{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMETTL7B, the protein underlying TMT1B activity, has been shown to function as an S‐adenosyl-L-methionine–dependent small molecule methyltransferase that catalyzes the methylation of alkyl thiols. Detailed biochemical studies demonstrated that METTL7B transfers a methyl group to substrates such as hydrogen sulfide, captopril, and other exogenous thiol compounds, with its activity being competitively inhibited by S-adenosyl-L-homocysteine and abolished by mutation of a key active site residue. This catalytic function extends to the methylation of thiol-based anticancer agents, thereby impacting their efficacy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn various cancer contexts, METTL7B has emerged as an important regulator of tumor progression and therapeutic resistance. In lung adenocarcinoma, enhanced METTL7B expression is implicated in resistance to EGFR-tyrosine kinase inhibitors, suggesting that its modulation may reverse drug resistance. Similarly, in thyroid cancers, including papillary thyroid carcinoma, elevated METTL7B promotes migratory and invasive capacities—likely through facilitating epithelial–mesenchymal transition—and is subject to regulation by noncoding RNAs. Moreover, increased METTL7B expression has been associated with glioma progression and glioblastoma cell proliferation, further underscoring its role as a potential prognostic marker and therapeutic target in solid tumors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in oncogenesis, METTL7B influences metabolic and immune processes. In hepatic cells, upregulation of METTL7B by bioactive compounds such as low-molecular-weight citrus pectin is linked to reduced lipid accumulation through the enhanced expression of catabolic enzymes, suggesting a protective role in nonalcoholic fatty liver pathology. In addition, in the context of sepsis, METTL7B expression in macrophages modulates the production of inflammatory cytokines and macrophage polarization, highlighting its potential as a diagnostic and therapeutic target in inflammatory conditions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nComplementary investigations into glioma biology have also begun to uncover complex regulatory networks involving noncoding RNAs, emphasizing the multifaceted molecular landscape in which METTL7B operates and reinforcing the need to further elucidate its interactions with other genomic regulators in cancer pathogenesis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Benjamin J Maldonato, Drake A Russell, Rheem A Totah "}, {"type": "b", "children": [{"type": "t", "text": "Human METTL7B is an alkyl thiol methyltransferase that metabolizes hydrogen sulfide and captopril."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-021-84218-5"}], "href": "https://doi.org/10.1038/s41598-021-84218-5"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33649426"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33649426"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Robert W Robey, Christina M Fitzsimmons, Wilfried M Guiblet, et al. 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