{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Manjasetty BA"],"funding":["National Institute of Allergy and Infectious Diseases","NIAID NIH HHS","Department of Health and Human Services","U.S. Department of Energy, Office of Biological and Environmental Research","National Institutes of Health"],"pagination":["537-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4796704"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_abstract":["The fluorescence-based thermal shift (FTS) data presented here include Table S1 and Fig. S1, and are supplemental to our original research article describing detailed structural, FTS, and fluorescence polarization analyses of the Salmonella enterica subsp. entrica serovar Typhimurium str. LT2 multidrug transcriptional regulator AcrR (StAcrR) (doi:10.1016/j.jsb.2016.01.008) (Manjasetty et al., 2015 [1]). Table S1 contains chemical formulas, a Chemical Abstracts Service (CAS) Registry Number (CAS no.), FTS rank (a ligand with the highest rank) has the largest difference in the melting temperature (ΔT m), and uses as drug molecules against various pathological conditions of sixteen small-molecule ligands that increase thermal stability of StAcrR. Thermal stability of human enolase 1, a negati"],"journal":["Data in brief"],"pubmed_title":["Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2."],"pmcid":["PMC4796704"],"funding_grant_id":["HHSN272201200026C","DE-AC02-06CH11357","HHSN272200700058C"],"pubmed_authors":["Halavaty AS","Joachimiak A","Manjasetty BA","Luan CH","Anderson WF","Mulligan R","Kwon K","Osipiuk J"],"additional_accession":[]},"is_claimable":false,"name":"Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2.","description":"The fluorescence-based thermal shift (FTS) data presented here include Table S1 and Fig. S1, and are supplemental to our original research article describing detailed structural, FTS, and fluorescence polarization analyses of the Salmonella enterica subsp. entrica serovar Typhimurium str. LT2 multidrug transcriptional regulator AcrR (StAcrR) (doi:10.1016/j.jsb.2016.01.008) (Manjasetty et al., 2015 [1]). Table S1 contains chemical formulas, a Chemical Abstracts Service (CAS) Registry Number (CAS no.), FTS rank (a ligand with the highest rank) has the largest difference in the melting temperature (ΔT m), and uses as drug molecules against various pathological conditions of sixteen small-molecule ligands that increase thermal stability of StAcrR. Thermal stability of human enolase 1, a negati","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jun","modification":"2025-04-04T22:50:00.01Z","creation":"2019-03-27T02:11:22Z"},"accession":"S-EPMC4796704","cross_references":{"pubmed":["27054155"],"doi":["10.1016/j.dib.2016.03.003"]}}