{"gene":"NIF3L1","run_date":"2026-04-29T11:37:56","timeline":{"discoveries":[{"year":2003,"finding":"Nif3l1 interacts with Trip15/CSN2 (a transcriptional corepressor/COP9 signalosome component), confirmed by yeast two-hybrid, pull-down assay, and coimmunoprecipitation. Nif3l1 acts as a transcriptional repressor and synergizes with Trip15/CSN2 in transcriptional repression. Enforced Nif3l1 expression enhances retinoic acid-primed neural differentiation of P19 cells, accompanied by down-regulation of Oct-3/4 and induction of Mash-1.","method":"Yeast two-hybrid, pull-down assay, epitope-tagged coimmunoprecipitation, luciferase reporter assay, sense/antisense overexpression in P19 cells","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 — multiple orthogonal methods (Y2H, pulldown, Co-IP, reporter assay, gain/loss-of-function) in a single study with defined phenotypic readouts","pmids":["12522100"],"is_preprint":false},{"year":2003,"finding":"Nif3l1 is mainly detected in the cytoplasm under basal conditions, but translocates into the nucleus during retinoic acid-primed neural differentiation of P19 cells; this nuclear translocation is enhanced by enforced expression of Trip15/CSN2.","method":"Subcellular fractionation/immunolocalization, overexpression of Trip15/CSN2 in P19 cells","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 — direct localization experiment with functional consequence (nuclear translocation linked to differentiation), single lab","pmids":["12522100"],"is_preprint":false},{"year":2003,"finding":"Human NIF3L1 interacts with itself (homodimerizes) and with a novel binding partner NIF3L1 BP1 (a 23.67 kDa protein bearing a putative leucine zipper domain). A C-terminal region of 100 amino acids of NIF3L1 BP1 is sufficient for interaction with NIF3L1. Both interactions occur in the cytoplasm of human LNCaP cells.","method":"Yeast two-hybrid screening of HeLa cDNA library, mammalian two-hybrid system, deletion analysis, cotransfection/colocalization in LNCaP cells","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 3 — Y2H confirmed by mammalian two-hybrid and deletion mapping, single lab, no in vitro reconstitution","pmids":["12951069"],"is_preprint":false},{"year":2004,"finding":"NIF3L1 forms a single polypeptide complex with WBSCR14 and four 14-3-3 isotypes in mammalian cells. This complex was identified by co-immunoprecipitation, and phosphatase treatment abrogates the WBSCR14–14-3-3 association, indicating phosphorylation-dependent interaction.","method":"Yeast two-hybrid, coimmunoprecipitation, phosphatase treatment","journal":"Human molecular genetics","confidence":"Medium","confidence_rationale":"Tier 3 — Co-IP with phosphatase validation, but NIF3L1's direct role in the complex not dissected further; single lab","pmids":["15163635"],"is_preprint":false},{"year":2000,"finding":"A GFP fusion protein of human NIF3L1 localizes to the cytoplasm, establishing the basal subcellular localization of the protein.","method":"GFP fusion protein fluorescence microscopy","journal":"Cytogenetics and cell genetics","confidence":"Medium","confidence_rationale":"Tier 3 — direct localization experiment, single method, foundational characterization paper","pmids":["11124544"],"is_preprint":false}],"current_model":"NIF3L1 is a highly conserved cytoplasmic protein that can translocate to the nucleus during neural differentiation, where it acts as a transcriptional repressor by cooperating with Trip15/CSN2 (COP9 signalosome component); it also participates in a phosphorylation-dependent complex with WBSCR14 and 14-3-3 proteins, homodimerizes, and interacts with a novel leucine-zipper-containing partner (NIF3L1 BP1) in the cytoplasm."},"narrative":{"teleology":[{"year":2000,"claim":"The subcellular localization of NIF3L1 was unknown; GFP-fusion imaging established that the protein resides in the cytoplasm under basal conditions, providing the first spatial framework for interpreting its function.","evidence":"GFP-fusion fluorescence microscopy in mammalian cells","pmids":["11124544"],"confidence":"Medium","gaps":["Single overexpression-based method; endogenous localization not confirmed by antibody staining","No functional consequence of cytoplasmic localization explored"]},{"year":2003,"claim":"NIF3L1 lacked known molecular activities; identification of Trip15/CSN2 as a binding partner and demonstration that NIF3L1 acts as a transcriptional repressor that synergizes with Trip15/CSN2 established its role in gene silencing and retinoic acid-primed neural differentiation, including Oct-3/4 down-regulation and Mash-1 induction.","evidence":"Yeast two-hybrid, pull-down, co-immunoprecipitation, luciferase reporter assays, gain- and loss-of-function in P19 cells with subcellular fractionation showing nuclear translocation during differentiation","pmids":["12522100"],"confidence":"High","gaps":["Direct DNA-binding or chromatin target sites of NIF3L1 not identified","Mechanism by which NIF3L1 represses transcription (direct vs. indirect) undefined","In vivo relevance (knockout animal) not tested"]},{"year":2003,"claim":"Whether NIF3L1 functions as a monomer or oligomer was unresolved; discovery of homodimerization and interaction with the novel leucine-zipper protein NIF3L1 BP1 in the cytoplasm revealed that NIF3L1 participates in cytoplasmic protein complexes beyond its nuclear repressor role.","evidence":"Yeast two-hybrid screen of HeLa cDNA library, mammalian two-hybrid, deletion mapping, cotransfection/colocalization in LNCaP cells","pmids":["12951069"],"confidence":"Medium","gaps":["No reciprocal endogenous co-IP or in vitro reconstitution of the dimer or NIF3L1 BP1 complex","Functional significance of homodimerization and NIF3L1 BP1 interaction not determined"]},{"year":2004,"claim":"The broader signaling context of NIF3L1 was unclear; identification of a phosphorylation-dependent ternary complex with WBSCR14 and 14-3-3 isoforms connected NIF3L1 to phospho-regulated cytoplasmic signaling.","evidence":"Co-immunoprecipitation and phosphatase treatment in mammalian cells, yeast two-hybrid","pmids":["15163635"],"confidence":"Medium","gaps":["Which kinase phosphorylates WBSCR14 or NIF3L1 to drive complex assembly is unknown","Direct versus bridged interaction between NIF3L1 and 14-3-3 not resolved","Physiological function of this ternary complex not defined"]},{"year":null,"claim":"The enzymatic or structural basis of NIF3L1's repressor activity, its direct genomic targets, and its in vivo requirement in neural development remain uncharacterized.","evidence":"","pmids":[],"confidence":"Low","gaps":["No ChIP or genome-wide target identification performed","No knockout or conditional loss-of-function animal model reported","Crystal structure or biochemical activity of the conserved NIF3 domain not determined in mammalian systems"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[1,2,4]},{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,1]}],"pathway":[{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[0]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[0]}],"complexes":[],"partners":["COPS2","NIF3L1BP1","WBSCR14","YWHAB"],"other_free_text":[]},"mechanistic_narrative":"NIF3L1 is a conserved cytoplasmic protein that functions as a transcriptional repressor and promotes neural differentiation. Under basal conditions NIF3L1 resides in the cytoplasm, where it homodimerizes and forms complexes with NIF3L1 BP1, WBSCR14, and 14-3-3 proteins in a phosphorylation-dependent manner [PMID:12951069, PMID:15163635]. During retinoic acid-induced neural differentiation, NIF3L1 translocates to the nucleus—a process enhanced by its partner Trip15/CSN2—where it represses transcription, down-regulates Oct-3/4, and induces the proneural factor Mash-1, thereby driving neuronal commitment of P19 embryonal carcinoma cells [PMID:12522100]."},"prefetch_data":{"uniprot":{"accession":"Q9GZT8","full_name":"NIF3-like protein 1","aliases":["Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 1 protein"],"length_aa":377,"mass_kda":42.0,"function":"May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation","subcellular_location":"Cytoplasm; Nucleus","url":"https://www.uniprot.org/uniprotkb/Q9GZT8/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/NIF3L1","classification":"Not Classified","n_dependent_lines":10,"n_total_lines":1208,"dependency_fraction":0.008278145695364239},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/NIF3L1","total_profiled":1310},"omim":[{"mim_id":"611965","title":"THO COMPLEX, SUBUNIT 7; THOC7","url":"https://www.omim.org/entry/611965"},{"mim_id":"605778","title":"NIF3-LIKE 1; NIF3L1","url":"https://www.omim.org/entry/605778"},{"mim_id":"605678","title":"MLX-INTERACTING PROTEIN-LIKE; MLXIPL","url":"https://www.omim.org/entry/605678"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Vesicles","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/NIF3L1"},"hgnc":{"alias_symbol":["CALS-7","MDS015"],"prev_symbol":["ALS2CR1"]},"alphafold":{"accession":"Q9GZT8","domains":[{"cath_id":"3.40.1390.30","chopping":"27-126_345-365","consensus_level":"high","plddt":97.5096,"start":27,"end":365},{"cath_id":"3.40.1390.30","chopping":"133-156_246-337","consensus_level":"high","plddt":97.9337,"start":133,"end":337},{"cath_id":"3.30.70.260","chopping":"166-238","consensus_level":"high","plddt":89.9015,"start":166,"end":238}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9GZT8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9GZT8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9GZT8-F1-predicted_aligned_error_v6.png","plddt_mean":91.75},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=NIF3L1","jax_strain_url":"https://www.jax.org/strain/search?query=NIF3L1"},"sequence":{"accession":"Q9GZT8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9GZT8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9GZT8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9GZT8"}},"corpus_meta":[{"pmid":"15163635","id":"PMC_15163635","title":"The subcellular localization of the ChoRE-binding protein, encoded by the Williams-Beuren syndrome critical region gene 14, is regulated by 14-3-3.","date":"2004","source":"Human molecular genetics","url":"https://pubmed.ncbi.nlm.nih.gov/15163635","citation_count":62,"is_preprint":false},{"pmid":"11161814","id":"PMC_11161814","title":"Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2) critical region at chromosome 2q33-q34: candidate genes for ALS2.","date":"2001","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/11161814","citation_count":41,"is_preprint":false},{"pmid":"12522100","id":"PMC_12522100","title":"The role of transcriptional corepressor Nif3l1 in early stage of neural differentiation via cooperation with Trip15/CSN2.","date":"2003","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/12522100","citation_count":27,"is_preprint":false},{"pmid":"12951069","id":"PMC_12951069","title":"Identification and characterization of NIF3L1 BP1, a novel cytoplasmic interaction partner of the NIF3L1 protein.","date":"2003","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/12951069","citation_count":17,"is_preprint":false},{"pmid":"11124544","id":"PMC_11124544","title":"Isolation and characterization of a novel human gene, NIF3L1, and its mouse ortholog, Nif3l1, highly conserved from bacteria to mammals.","date":"2000","source":"Cytogenetics and cell genetics","url":"https://pubmed.ncbi.nlm.nih.gov/11124544","citation_count":15,"is_preprint":false},{"pmid":"31934183","id":"PMC_31934183","title":"Relationship between osteoporosis and osteoarthritis based on DNA methylation.","date":"2019","source":"International journal of clinical and experimental pathology","url":"https://pubmed.ncbi.nlm.nih.gov/31934183","citation_count":12,"is_preprint":false},{"pmid":"37371576","id":"PMC_37371576","title":"The Ubiquitin-Proteasome System Participates in Sperm Surface Subproteome Remodeling during Boar Sperm Capacitation.","date":"2023","source":"Biomolecules","url":"https://pubmed.ncbi.nlm.nih.gov/37371576","citation_count":10,"is_preprint":false},{"pmid":"38585359","id":"PMC_38585359","title":"Serum biomarkers in patients with drug-resistant epilepsy: a proteomics-based analysis.","date":"2024","source":"Frontiers in neurology","url":"https://pubmed.ncbi.nlm.nih.gov/38585359","citation_count":6,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5440,"output_tokens":1275,"usd":0.017722},"stage2":{"model":"claude-opus-4-6","input_tokens":4495,"output_tokens":1493,"usd":0.0897},"total_usd":0.107422,"stage1_batch_id":"msgbatch_012ZiiCUBfB62NCTQd4Bk1Jo","stage2_batch_id":"msgbatch_01Xuqq9aUHoQouS7UVGZNStZ","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2003,\n      \"finding\": \"Nif3l1 interacts with Trip15/CSN2 (a transcriptional corepressor/COP9 signalosome component), confirmed by yeast two-hybrid, pull-down assay, and coimmunoprecipitation. Nif3l1 acts as a transcriptional repressor and synergizes with Trip15/CSN2 in transcriptional repression. Enforced Nif3l1 expression enhances retinoic acid-primed neural differentiation of P19 cells, accompanied by down-regulation of Oct-3/4 and induction of Mash-1.\",\n      \"method\": \"Yeast two-hybrid, pull-down assay, epitope-tagged coimmunoprecipitation, luciferase reporter assay, sense/antisense overexpression in P19 cells\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (Y2H, pulldown, Co-IP, reporter assay, gain/loss-of-function) in a single study with defined phenotypic readouts\",\n      \"pmids\": [\"12522100\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"Nif3l1 is mainly detected in the cytoplasm under basal conditions, but translocates into the nucleus during retinoic acid-primed neural differentiation of P19 cells; this nuclear translocation is enhanced by enforced expression of Trip15/CSN2.\",\n      \"method\": \"Subcellular fractionation/immunolocalization, overexpression of Trip15/CSN2 in P19 cells\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — direct localization experiment with functional consequence (nuclear translocation linked to differentiation), single lab\",\n      \"pmids\": [\"12522100\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"Human NIF3L1 interacts with itself (homodimerizes) and with a novel binding partner NIF3L1 BP1 (a 23.67 kDa protein bearing a putative leucine zipper domain). A C-terminal region of 100 amino acids of NIF3L1 BP1 is sufficient for interaction with NIF3L1. Both interactions occur in the cytoplasm of human LNCaP cells.\",\n      \"method\": \"Yeast two-hybrid screening of HeLa cDNA library, mammalian two-hybrid system, deletion analysis, cotransfection/colocalization in LNCaP cells\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 — Y2H confirmed by mammalian two-hybrid and deletion mapping, single lab, no in vitro reconstitution\",\n      \"pmids\": [\"12951069\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"NIF3L1 forms a single polypeptide complex with WBSCR14 and four 14-3-3 isotypes in mammalian cells. This complex was identified by co-immunoprecipitation, and phosphatase treatment abrogates the WBSCR14–14-3-3 association, indicating phosphorylation-dependent interaction.\",\n      \"method\": \"Yeast two-hybrid, coimmunoprecipitation, phosphatase treatment\",\n      \"journal\": \"Human molecular genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 — Co-IP with phosphatase validation, but NIF3L1's direct role in the complex not dissected further; single lab\",\n      \"pmids\": [\"15163635\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2000,\n      \"finding\": \"A GFP fusion protein of human NIF3L1 localizes to the cytoplasm, establishing the basal subcellular localization of the protein.\",\n      \"method\": \"GFP fusion protein fluorescence microscopy\",\n      \"journal\": \"Cytogenetics and cell genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 — direct localization experiment, single method, foundational characterization paper\",\n      \"pmids\": [\"11124544\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"NIF3L1 is a highly conserved cytoplasmic protein that can translocate to the nucleus during neural differentiation, where it acts as a transcriptional repressor by cooperating with Trip15/CSN2 (COP9 signalosome component); it also participates in a phosphorylation-dependent complex with WBSCR14 and 14-3-3 proteins, homodimerizes, and interacts with a novel leucine-zipper-containing partner (NIF3L1 BP1) in the cytoplasm.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"NIF3L1 is a conserved cytoplasmic protein that functions as a transcriptional repressor and promotes neural differentiation. Under basal conditions NIF3L1 resides in the cytoplasm, where it homodimerizes and forms complexes with NIF3L1 BP1, WBSCR14, and 14-3-3 proteins in a phosphorylation-dependent manner [PMID:12951069, PMID:15163635]. During retinoic acid-induced neural differentiation, NIF3L1 translocates to the nucleus—a process enhanced by its partner Trip15/CSN2—where it represses transcription, down-regulates Oct-3/4, and induces the proneural factor Mash-1, thereby driving neuronal commitment of P19 embryonal carcinoma cells [PMID:12522100].\",\n  \"teleology\": [\n    {\n      \"year\": 2000,\n      \"claim\": \"The subcellular localization of NIF3L1 was unknown; GFP-fusion imaging established that the protein resides in the cytoplasm under basal conditions, providing the first spatial framework for interpreting its function.\",\n      \"evidence\": \"GFP-fusion fluorescence microscopy in mammalian cells\",\n      \"pmids\": [\"11124544\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single overexpression-based method; endogenous localization not confirmed by antibody staining\",\n        \"No functional consequence of cytoplasmic localization explored\"\n      ]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"NIF3L1 lacked known molecular activities; identification of Trip15/CSN2 as a binding partner and demonstration that NIF3L1 acts as a transcriptional repressor that synergizes with Trip15/CSN2 established its role in gene silencing and retinoic acid-primed neural differentiation, including Oct-3/4 down-regulation and Mash-1 induction.\",\n      \"evidence\": \"Yeast two-hybrid, pull-down, co-immunoprecipitation, luciferase reporter assays, gain- and loss-of-function in P19 cells with subcellular fractionation showing nuclear translocation during differentiation\",\n      \"pmids\": [\"12522100\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct DNA-binding or chromatin target sites of NIF3L1 not identified\",\n        \"Mechanism by which NIF3L1 represses transcription (direct vs. indirect) undefined\",\n        \"In vivo relevance (knockout animal) not tested\"\n      ]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"Whether NIF3L1 functions as a monomer or oligomer was unresolved; discovery of homodimerization and interaction with the novel leucine-zipper protein NIF3L1 BP1 in the cytoplasm revealed that NIF3L1 participates in cytoplasmic protein complexes beyond its nuclear repressor role.\",\n      \"evidence\": \"Yeast two-hybrid screen of HeLa cDNA library, mammalian two-hybrid, deletion mapping, cotransfection/colocalization in LNCaP cells\",\n      \"pmids\": [\"12951069\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No reciprocal endogenous co-IP or in vitro reconstitution of the dimer or NIF3L1 BP1 complex\",\n        \"Functional significance of homodimerization and NIF3L1 BP1 interaction not determined\"\n      ]\n    },\n    {\n      \"year\": 2004,\n      \"claim\": \"The broader signaling context of NIF3L1 was unclear; identification of a phosphorylation-dependent ternary complex with WBSCR14 and 14-3-3 isoforms connected NIF3L1 to phospho-regulated cytoplasmic signaling.\",\n      \"evidence\": \"Co-immunoprecipitation and phosphatase treatment in mammalian cells, yeast two-hybrid\",\n      \"pmids\": [\"15163635\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Which kinase phosphorylates WBSCR14 or NIF3L1 to drive complex assembly is unknown\",\n        \"Direct versus bridged interaction between NIF3L1 and 14-3-3 not resolved\",\n        \"Physiological function of this ternary complex not defined\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The enzymatic or structural basis of NIF3L1's repressor activity, its direct genomic targets, and its in vivo requirement in neural development remain uncharacterized.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No ChIP or genome-wide target identification performed\",\n        \"No knockout or conditional loss-of-function animal model reported\",\n        \"Crystal structure or biochemical activity of the conserved NIF3 domain not determined in mammalian systems\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [1, 2, 4]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"COPS2\",\n      \"NIF3L1BP1\",\n      \"WBSCR14\",\n      \"YWHAB\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}