{"gene":"MRGBP","run_date":"2026-06-10T02:59:51","timeline":{"discoveries":[{"year":2010,"finding":"MRGBP (C20orf20) is a subunit of the TRRAP/TIP60-containing histone acetyltransferase complex, and interacts with bromodomain containing 8 (BRD8) as identified by yeast two-hybrid screening and immunoprecipitation.","method":"Yeast two-hybrid screening, co-immunoprecipitation","journal":"British journal of cancer","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — yeast two-hybrid plus reciprocal IP in a single lab; interaction confirmed by two methods but no reconstitution or structural validation","pmids":["20051959"],"is_preprint":false},{"year":2018,"finding":"MRGBP promotes androgen receptor (AR)-mediated transactivation of KLK3 and TMPRSS2 in prostate cancer cells by interacting with MRG15 and TIP60; MRGBP is recruited to active gene regions via MRG15 binding to H3K4me1/3, then promotes TIP60 recruitment and acetylation of histone variant H2A.Z at AR binding regions, thereby increasing AR occupancy.","method":"Co-immunoprecipitation, ChIP assay, siRNA knockdown, gene expression analysis","journal":"Biochimica et biophysica acta. Gene regulatory mechanisms","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP and ChIP with functional readout in a single lab, two orthogonal methods","pmids":["30076933"],"is_preprint":false},{"year":2021,"finding":"MRGBP is a member of the NuA4 complex and acts as a general inhibitor of DNA double-strand break repair; its downregulation increases repair efficiency, particularly stimulating early events of homologous recombination by expanding DNA-end resection, opposing the role of the main catalytic subunits of the NuA4 complex.","method":"siRNA knockdown, DNA damage repair assays, homologous recombination assays","journal":"FEBS open bio","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — loss-of-function with defined cellular phenotype (DNA repair) and pathway placement within NuA4, single lab single study","pmids":["33354938"],"is_preprint":false},{"year":2022,"finding":"MRGBP promotes colorectal cancer EMT and metastasis by suppressing DKK1 expression (thereby activating Wnt/β-catenin signaling) and by enhancing acetylation of the NF-κB/p65 pathway; pharmacological inhibition of Wnt/β-catenin and NF-κB pathways reversed MRGBP-promoted cell processes.","method":"siRNA knockdown, overexpression, pathway inhibitor treatment, in vitro and in vivo assays","journal":"Experimental cell research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single study; mechanistic pathway placement is inferred from inhibitor rescue without direct biochemical demonstration of the molecular link","pmids":["36208716"],"is_preprint":false},{"year":2011,"finding":"siRNA-mediated knockdown of C20orf20 (MRGBP) induces apoptosis in cutaneous squamous cell carcinoma cells in vitro and reduces xenograft tumor growth in vivo, establishing a functional role for MRGBP in cancer cell survival.","method":"siRNA knockdown, apoptosis assay, xenograft tumor model","journal":"Oncogene","confidence":"Low","confidence_rationale":"Tier 3 / Weak — loss-of-function phenotype established but no molecular mechanism identified; single lab","pmids":["21602893"],"is_preprint":false}],"current_model":"MRGBP is a subunit of the NuA4/TIP60 histone acetyltransferase complex that is recruited to active chromatin through MRG15 binding to H3K4me1/3 marks, whereupon it promotes TIP60 recruitment and H2A.Z acetylation to enhance transcriptional activation (e.g., of AR target genes), while also acting as a negative regulator of DNA double-strand break repair by limiting DNA-end resection; it additionally interacts with BRD8 and engages Wnt/β-catenin and NF-κB signaling pathways to regulate cell proliferation and EMT."},"narrative":{"mechanistic_narrative":"MRGBP (C20orf20) is a subunit of the TRRAP/TIP60-containing NuA4 histone acetyltransferase complex that couples chromatin acetylation to transcriptional control and genome stability [PMID:20051959, PMID:33354938]. Within this complex it interacts with BRD8 and bridges MRG15 to TIP60: recruited to active gene regions through MRG15 recognition of H3K4me1/3, MRGBP promotes TIP60 recruitment and acetylation of the histone variant H2A.Z at androgen receptor binding regions, thereby increasing AR occupancy and transactivation of target genes such as KLK3 and TMPRSS2 [PMID:30076933]. In the context of DNA double-strand break repair, MRGBP acts as a general inhibitor that limits DNA-end resection, opposing the catalytic subunits of NuA4; its loss enhances early homologous recombination [PMID:33354938]. Functionally, MRGBP supports cancer cell survival, as its depletion induces apoptosis and reduces xenograft tumor growth [PMID:21602893].","teleology":[{"year":2010,"claim":"Established MRGBP as a physical component of the TRRAP/TIP60 acetyltransferase machinery and identified its direct binding partner BRD8, placing it within a defined chromatin-modifying complex.","evidence":"Yeast two-hybrid screening and reciprocal co-immunoprecipitation","pmids":["20051959"],"confidence":"Medium","gaps":["No reconstitution or structural validation of the interaction","Stoichiometry and architecture within the complex undefined"]},{"year":2011,"claim":"Demonstrated that MRGBP is functionally required for cancer cell survival, showing a phenotypic consequence of its loss before any molecular mechanism was known.","evidence":"siRNA knockdown with apoptosis assay and xenograft tumor model in cutaneous squamous cell carcinoma","pmids":["21602893"],"confidence":"Low","gaps":["No molecular mechanism linking knockdown to apoptosis identified","Single lab, single tumor type"]},{"year":2018,"claim":"Resolved how MRGBP is targeted to chromatin and what it does there, defining a recruitment-to-acetylation axis that drives AR-dependent transcription.","evidence":"Co-immunoprecipitation, ChIP, and siRNA knockdown with gene expression readout in prostate cancer cells","pmids":["30076933"],"confidence":"Medium","gaps":["Direct demonstration that MRGBP enzymatically enables H2A.Z acetylation versus stabilizing complex recruitment","Single lab, single cancer model"]},{"year":2021,"claim":"Revealed an unexpected role for MRGBP in genome maintenance, showing it restrains DNA-end resection and thereby acts opposite to the catalytic NuA4 subunits in DSB repair.","evidence":"siRNA knockdown with DNA damage repair and homologous recombination assays","pmids":["33354938"],"confidence":"Medium","gaps":["Molecular basis by which MRGBP limits resection unknown","Single lab, single study"]},{"year":2022,"claim":"Extended MRGBP's pro-tumorigenic function to Wnt/β-catenin and NF-κB signaling, linking it to EMT and metastasis.","evidence":"siRNA knockdown, overexpression, pathway inhibitor rescue, and in vitro/in vivo assays in colorectal cancer","pmids":["36208716"],"confidence":"Low","gaps":["Pathway placement inferred from inhibitor rescue without direct biochemical demonstration of the molecular link to DKK1 or p65","Single lab, single study"]},{"year":null,"claim":"How MRGBP's two opposing activities — promoting transcriptional acetylation versus inhibiting DSB-repair resection — are mechanistically partitioned within the same NuA4/TIP60 complex remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of MRGBP within NuA4","No biochemical reconstitution of its specific contribution to H2A.Z acetylation or resection control"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[1,2]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[1,2]}],"pathway":[{"term_id":"R-HSA-4839726","term_label":"Chromatin organization","supporting_discovery_ids":[1]},{"term_id":"R-HSA-73894","term_label":"DNA Repair","supporting_discovery_ids":[2]}],"complexes":["NuA4/TIP60 histone acetyltransferase complex"],"partners":["BRD8","MRG15","TIP60"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9NV56","full_name":"MRG/MORF4L-binding protein","aliases":["MRG-binding protein","Up-regulated in colon cancer 4","Urcc4"],"length_aa":204,"mass_kda":22.4,"function":"Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage","subcellular_location":"Nucleus","url":"https://www.uniprot.org/uniprotkb/Q9NV56/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/MRGBP","classification":"Common Essential","n_dependent_lines":1080,"n_total_lines":1208,"dependency_fraction":0.8940397350993378},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"H2AFZ","stoichiometry":0.2},{"gene":"USP7","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/MRGBP","total_profiled":1310},"omim":[{"mim_id":"611157","title":"MRG/MORF4L-BINDING PROTEIN; MRGBP","url":"https://www.omim.org/entry/611157"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"testis","ntpm":46.0}],"url":"https://www.proteinatlas.org/search/MRGBP"},"hgnc":{"alias_symbol":["FLJ10914","MRG15BP","Eaf7"],"prev_symbol":["C20orf20"]},"alphafold":{"accession":"Q9NV56","domains":[{"cath_id":"-","chopping":"32-92","consensus_level":"high","plddt":89.6921,"start":32,"end":92}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NV56","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NV56-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NV56-F1-predicted_aligned_error_v6.png","plddt_mean":65.75},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=MRGBP","jax_strain_url":"https://www.jax.org/strain/search?query=MRGBP"},"sequence":{"accession":"Q9NV56","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9NV56.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9NV56/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NV56"}},"corpus_meta":[{"pmid":"21602893","id":"PMC_21602893","title":"Integrative mRNA profiling comparing cultured primary cells with clinical samples reveals PLK1 and C20orf20 as therapeutic targets in cutaneous squamous cell carcinoma.","date":"2011","source":"Oncogene","url":"https://pubmed.ncbi.nlm.nih.gov/21602893","citation_count":60,"is_preprint":false},{"pmid":"20051959","id":"PMC_20051959","title":"C20orf20 (MRG-binding protein) as a potential therapeutic target for colorectal cancer.","date":"2010","source":"British journal of cancer","url":"https://pubmed.ncbi.nlm.nih.gov/20051959","citation_count":34,"is_preprint":false},{"pmid":"29331027","id":"PMC_29331027","title":"MiR-137 functions as a tumor suppressor in pancreatic cancer by targeting MRGBP.","date":"2018","source":"Journal of cellular biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/29331027","citation_count":29,"is_preprint":false},{"pmid":"30076933","id":"PMC_30076933","title":"MRGBP promotes AR-mediated transactivation of KLK3 and TMPRSS2 via acetylation of histone H2A.Z in prostate cancer cells.","date":"2018","source":"Biochimica et biophysica acta. Gene regulatory mechanisms","url":"https://pubmed.ncbi.nlm.nih.gov/30076933","citation_count":23,"is_preprint":false},{"pmid":"36208716","id":"PMC_36208716","title":"MRGBP promotes colorectal cancer metastasis via DKK1/Wnt/β-catenin and NF-kB/p65 pathways mediated EMT.","date":"2022","source":"Experimental cell research","url":"https://pubmed.ncbi.nlm.nih.gov/36208716","citation_count":12,"is_preprint":false},{"pmid":"28969065","id":"PMC_28969065","title":"MRGBP as a potential biomarker for the malignancy of pancreatic ductal adenocarcinoma.","date":"2017","source":"Oncotarget","url":"https://pubmed.ncbi.nlm.nih.gov/28969065","citation_count":10,"is_preprint":false},{"pmid":"33354938","id":"PMC_33354938","title":"MRGBP, a member of the NuA4 complex, inhibits DNA double-strand break repair.","date":"2021","source":"FEBS open bio","url":"https://pubmed.ncbi.nlm.nih.gov/33354938","citation_count":5,"is_preprint":false},{"pmid":"35924262","id":"PMC_35924262","title":"MRGBP: A New Factor for Diagnosis and Prediction of Head and Neck Squamous Cell Carcinoma.","date":"2022","source":"BioMed research international","url":"https://pubmed.ncbi.nlm.nih.gov/35924262","citation_count":2,"is_preprint":false},{"pmid":"38558220","id":"PMC_38558220","title":"Retraction: \"MiR-137 functions as a tumor suppressor in pancreatic cancer by targeting MRGBP\".","date":"2024","source":"Journal of cellular biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/38558220","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.07.21.665854","title":"BDF6 deficiency severely compromises intracellular amastigote development and infectivity of  <i>Trypanosoma cruzi</i>","date":"2025-07-21","source":"bioRxiv","url":"https://doi.org/10.1101/2025.07.21.665854","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6468,"output_tokens":1253,"usd":0.019099,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7883,"output_tokens":1861,"usd":0.04297,"stage2_stop_reason":"end_turn"},"total_usd":0.062069,"stage1_batch_id":"msgbatch_01BbTCMyrRPyhtEq6b1MdwCN","stage2_batch_id":"msgbatch_011dEed5bbxYvTAaQWKJevxu","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2010,\n      \"finding\": \"MRGBP (C20orf20) is a subunit of the TRRAP/TIP60-containing histone acetyltransferase complex, and interacts with bromodomain containing 8 (BRD8) as identified by yeast two-hybrid screening and immunoprecipitation.\",\n      \"method\": \"Yeast two-hybrid screening, co-immunoprecipitation\",\n      \"journal\": \"British journal of cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — yeast two-hybrid plus reciprocal IP in a single lab; interaction confirmed by two methods but no reconstitution or structural validation\",\n      \"pmids\": [\"20051959\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"MRGBP promotes androgen receptor (AR)-mediated transactivation of KLK3 and TMPRSS2 in prostate cancer cells by interacting with MRG15 and TIP60; MRGBP is recruited to active gene regions via MRG15 binding to H3K4me1/3, then promotes TIP60 recruitment and acetylation of histone variant H2A.Z at AR binding regions, thereby increasing AR occupancy.\",\n      \"method\": \"Co-immunoprecipitation, ChIP assay, siRNA knockdown, gene expression analysis\",\n      \"journal\": \"Biochimica et biophysica acta. Gene regulatory mechanisms\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and ChIP with functional readout in a single lab, two orthogonal methods\",\n      \"pmids\": [\"30076933\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"MRGBP is a member of the NuA4 complex and acts as a general inhibitor of DNA double-strand break repair; its downregulation increases repair efficiency, particularly stimulating early events of homologous recombination by expanding DNA-end resection, opposing the role of the main catalytic subunits of the NuA4 complex.\",\n      \"method\": \"siRNA knockdown, DNA damage repair assays, homologous recombination assays\",\n      \"journal\": \"FEBS open bio\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — loss-of-function with defined cellular phenotype (DNA repair) and pathway placement within NuA4, single lab single study\",\n      \"pmids\": [\"33354938\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"MRGBP promotes colorectal cancer EMT and metastasis by suppressing DKK1 expression (thereby activating Wnt/β-catenin signaling) and by enhancing acetylation of the NF-κB/p65 pathway; pharmacological inhibition of Wnt/β-catenin and NF-κB pathways reversed MRGBP-promoted cell processes.\",\n      \"method\": \"siRNA knockdown, overexpression, pathway inhibitor treatment, in vitro and in vivo assays\",\n      \"journal\": \"Experimental cell research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single study; mechanistic pathway placement is inferred from inhibitor rescue without direct biochemical demonstration of the molecular link\",\n      \"pmids\": [\"36208716\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"siRNA-mediated knockdown of C20orf20 (MRGBP) induces apoptosis in cutaneous squamous cell carcinoma cells in vitro and reduces xenograft tumor growth in vivo, establishing a functional role for MRGBP in cancer cell survival.\",\n      \"method\": \"siRNA knockdown, apoptosis assay, xenograft tumor model\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — loss-of-function phenotype established but no molecular mechanism identified; single lab\",\n      \"pmids\": [\"21602893\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"MRGBP is a subunit of the NuA4/TIP60 histone acetyltransferase complex that is recruited to active chromatin through MRG15 binding to H3K4me1/3 marks, whereupon it promotes TIP60 recruitment and H2A.Z acetylation to enhance transcriptional activation (e.g., of AR target genes), while also acting as a negative regulator of DNA double-strand break repair by limiting DNA-end resection; it additionally interacts with BRD8 and engages Wnt/β-catenin and NF-κB signaling pathways to regulate cell proliferation and EMT.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MRGBP (C20orf20) is a subunit of the TRRAP/TIP60-containing NuA4 histone acetyltransferase complex that couples chromatin acetylation to transcriptional control and genome stability [#0, #2]. Within this complex it interacts with BRD8 and bridges MRG15 to TIP60: recruited to active gene regions through MRG15 recognition of H3K4me1/3, MRGBP promotes TIP60 recruitment and acetylation of the histone variant H2A.Z at androgen receptor binding regions, thereby increasing AR occupancy and transactivation of target genes such as KLK3 and TMPRSS2 [#1]. In the context of DNA double-strand break repair, MRGBP acts as a general inhibitor that limits DNA-end resection, opposing the catalytic subunits of NuA4; its loss enhances early homologous recombination [#2]. Functionally, MRGBP supports cancer cell survival, as its depletion induces apoptosis and reduces xenograft tumor growth [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"Established MRGBP as a physical component of the TRRAP/TIP60 acetyltransferase machinery and identified its direct binding partner BRD8, placing it within a defined chromatin-modifying complex.\",\n      \"evidence\": \"Yeast two-hybrid screening and reciprocal co-immunoprecipitation\",\n      \"pmids\": [\"20051959\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No reconstitution or structural validation of the interaction\", \"Stoichiometry and architecture within the complex undefined\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Demonstrated that MRGBP is functionally required for cancer cell survival, showing a phenotypic consequence of its loss before any molecular mechanism was known.\",\n      \"evidence\": \"siRNA knockdown with apoptosis assay and xenograft tumor model in cutaneous squamous cell carcinoma\",\n      \"pmids\": [\"21602893\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No molecular mechanism linking knockdown to apoptosis identified\", \"Single lab, single tumor type\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Resolved how MRGBP is targeted to chromatin and what it does there, defining a recruitment-to-acetylation axis that drives AR-dependent transcription.\",\n      \"evidence\": \"Co-immunoprecipitation, ChIP, and siRNA knockdown with gene expression readout in prostate cancer cells\",\n      \"pmids\": [\"30076933\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct demonstration that MRGBP enzymatically enables H2A.Z acetylation versus stabilizing complex recruitment\", \"Single lab, single cancer model\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Revealed an unexpected role for MRGBP in genome maintenance, showing it restrains DNA-end resection and thereby acts opposite to the catalytic NuA4 subunits in DSB repair.\",\n      \"evidence\": \"siRNA knockdown with DNA damage repair and homologous recombination assays\",\n      \"pmids\": [\"33354938\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular basis by which MRGBP limits resection unknown\", \"Single lab, single study\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Extended MRGBP's pro-tumorigenic function to Wnt/\\u03b2-catenin and NF-\\u03baB signaling, linking it to EMT and metastasis.\",\n      \"evidence\": \"siRNA knockdown, overexpression, pathway inhibitor rescue, and in vitro/in vivo assays in colorectal cancer\",\n      \"pmids\": [\"36208716\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Pathway placement inferred from inhibitor rescue without direct biochemical demonstration of the molecular link to DKK1 or p65\", \"Single lab, single study\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How MRGBP's two opposing activities — promoting transcriptional acetylation versus inhibiting DSB-repair resection — are mechanistically partitioned within the same NuA4/TIP60 complex remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structural model of MRGBP within NuA4\", \"No biochemical reconstitution of its specific contribution to H2A.Z acetylation or resection control\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-4839726\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-73894\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\"NuA4/TIP60 histone acetyltransferase complex\"],\n    \"partners\": [\"BRD8\", \"MRG15\", \"TIP60\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}