{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Scietti L"],"funding":["Giovanni Armenise-Harvard Foundation","Mizutani Foundation for Glycoscience","Ministero Dell’Istruzione, dell’Università e Della Ricerca","European Commission","Associazione Italiana per la Ricerca Sul Cancro"],"pagination":["876352"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9453210"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9"],"pubmed_abstract":["Multifunctional human collagen lysyl hydroxylase (LH/PLOD) enzymes catalyze post-translational hydroxylation and subsequent glycosylation of collagens, enabling their maturation and supramolecular organization in the extracellular matrix (ECM). Recently, the overexpression of LH/PLODs in the tumor microenvironment results in abnormal accumulation of these collagen post-translational modifications, which has been correlated with increased metastatic progression of a wide variety of solid tumors. These observations make LH/PLODs excellent candidates for prospective treatment of aggressive cancers. The recent years have witnessed significant research efforts to facilitate drug discovery on LH/PLODs, including molecular structure characterizations and development of reliable high-throughput en"],"journal":["Frontiers in molecular biosciences"],"pubmed_title":["A Fe<sup>2+</sup>-dependent self-inhibited state influences the druggability of human collagen lysyl hydroxylase (LH/PLOD) enzymes."],"pmcid":["PMC9453210"],"funding_grant_id":["to FF","H2020-MSCA-IF COTETHERS (n. 745934) to AC","200039 to FF","MFAG 20075 to FF"],"pubmed_authors":["Fumagalli M","De Giorgi F","Mattoteia D","Chiapparino A","Faravelli S","Colombo G","Forneris F","Moroni E","Negro L","De Marco M","Scietti L","Serapian SA"],"additional_accession":[]},"is_claimable":false,"name":"A Fe<sup>2+</sup>-dependent self-inhibited state influences the druggability of human collagen lysyl hydroxylase (LH/PLOD) enzymes.","description":"Multifunctional human collagen lysyl hydroxylase (LH/PLOD) enzymes catalyze post-translational hydroxylation and subsequent glycosylation of collagens, enabling their maturation and supramolecular organization in the extracellular matrix (ECM). Recently, the overexpression of LH/PLODs in the tumor microenvironment results in abnormal accumulation of these collagen post-translational modifications, which has been correlated with increased metastatic progression of a wide variety of solid tumors. These observations make LH/PLODs excellent candidates for prospective treatment of aggressive cancers. The recent years have witnessed significant research efforts to facilitate drug discovery on LH/PLODs, including molecular structure characterizations and development of reliable high-throughput en","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-05-28T05:41:08.108Z","creation":"2025-02-19T04:38:59.664Z"},"accession":"S-EPMC9453210","cross_references":{"pubmed":["36090047"],"doi":["10.3389/fmolb.2022.876352"]}}