{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe set of abstracts provided primarily focuses on the roles of methionine sulfoxide reductases (Msrs) in protecting cells against oxidative stress by repairing oxidized methionine residues. For example, one study describes how the mitochondrial MsrB2 is released from damaged mitochondria to initiate mitophagy via Parkin activation and LC3 interactions, thereby reducing apoptosis and contributing to cellular homeostasis in conditions such as diabetes mellitus and Parkinson’s disease."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " \n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOther reports detail the broad functions of the Msr system. One investigation identified methionine‐rich proteins and monitored the oxidation state of Met residues, demonstrating that both MsrA and MsrB enzymes are critical for reducing protein Met sulfoxides via thioredoxin and glutaredoxin pathways."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " In related studies, overexpression of these enzymes in yeast and Drosophila provided significant protection against oxidative stress and exerted beneficial effects on cell survival and lifespan, although the two Msr isoforms appeared to have distinct impacts on aging."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurthermore, insights from structural and functional analyses revealed that MsrB2—a mitochondrial, β‐strand rich, globular protein whose catalytic mechanism notably lacks a resolving cysteine—is structurally more similar to bacterial counterparts than to the cytosolic MsrB1."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " In models of Alzheimer’s disease, MsrB2 was also shown to attenuate amyloidogenic processes and Tau phosphorylation via modulation of JNK/ERK signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": " Notably, however, none of these studies provide any information on FAM236D. Thus, while these abstracts collectively offer a detailed picture of the antioxidant and regulatory functions of Msr proteins in diverse tissue contexts, they do not currently shed light on the role or function of FAM236D. Future studies will be needed to determine whether FAM236D might intersect with these redox-regulatory pathways or serve other cellular functions.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Seung Hee Lee, Suho Lee, Jing Du, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial MsrB2 serves as a switch and transducer for mitophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO Mol Med (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/emmm.201910409"}], "href": "https://doi.org/10.15252/emmm.201910409"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31282614"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31282614"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Dung Tien Le, Xinwen Liang, Dmitri E Fomenko, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Overexpression of methionine-R-sulfoxide reductases has no influence on fruit fly aging."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mech Ageing Dev (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.mad.2009.04.003"}], "href": "https://doi.org/10.1016/j.mad.2009.04.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19409408"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19409408"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Finn L Aachmann, Geun-Hee Kwak, Rebecca Del Conte, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proteins (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/prot.23141"}], "href": "https://doi.org/10.1002/prot.23141"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21989933"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21989933"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Hwa-Young Kim "}, {"type": "b", "children": [{"type": "t", "text": "Glutaredoxin serves as a reductant for methionine sulfoxide reductases with or without resolving cysteine."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Acta Biochim Biophys Sin (Shanghai) (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/abbs/gms038"}], "href": "https://doi.org/10.1093/abbs/gms038"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22634633"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22634633"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Xiao-Jiao Xiang, Li Song, Xiao-Juan Deng, et al. 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