{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["15(2)"],"submitter":["Bunimov N"],"pubmed_abstract":["Induction of Prostaglandin Endoperoxide H Synthase-1 (PGHS-1) gene has been previously documented in a few studies during events such as development and cellular differentiation. However, molecular mechanisms governing the regulation of PGHS-1 gene expression and contributing to changes in protein levels are poorly understood. Using the MEG-01 cell model of PGHS-1 gene induction, our laboratory has previously demonstrated that the 5'UTR and the first two exons of PGHS-1 mRNA had a significant impact on decreasing the translational efficiency of a reporter gene and suggested that the presence of a secondary structure is required for conservation of this activity. This 5'end of PGHS-1 mRNA sequence has also been shown to associate with nucleolin protein. In the current study, we set to inves"],"journal":["Cellular & molecular biology letters"],"pagination":["196-214"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6275937"],"repository":["biostudies-literature"],"pubmed_title":["Characterization of proteins associating with 5' terminus of PGHS-1 mRNA."],"pmcid":["PMC6275937"],"pubmed_authors":["Laneuville O","Bunimov N"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of proteins associating with 5' terminus of PGHS-1 mRNA.","description":"Induction of Prostaglandin Endoperoxide H Synthase-1 (PGHS-1) gene has been previously documented in a few studies during events such as development and cellular differentiation. However, molecular mechanisms governing the regulation of PGHS-1 gene expression and contributing to changes in protein levels are poorly understood. Using the MEG-01 cell model of PGHS-1 gene induction, our laboratory has previously demonstrated that the 5'UTR and the first two exons of PGHS-1 mRNA had a significant impact on decreasing the translational efficiency of a reporter gene and suggested that the presence of a secondary structure is required for conservation of this activity. This 5'end of PGHS-1 mRNA sequence has also been shown to associate with nucleolin protein. In the current study, we set to inves","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Jun","modification":"2026-05-06T00:32:47.602Z","creation":"2025-05-18T13:35:11.282Z"},"accession":"S-EPMC6275937","cross_references":{"pubmed":["20112001"],"doi":["10.2478/s11658-010-0005-5"]}}