<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>15(2)</volume><submitter>Bunimov N</submitter><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</pubmed_abstract><journal>Cellular &amp; molecular biology letters</journal><pagination>196-214</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6275937</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Characterization of proteins associating with 5' terminus of PGHS-1 mRNA.</pubmed_title><pmcid>PMC6275937</pmcid><pubmed_authors>Laneuville O</pubmed_authors><pubmed_authors>Bunimov N</pubmed_authors></additional><is_claimable>false</is_claimable><name>Characterization of proteins associating with 5' terminus of PGHS-1 mRNA.</name><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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Jun</publication><modification>2026-05-06T00:32:47.602Z</modification><creation>2025-05-18T13:35:11.282Z</creation></dates><accession>S-EPMC6275937</accession><cross_references><pubmed>20112001</pubmed><doi>10.2478/s11658-010-0005-5</doi></cross_references></HashMap>