{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Khoury G"],"funding":["amfAR, The Foundation for AIDS Research","National Health and Medical Research Council","Office of AIDS Research"],"pagination":["36"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5948896"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["<h4>Background</h4>Different classes of latency reversing agents (LRAs) are being evaluated to measure their effects in reactivating HIV replication from latently infected cells. A limited number of studies have demonstrated additive effects of LRAs with the viral protein Tat in initiating transcription, but less is known about how LRAs interact with Tat, particularly through basic residues that may be post-translationally modified to alter the behaviour of Tat for processive transcription and co-transcriptional RNA processing.<h4>Results</h4>Here we show that various lysine and arginine mutations reduce the capacity of Tat to induce both transcription and mRNA splicing. The lysine 28 and lysine 50 residues of Tat, or the acetylation and methylation modifications of these basic amino acids"],"journal":["Retrovirology"],"pubmed_title":["HIV latency reversing agents act through Tat post translational modifications."],"pmcid":["PMC5948896"],"funding_grant_id":["DARE U19 AI096109","APP1129320","APP1052979"],"pubmed_authors":["Anderson JL","Khoury G","Mota TM","Li S","Lewin SR","Jacobson J","Harty L","Tumpach C","Lee MY","Purcell DFJ"],"additional_accession":[]},"is_claimable":false,"name":"HIV latency reversing agents act through Tat post translational modifications.","description":"<h4>Background</h4>Different classes of latency reversing agents (LRAs) are being evaluated to measure their effects in reactivating HIV replication from latently infected cells. A limited number of studies have demonstrated additive effects of LRAs with the viral protein Tat in initiating transcription, but less is known about how LRAs interact with Tat, particularly through basic residues that may be post-translationally modified to alter the behaviour of Tat for processive transcription and co-transcriptional RNA processing.<h4>Results</h4>Here we show that various lysine and arginine mutations reduce the capacity of Tat to induce both transcription and mRNA splicing. The lysine 28 and lysine 50 residues of Tat, or the acetylation and methylation modifications of these basic amino acids","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 May","modification":"2025-04-22T01:35:35.891Z","creation":"2019-03-26T23:37:51Z"},"accession":"S-EPMC5948896","cross_references":{"pubmed":["29751762"],"doi":["10.1186/s12977-018-0421-6"]}}