{"gene":"NXN","run_date":"2026-06-10T05:19:52","timeline":{"discoveries":[{"year":2022,"finding":"NXN (nucleoredoxin) interacts with both Snail and DUB3 (a deubiquitylase), and promotes ubiquitin-proteasome-mediated degradation of Snail by inhibiting DUB3-mediated deubiquitylation of Snail. Co-immunoprecipitation confirmed the NXN-Snail-DUB3 ternary complex. Loss of Snail abolished the anti-proliferative and anti-metastatic effects of NXN in hepatocellular carcinoma cells.","method":"Co-immunoprecipitation, ectopic expression/knockdown with proliferation and metastasis assays (CCK-8, EdU, Transwell, wound healing, tail vein injection), in vitro and in vivo functional assays","journal":"Cell death & disease","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP establishing ternary complex, functional rescue (Snail depletion abolishes NXN effects), in vivo confirmation; single lab, multiple orthogonal methods","pmids":["35927236"],"is_preprint":false},{"year":2026,"finding":"KCMF1, a RING zinc-finger E3 ubiquitin ligase, interacts with NXN and promotes its degradation through K63-linked ubiquitination, thereby reducing NXN protein levels. Silencing NXN activated the β-catenin signaling pathway and facilitated ovarian cancer cell proliferation, migration, and invasion. NXN was identified as a substrate of KCMF1 by IP-LC/MS and label-free proteomics.","method":"IP-LC/MS, label-free proteomics, co-immunoprecipitation, KCMF1/NXN knockdown/overexpression with functional assays (cell viability, EMT, migration, invasion), in vivo xenograft experiments","journal":"Cell cycle (Georgetown, Tex.)","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — substrate identified by MS-based proteomics and validated by Co-IP, K63-linkage specificity established, β-catenin pathway placement; single lab, multiple orthogonal methods","pmids":["41721648"],"is_preprint":false},{"year":2025,"finding":"Nxn deficiency in mice reduces both canonical and non-canonical WNT signaling in the developing pituitary gland, impairs differentiation of pituitary stem cells into hormone-producing cells, and causes pituitary dysmorphology and craniofacial abnormalities including cleft palate. Single-cell RNA-seq revealed a delayed differentiation trajectory in Nxn mutant mice.","method":"Nxn knockout mouse model, WNT signaling reporter assays, single-cell RNA sequencing, histological analysis of pituitary and craniofacial structures","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic loss-of-function with specific cellular phenotype (stem cell differentiation) and pathway placement (WNT signaling); single lab, multiple orthogonal methods (scRNA-seq + signaling assays + histology); preprint, not yet peer-reviewed","pmids":[],"is_preprint":true}],"current_model":"NXN (nucleoredoxin) is a multifunctional redox-active protein that suppresses EMT and cancer progression by forming a complex with DUB3 and Snail to promote Snail's ubiquitin-proteasome degradation; NXN protein levels are themselves regulated by KCMF1-mediated K63-linked ubiquitination; and NXN acts upstream of WNT signaling during pituitary stem cell differentiation, with Nxn deficiency reducing both canonical and non-canonical WNT signaling and impairing hormone-producing cell differentiation."},"narrative":{"mechanistic_narrative":"NXN (nucleoredoxin) is a redox-active protein that functions as a regulatory node controlling both EMT-associated transcription factors and WNT/β-catenin signaling in development and cancer [PMID:35927236]. In hepatocellular carcinoma cells, NXN forms a ternary complex with the transcription factor Snail and the deubiquitylase DUB3, antagonizing DUB3-mediated deubiquitylation of Snail and thereby driving Snail toward ubiquitin-proteasome degradation; this Snail-suppressing activity underlies NXN's anti-proliferative and anti-metastatic effects, which are lost upon Snail depletion [PMID:35927236]. NXN's own abundance is set by the RING E3 ligase KCMF1, which binds NXN and targets it for K63-linked ubiquitination; loss of NXN activates β-catenin signaling and promotes ovarian cancer cell proliferation, migration, and invasion [PMID:41721648]. Consistent with a role upstream of WNT, Nxn-deficient mice show reduced canonical and non-canonical WNT signaling in the developing pituitary, delayed differentiation of pituitary stem cells into hormone-producing cells, and craniofacial defects including cleft palate. Beyond these contexts, the biochemical basis of NXN's redox activity has not been characterized in the available corpus.","teleology":[{"year":2022,"claim":"Established that NXN acts as a tumor suppressor by controlling the stability of the EMT driver Snail, answering how NXN restrains cancer cell proliferation and metastasis at the molecular level.","evidence":"Reciprocal Co-IP defining an NXN-Snail-DUB3 ternary complex, with Snail-depletion rescue and in vivo metastasis assays in hepatocellular carcinoma cells","pmids":["35927236"],"confidence":"Medium","gaps":["Mechanism by which NXN inhibits DUB3 catalytic activity not resolved","Whether NXN redox activity is required for Snail/DUB3 regulation untested","Single lab; effect in other cancer types not assessed"]},{"year":2026,"claim":"Identified how NXN protein levels are themselves regulated, showing KCMF1 targets NXN for K63-linked ubiquitination and that NXN loss derepresses β-catenin signaling in ovarian cancer.","evidence":"IP-LC/MS and label-free proteomics substrate identification, Co-IP validation, and KCMF1/NXN perturbation with functional and xenograft assays","pmids":["41721648"],"confidence":"Medium","gaps":["K63-linked ubiquitination typically signals non-degradative fates; how it reduces NXN levels here is not mechanistically dissected","Direct link between NXN loss and β-catenin activation not biochemically mapped","Ubiquitination site(s) on NXN not defined"]},{"year":2025,"claim":"Placed NXN upstream of WNT signaling in vivo, demonstrating it is required for pituitary stem cell differentiation and normal craniofacial development.","evidence":"Nxn knockout mouse with WNT reporter assays, single-cell RNA-seq differentiation trajectories, and histology of pituitary and craniofacial structures (preprint)","pmids":[],"confidence":"Medium","gaps":["Preprint, not yet peer-reviewed","Molecular mechanism by which NXN modulates canonical vs non-canonical WNT not defined","Relationship between developmental WNT role and cancer β-catenin role unresolved"]},{"year":null,"claim":"The biochemical basis of NXN's redox (nucleoredoxin) activity and how it mechanistically connects its roles in Snail degradation, KCMF1 regulation, and WNT signaling remain unestablished.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural or enzymatic characterization of NXN redox function in the corpus","No unified model linking the three reported contexts","Direct substrates or redox targets of NXN not identified"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0]}],"localization":[],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[1,2]}],"complexes":[],"partners":["SNAI1","DUB3","KCMF1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q6DKJ4","full_name":"Nucleoredoxin","aliases":[],"length_aa":435,"mass_kda":48.4,"function":"Functions as a redox-dependent negative regulator of the Wnt signaling pathway, possibly by preventing ubiquitination of DVL3 by the BCR(KLHL12) complex. May also function as a transcriptional regulator act as a regulator of protein phosphatase 2A (PP2A) (By similarity)","subcellular_location":"Cytoplasm, cytosol; Nucleus","url":"https://www.uniprot.org/uniprotkb/Q6DKJ4/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/NXN","classification":"Not Classified","n_dependent_lines":1,"n_total_lines":1208,"dependency_fraction":0.0008278145695364238},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/NXN","total_profiled":1310},"omim":[{"mim_id":"618529","title":"ROBINOW SYNDROME, AUTOSOMAL RECESSIVE 2; RRS2","url":"https://www.omim.org/entry/618529"},{"mim_id":"612895","title":"NUCLEOREDOXIN; NXN","url":"https://www.omim.org/entry/612895"},{"mim_id":"268310","title":"ROBINOW SYNDROME, AUTOSOMAL RECESSIVE 1; RRS1","url":"https://www.omim.org/entry/268310"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Cytosol","reliability":"Approved"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"skeletal muscle","ntpm":95.2}],"url":"https://www.proteinatlas.org/search/NXN"},"hgnc":{"alias_symbol":["FLJ12614","NRX"],"prev_symbol":[]},"alphafold":{"accession":"Q6DKJ4","domains":[{"cath_id":"3.40.30.10","chopping":"1-63_83-167","consensus_level":"medium","plddt":89.4813,"start":1,"end":167},{"cath_id":"3.40.30.10","chopping":"169-297","consensus_level":"high","plddt":96.1916,"start":169,"end":297},{"cath_id":"3.40.30.10","chopping":"312-433","consensus_level":"high","plddt":92.1021,"start":312,"end":433}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6DKJ4","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q6DKJ4-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q6DKJ4-F1-predicted_aligned_error_v6.png","plddt_mean":89.56},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=NXN","jax_strain_url":"https://www.jax.org/strain/search?query=NXN"},"sequence":{"accession":"Q6DKJ4","fasta_url":"https://rest.uniprot.org/uniprotkb/Q6DKJ4.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q6DKJ4/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6DKJ4"}},"corpus_meta":[{"pmid":"23155193","id":"PMC_23155193","title":"NXN-188, a selective nNOS inhibitor and a 5-HT1B/1D receptor agonist, inhibits CGRP release in preclinical migraine models.","date":"2012","source":"Cephalalgia : an international journal of headache","url":"https://pubmed.ncbi.nlm.nih.gov/23155193","citation_count":42,"is_preprint":false},{"pmid":"29913885","id":"PMC_29913885","title":"The nitric oxide synthase inhibitor and serotonin-receptor agonist NXN-188 during the aura phase of migraine with aura: A randomized, double-blind, placebo-controlled cross-over study.","date":"2013","source":"Scandinavian journal of pain","url":"https://pubmed.ncbi.nlm.nih.gov/29913885","citation_count":26,"is_preprint":false},{"pmid":"36375120","id":"PMC_36375120","title":"NRX-0492 degrades wild-type and C481 mutant BTK and demonstrates in vivo activity in CLL patient-derived xenografts.","date":"2023","source":"Blood","url":"https://pubmed.ncbi.nlm.nih.gov/36375120","citation_count":25,"is_preprint":false},{"pmid":"20171420","id":"PMC_20171420","title":"Safety and pharmacokinetics of NXN-188 after single and multiple doses in five phase I, randomized, double-blind, parallel studies in healthy adult volunteers.","date":"2010","source":"Clinical therapeutics","url":"https://pubmed.ncbi.nlm.nih.gov/20171420","citation_count":16,"is_preprint":false},{"pmid":"12019022","id":"PMC_12019022","title":"NBLAST: a cluster variant of BLAST for NxN comparisons.","date":"2002","source":"BMC bioinformatics","url":"https://pubmed.ncbi.nlm.nih.gov/12019022","citation_count":10,"is_preprint":false},{"pmid":"35927236","id":"PMC_35927236","title":"NXN suppresses metastasis of hepatocellular carcinoma by promoting degradation of Snail through binding to DUB3.","date":"2022","source":"Cell death & disease","url":"https://pubmed.ncbi.nlm.nih.gov/35927236","citation_count":7,"is_preprint":false},{"pmid":"35406633","id":"PMC_35406633","title":"NXN Gene Epigenetic Changes in an Adult Neurogenesis Model of Alzheimer's Disease.","date":"2022","source":"Cells","url":"https://pubmed.ncbi.nlm.nih.gov/35406633","citation_count":6,"is_preprint":false},{"pmid":"37226048","id":"PMC_37226048","title":"NRX-101, a Rapid-Acting Anti-Depressant, Does Not Cause Neurotoxicity Following Ketamine Administration in Preclinical Models.","date":"2023","source":"International journal of toxicology","url":"https://pubmed.ncbi.nlm.nih.gov/37226048","citation_count":5,"is_preprint":false},{"pmid":"41721648","id":"PMC_41721648","title":"KCMF1 promotes malignant progression by NXN ubiquitin-dependent degradation in ovarian cancer.","date":"2026","source":"Cell cycle (Georgetown, Tex.)","url":"https://pubmed.ncbi.nlm.nih.gov/41721648","citation_count":0,"is_preprint":false},{"pmid":"39988878","id":"PMC_39988878","title":"Circular RNA NXN (circNXN) promotes diabetic retinopathy by regulating the miR-338-3p/FGFR1 axis.","date":"2025","source":"Archives of physiology and biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/39988878","citation_count":0,"is_preprint":false},{"pmid":"39736406","id":"PMC_39736406","title":"Molecular characterization, transcriptional profiling, and antioxidant activity assessment of nucleoredoxin (NXN) as a novel member of thioredoxin from red-lip mullet (Planiliza haematocheilus).","date":"2024","source":"Fish & shellfish immunology","url":"https://pubmed.ncbi.nlm.nih.gov/39736406","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.11.17.688316","title":"Dynamic methylation changes in Alzheimer’s disease-related genes during mindfulness practice – a proof-of-concept study","date":"2025-11-24","source":"bioRxiv","url":"https://doi.org/10.1101/2025.11.17.688316","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2025.01.30.635771","title":"Nucleoredoxin regulates WNT signaling during pituitary stem cell differentiation","date":"2025-01-30","source":"bioRxiv","url":"https://doi.org/10.1101/2025.01.30.635771","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2025.08.29.672776","title":"<i>In vivo</i>  dissection of human  <i>NRXN1</i>  isoforms reveals gain-of-function pathogenicity of schizophrenia-associated 3’ deletions","date":"2025-09-02","source":"bioRxiv","url":"https://doi.org/10.1101/2025.08.29.672776","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.10.16.618688","title":"Weaker neuroligin 2 – neurexin 1β interaction tethers membranes and signal synaptogenesis through clustering","date":"2024-10-18","source":"bioRxiv","url":"https://doi.org/10.1101/2024.10.16.618688","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2025.01.23.634392","title":"TIME-CoExpress: Temporal Trajectory Modeling of Dynamic Gene Co-expression Patterns Using Single-Cell Transcriptomics Data","date":"2025-01-26","source":"bioRxiv","url":"https://doi.org/10.1101/2025.01.23.634392","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":11275,"output_tokens":1051,"usd":0.024795,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7569,"output_tokens":1703,"usd":0.04021,"stage2_stop_reason":"end_turn"},"total_usd":0.065005,"stage1_batch_id":"msgbatch_013a8chtv3AWyTqv4z4sEF4C","stage2_batch_id":"msgbatch_01AHsuW63vinsvuTgzmQ3n62","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2022,\n      \"finding\": \"NXN (nucleoredoxin) interacts with both Snail and DUB3 (a deubiquitylase), and promotes ubiquitin-proteasome-mediated degradation of Snail by inhibiting DUB3-mediated deubiquitylation of Snail. Co-immunoprecipitation confirmed the NXN-Snail-DUB3 ternary complex. Loss of Snail abolished the anti-proliferative and anti-metastatic effects of NXN in hepatocellular carcinoma cells.\",\n      \"method\": \"Co-immunoprecipitation, ectopic expression/knockdown with proliferation and metastasis assays (CCK-8, EdU, Transwell, wound healing, tail vein injection), in vitro and in vivo functional assays\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP establishing ternary complex, functional rescue (Snail depletion abolishes NXN effects), in vivo confirmation; single lab, multiple orthogonal methods\",\n      \"pmids\": [\"35927236\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"KCMF1, a RING zinc-finger E3 ubiquitin ligase, interacts with NXN and promotes its degradation through K63-linked ubiquitination, thereby reducing NXN protein levels. Silencing NXN activated the β-catenin signaling pathway and facilitated ovarian cancer cell proliferation, migration, and invasion. NXN was identified as a substrate of KCMF1 by IP-LC/MS and label-free proteomics.\",\n      \"method\": \"IP-LC/MS, label-free proteomics, co-immunoprecipitation, KCMF1/NXN knockdown/overexpression with functional assays (cell viability, EMT, migration, invasion), in vivo xenograft experiments\",\n      \"journal\": \"Cell cycle (Georgetown, Tex.)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — substrate identified by MS-based proteomics and validated by Co-IP, K63-linkage specificity established, β-catenin pathway placement; single lab, multiple orthogonal methods\",\n      \"pmids\": [\"41721648\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Nxn deficiency in mice reduces both canonical and non-canonical WNT signaling in the developing pituitary gland, impairs differentiation of pituitary stem cells into hormone-producing cells, and causes pituitary dysmorphology and craniofacial abnormalities including cleft palate. Single-cell RNA-seq revealed a delayed differentiation trajectory in Nxn mutant mice.\",\n      \"method\": \"Nxn knockout mouse model, WNT signaling reporter assays, single-cell RNA sequencing, histological analysis of pituitary and craniofacial structures\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic loss-of-function with specific cellular phenotype (stem cell differentiation) and pathway placement (WNT signaling); single lab, multiple orthogonal methods (scRNA-seq + signaling assays + histology); preprint, not yet peer-reviewed\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"NXN (nucleoredoxin) is a multifunctional redox-active protein that suppresses EMT and cancer progression by forming a complex with DUB3 and Snail to promote Snail's ubiquitin-proteasome degradation; NXN protein levels are themselves regulated by KCMF1-mediated K63-linked ubiquitination; and NXN acts upstream of WNT signaling during pituitary stem cell differentiation, with Nxn deficiency reducing both canonical and non-canonical WNT signaling and impairing hormone-producing cell differentiation.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"NXN (nucleoredoxin) is a redox-active protein that functions as a regulatory node controlling both EMT-associated transcription factors and WNT/β-catenin signaling in development and cancer [#0, #2]. In hepatocellular carcinoma cells, NXN forms a ternary complex with the transcription factor Snail and the deubiquitylase DUB3, antagonizing DUB3-mediated deubiquitylation of Snail and thereby driving Snail toward ubiquitin-proteasome degradation; this Snail-suppressing activity underlies NXN's anti-proliferative and anti-metastatic effects, which are lost upon Snail depletion [#0]. NXN's own abundance is set by the RING E3 ligase KCMF1, which binds NXN and targets it for K63-linked ubiquitination; loss of NXN activates β-catenin signaling and promotes ovarian cancer cell proliferation, migration, and invasion [#1]. Consistent with a role upstream of WNT, Nxn-deficient mice show reduced canonical and non-canonical WNT signaling in the developing pituitary, delayed differentiation of pituitary stem cells into hormone-producing cells, and craniofacial defects including cleft palate [#2]. Beyond these contexts, the biochemical basis of NXN's redox activity has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2022,\n      \"claim\": \"Established that NXN acts as a tumor suppressor by controlling the stability of the EMT driver Snail, answering how NXN restrains cancer cell proliferation and metastasis at the molecular level.\",\n      \"evidence\": \"Reciprocal Co-IP defining an NXN-Snail-DUB3 ternary complex, with Snail-depletion rescue and in vivo metastasis assays in hepatocellular carcinoma cells\",\n      \"pmids\": [\"35927236\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanism by which NXN inhibits DUB3 catalytic activity not resolved\",\n        \"Whether NXN redox activity is required for Snail/DUB3 regulation untested\",\n        \"Single lab; effect in other cancer types not assessed\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Identified how NXN protein levels are themselves regulated, showing KCMF1 targets NXN for K63-linked ubiquitination and that NXN loss derepresses β-catenin signaling in ovarian cancer.\",\n      \"evidence\": \"IP-LC/MS and label-free proteomics substrate identification, Co-IP validation, and KCMF1/NXN perturbation with functional and xenograft assays\",\n      \"pmids\": [\"41721648\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"K63-linked ubiquitination typically signals non-degradative fates; how it reduces NXN levels here is not mechanistically dissected\",\n        \"Direct link between NXN loss and β-catenin activation not biochemically mapped\",\n        \"Ubiquitination site(s) on NXN not defined\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Placed NXN upstream of WNT signaling in vivo, demonstrating it is required for pituitary stem cell differentiation and normal craniofacial development.\",\n      \"evidence\": \"Nxn knockout mouse with WNT reporter assays, single-cell RNA-seq differentiation trajectories, and histology of pituitary and craniofacial structures (preprint)\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Preprint, not yet peer-reviewed\",\n        \"Molecular mechanism by which NXN modulates canonical vs non-canonical WNT not defined\",\n        \"Relationship between developmental WNT role and cancer β-catenin role unresolved\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The biochemical basis of NXN's redox (nucleoredoxin) activity and how it mechanistically connects its roles in Snail degradation, KCMF1 regulation, and WNT signaling remain unestablished.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural or enzymatic characterization of NXN redox function in the corpus\",\n        \"No unified model linking the three reported contexts\",\n        \"Direct substrates or redox targets of NXN not identified\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"SNAI1\", \"DUB3\", \"KCMF1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":3,"faith_total":3,"faith_pct":100.0}}