{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12(3)"],"submitter":["Stefanovic B"],"funding":["Florida Department of Health"],"pubmed_abstract":["Fibrosis is a major medical problem caused by excessive synthesis of the extracellular matrix, composed predominantly of type I collagen, in various tissues. There are no approved antifibrotic drugs, and the major obstacle in finding clinically relevant compounds is the lack of specificity of current experimental drugs for type I collagen. Here we describe the discovery of a lead compound that specifically inhibited secretion of type I collagen by fibroblasts in culture at IC<sub>50</sub> = 4.5 μM. The inhibition was specific for type I collagen, because secretion of fibronectin was not affected. In vitro, the compound inhibited binding of LARP6, the master regulator of translation of type I collagen mRNAs, to the 5' stem-loop sequence element which regulates their translation. Because bin"],"journal":["ACS medicinal chemistry letters"],"pagination":["477-484"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7958148"],"repository":["biostudies-literature"],"pubmed_title":["Discovery of a Lead Compound for Specific Inhibition of Type I Collagen Production in Fibrosis."],"pmcid":["PMC7958148"],"pubmed_authors":["Stefanovic B","Nefzi A","Michaels HA"],"additional_accession":[]},"is_claimable":false,"name":"Discovery of a Lead Compound for Specific Inhibition of Type I Collagen Production in Fibrosis.","description":"Fibrosis is a major medical problem caused by excessive synthesis of the extracellular matrix, composed predominantly of type I collagen, in various tissues. There are no approved antifibrotic drugs, and the major obstacle in finding clinically relevant compounds is the lack of specificity of current experimental drugs for type I collagen. Here we describe the discovery of a lead compound that specifically inhibited secretion of type I collagen by fibroblasts in culture at IC<sub>50</sub> = 4.5 μM. The inhibition was specific for type I collagen, because secretion of fibronectin was not affected. In vitro, the compound inhibited binding of LARP6, the master regulator of translation of type I collagen mRNAs, to the 5' stem-loop sequence element which regulates their translation. Because bin","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2025-04-04T20:50:22.435Z","creation":"2025-04-04T20:50:22.435Z"},"accession":"S-EPMC7958148","cross_references":{"pubmed":["33738075"],"doi":["10.1021/acsmedchemlett.1c00006"]}}