culture conditions and the selective pressures in changing environments over evolutionary timescales. Building on our previous work (Mavor et al., 2016), we used deep mutational scanning to determine how twelve new chemicals (3-Amino-1,2,4-triazole, 5-fluorocytosine, Amphotericin B, CaCl<sub>2</sub>, Cerulenin, Cobalt Acetate, Menadione, Nickel Chloride, p-Fluorophenylalanine, Rapamycin, Tamoxifen, and Tunicamycin) reveal novel mutational sensitivities of ubiquitin residues. Collectively, our experiment","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jul","modification":"2026-05-04T13:27:04.431Z","creation":"2019-03-26T23:50:32Z"},"accession":"S-EPMC6078352","cross_references":{"pubmed":["30037883"],"doi":["10.1242/bio.036103"]}}