{"gene":"BPIFB3","run_date":"2026-06-09T22:02:45","timeline":{"discoveries":[{"year":2014,"finding":"BPIFB3 localizes to the endoplasmic reticulum (ER), and its silencing by RNAi enhances basal autophagy and promotes autophagy during coxsackievirus B (CVB) replication, while overexpression suppresses autophagy and CVB replication. Critically, silencing core autophagy initiation components (which suppresses CVB replication in control cells) had no effect on CVB-induced autophagy or replication in BPIFB3-silenced cells, defining BPIFB3 as a negative regulator of a noncanonical autophagy pathway independent of core autophagy initiation machinery.","method":"RNAi silencing, overexpression, fluorescence microscopy (LC3B-positive vesicle morphology), rapamycin-induced autophagy assay, double-silencing epistasis experiments","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (RNAi, overexpression, epistasis), replicated across conditions; single lab but rigorous genetic epistasis placing BPIFB3 in a defined pathway","pmids":["25491355"],"is_preprint":false},{"year":2016,"finding":"BPIFB3 localizes exclusively to the ER (confirmed independently) and associates with other BPIFB family members including BPIFB6 at the ER.","method":"Fluorescence localization (confocal microscopy), co-localization/association assays with BPIFB family members","journal":"Journal of virology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — localization confirmed independently, association inferred from co-localization; single lab, supporting prior finding","pmids":["26962226"],"is_preprint":false},{"year":2020,"finding":"BPIFB3 positively regulates dengue virus (DENV) and Zika virus (ZIKV) replication by suppressing RETREG1 (FAM134B)-dependent reticulophagy; depletion of BPIFB3 enhances RETREG1-dependent ER turnover and inhibits formation of flavivirus replication organelles, while silencing RETREG1 rescues the antiviral effect of BPIFB3 depletion.","method":"RNAi silencing, double-silencing epistasis (BPIFB3 + RETREG1), viral replication assays, fluorescence microscopy of replication organelles","journal":"Journal of virology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — genetic epistasis with double KD rescue, multiple orthogonal assays; single lab but rigorous pathway placement via RETREG1 suppressor experiment","pmids":["32102874"],"is_preprint":false},{"year":2021,"finding":"Using proximity-dependent biotinylation (BioID) followed by mass spectrometry, ARFGAP1 and TMED9 were identified as direct interactors of ER-localized BPIFB3. These interactions are functionally required for BPIFB3-regulated noncanonical autophagy and for its role in controlling enterovirus and flavivirus replication.","method":"BioID proximity-dependent biotinylation, mass spectrometry, RNAi silencing of ARFGAP1 and TMED9, viral replication assays, autophagy assays","journal":"Journal of cell science","confidence":"High","confidence_rationale":"Tier 2 / Moderate — BioID/MS interaction discovery validated by functional RNAi knockdown of interactors with defined phenotypic readouts; single lab, two orthogonal methods","pmids":["33277377"],"is_preprint":false}],"current_model":"BPIFB3 is an ER-resident protein that negatively regulates a noncanonical autophagy pathway (independent of core autophagy initiation machinery) through interactions with ARFGAP1 and TMED9; it suppresses enterovirus (CVB) replication by restricting autophagosome formation, while positively supporting flavivirus (DENV/ZIKV) replication by restraining RETREG1-dependent reticulophagy to preserve ER membranes needed for viral replication organelles."},"narrative":{"mechanistic_narrative":"BPIFB3 is an endoplasmic reticulum-resident protein that functions as a negative regulator of a noncanonical autophagy pathway operating independently of the core autophagy initiation machinery [PMID:25491355]. Silencing BPIFB3 enhances basal and virus-induced autophagy, and epistasis with core initiation components establishes that the BPIFB3-controlled pathway bypasses canonical autophagy initiation [PMID:25491355]. Through this control of membrane turnover, BPIFB3 exerts opposing effects on distinct viruses: it restricts coxsackievirus B replication by suppressing autophagosome formation [PMID:25491355], yet positively supports dengue and Zika virus replication by restraining RETREG1 (FAM134B)-dependent reticulophagy, thereby preserving ER membranes required for assembly of flavivirus replication organelles [PMID:32102874]. Its regulatory activity depends on the ER-localized interactors ARFGAP1 and TMED9, identified by proximity biotinylation and functionally required for both BPIFB3-regulated noncanonical autophagy and its control of enterovirus and flavivirus replication [PMID:33277377]. BPIFB3 localizes exclusively to the ER and associates with other BPIFB family members [PMID:26962226]. Beyond these findings, the biochemical mechanism by which BPIFB3 restrains autophagic membrane turnover has not been characterized in the available corpus.","teleology":[{"year":2014,"claim":"Established that BPIFB3 is an ER protein that negatively regulates autophagy through a pathway distinct from canonical autophagy initiation, answering where it acts and how it intersects with virus replication.","evidence":"RNAi, overexpression, LC3B vesicle microscopy, and double-silencing epistasis with core autophagy components during CVB infection","pmids":["25491355"],"confidence":"High","gaps":["The molecular activity by which BPIFB3 suppresses noncanonical autophagy is undefined","No interacting partners were identified at this stage"]},{"year":2016,"claim":"Confirmed exclusive ER localization independently and placed BPIFB3 in physical proximity to other BPIFB family members at the ER, defining its subcellular context.","evidence":"Confocal localization and co-localization/association assays with BPIFB family members including BPIFB6","pmids":["26962226"],"confidence":"Medium","gaps":["Family-member association inferred from co-localization rather than direct binding assays","Functional consequence of BPIFB family association unknown"]},{"year":2020,"claim":"Revealed that BPIFB3 has a virus-dependent dual role, promoting flavivirus replication by restraining RETREG1-dependent reticulophagy, answering how ER membrane turnover is coupled to viral replication organelle formation.","evidence":"BPIFB3 + RETREG1 double-knockdown epistasis with rescue, viral replication assays, and replication-organelle microscopy in DENV/ZIKV infection","pmids":["32102874"],"confidence":"High","gaps":["The direct molecular link between BPIFB3 and the RETREG1 reticulophagy machinery is not defined","Whether BPIFB3 acts directly on RETREG1 or upstream remains unresolved"]},{"year":2021,"claim":"Identified ARFGAP1 and TMED9 as ER interactors functionally required for BPIFB3 activity, providing the first molecular partners through which it regulates autophagy and viral replication.","evidence":"BioID proximity biotinylation with mass spectrometry, followed by RNAi of interactors with autophagy and viral replication readouts","pmids":["33277377"],"confidence":"High","gaps":["Whether interactions are direct binary contacts versus proximity-based is not resolved by BioID alone","The biochemical step ARFGAP1/TMED9 perform with BPIFB3 is undefined"]},{"year":null,"claim":"The catalytic or biochemical mechanism by which BPIFB3, with ARFGAP1 and TMED9, restrains autophagic and reticulophagic ER membrane turnover remains unknown.","evidence":"","pmids":[],"confidence":"High","gaps":["No defined enzymatic or molecular activity for BPIFB3","No structural model of BPIFB3 or its complexes","Mechanism distinguishing autophagy suppression from reticulophagy restraint unresolved"]}],"mechanism_profile":{"molecular_activity":[],"localization":[{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[0,1,3]}],"pathway":[{"term_id":"R-HSA-9612973","term_label":"Autophagy","supporting_discovery_ids":[0,2]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[0,2,3]}],"complexes":[],"partners":["ARFGAP1","TMED9","BPIFB6"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P59826","full_name":"BPI fold-containing family B member 3","aliases":["Ligand-binding protein RYA3","Long palate, lung and nasal epithelium carcinoma-associated protein 3"],"length_aa":472,"mass_kda":49.9,"function":"May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity)","subcellular_location":"Secreted; Cytoplasm","url":"https://www.uniprot.org/uniprotkb/P59826/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/BPIFB3","classification":"Not Classified","n_dependent_lines":3,"n_total_lines":1208,"dependency_fraction":0.0024834437086092716},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/BPIFB3","total_profiled":1310},"omim":[{"mim_id":"615718","title":"BPI FOLD-CONTAINING PROTEIN, FAMILY B, MEMBER 4; BPIFB4","url":"https://www.omim.org/entry/615718"},{"mim_id":"615717","title":"BPI FOLD-CONTAINING PROTEIN, FAMILY B, MEMBER 3; BPIFB3","url":"https://www.omim.org/entry/615717"},{"mim_id":"614108","title":"BPI FOLD-CONTAINING PROTEIN, FAMILY B, MEMBER 2; BPIFB2","url":"https://www.omim.org/entry/614108"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Not detected","tissue_distribution":"Not detected","driving_tissues":[],"url":"https://www.proteinatlas.org/search/BPIFB3"},"hgnc":{"alias_symbol":["dJ726C3.4","LPLUNC3","RYA3"],"prev_symbol":["C20orf185"]},"alphafold":{"accession":"P59826","domains":[{"cath_id":"3.15.10.10","chopping":"37-58_94-216","consensus_level":"medium","plddt":83.2819,"start":37,"end":216},{"cath_id":"3.15.20.10","chopping":"229-476","consensus_level":"high","plddt":87.701,"start":229,"end":476}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P59826","model_url":"https://alphafold.ebi.ac.uk/files/AF-P59826-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P59826-F1-predicted_aligned_error_v6.png","plddt_mean":81.25},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=BPIFB3","jax_strain_url":"https://www.jax.org/strain/search?query=BPIFB3"},"sequence":{"accession":"P59826","fasta_url":"https://rest.uniprot.org/uniprotkb/P59826.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P59826/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P59826"}},"corpus_meta":[{"pmid":"1915264","id":"PMC_1915264","title":"Novel genes for potential ligand-binding proteins in subregions of the olfactory mucosa.","date":"1991","source":"The EMBO journal","url":"https://pubmed.ncbi.nlm.nih.gov/1915264","citation_count":63,"is_preprint":false},{"pmid":"12427544","id":"PMC_12427544","title":"The BSP30 salivary proteins from cattle, LUNX/PLUNC and von Ebner's minor salivary gland protein are members of the PSP/LBP superfamily of proteins.","date":"2002","source":"Biochimica et biophysica acta","url":"https://pubmed.ncbi.nlm.nih.gov/12427544","citation_count":44,"is_preprint":false},{"pmid":"25491355","id":"PMC_25491355","title":"BPIFB3 regulates autophagy and coxsackievirus B replication through a noncanonical pathway independent of the core initiation machinery.","date":"2014","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/25491355","citation_count":36,"is_preprint":false},{"pmid":"26962226","id":"PMC_26962226","title":"BPIFB6 Regulates Secretory Pathway Trafficking and Enterovirus Replication.","date":"2016","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/26962226","citation_count":31,"is_preprint":false},{"pmid":"32102874","id":"PMC_32102874","title":"BPIFB3 Regulates Endoplasmic Reticulum Morphology To Facilitate Flavivirus Replication.","date":"2020","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/32102874","citation_count":29,"is_preprint":false},{"pmid":"12837268","id":"PMC_12837268","title":"Expansion of the BPI family by duplication on human chromosome 20: characterization of the RY gene cluster in 20q11.21 encoding olfactory transporters/antimicrobial-like peptides.","date":"2003","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/12837268","citation_count":27,"is_preprint":false},{"pmid":"31316551","id":"PMC_31316551","title":"Genomic Analysis Reveals Pleiotropic Alleles at EDN3 and BMP7 Involved in Chicken Comb Color and Egg Production.","date":"2019","source":"Frontiers in genetics","url":"https://pubmed.ncbi.nlm.nih.gov/31316551","citation_count":27,"is_preprint":false},{"pmid":"39394962","id":"PMC_39394962","title":"Reticulophagy and viral infection.","date":"2024","source":"Autophagy","url":"https://pubmed.ncbi.nlm.nih.gov/39394962","citation_count":20,"is_preprint":false},{"pmid":"32718314","id":"PMC_32718314","title":"Transcriptome analysis of the uterus of hens laying eggs differing in cuticle deposition.","date":"2020","source":"BMC genomics","url":"https://pubmed.ncbi.nlm.nih.gov/32718314","citation_count":19,"is_preprint":false},{"pmid":"33277377","id":"PMC_33277377","title":"BPIFB3 interacts with ARFGAP1 and TMED9 to regulate non-canonical autophagy and RNA virus infection.","date":"2021","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/33277377","citation_count":10,"is_preprint":false},{"pmid":"35712705","id":"PMC_35712705","title":"Age-Related Increase of Collagen/Fibrin Deposition and High PAI-1 Production in Human Nasal Polyps.","date":"2022","source":"Frontiers in pharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/35712705","citation_count":10,"is_preprint":false},{"pmid":"39728450","id":"PMC_39728450","title":"Transcriptomic Profiling Reveals Altered Expression of Genes Involved in Metabolic and Immune Processes in NDV-Infected Chicken Embryos.","date":"2024","source":"Metabolites","url":"https://pubmed.ncbi.nlm.nih.gov/39728450","citation_count":0,"is_preprint":false},{"pmid":"41321507","id":"PMC_41321507","title":"Regulatory effects of hawthorn leaf flavonoids and stevioside on the uterine function and eggshell quality in laying hens.","date":"2025","source":"Animal nutrition (Zhongguo xu mu shou yi xue hui)","url":"https://pubmed.ncbi.nlm.nih.gov/41321507","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":10856,"output_tokens":1193,"usd":0.025232,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7691,"output_tokens":1850,"usd":0.042353,"stage2_stop_reason":"end_turn"},"total_usd":0.067585,"stage1_batch_id":"msgbatch_0179Z2pxRYBsXi2xADneafRw","stage2_batch_id":"msgbatch_01LaY9ZaVdgjWArcZo9eqQE5","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"BPIFB3 localizes to the endoplasmic reticulum (ER), and its silencing by RNAi enhances basal autophagy and promotes autophagy during coxsackievirus B (CVB) replication, while overexpression suppresses autophagy and CVB replication. Critically, silencing core autophagy initiation components (which suppresses CVB replication in control cells) had no effect on CVB-induced autophagy or replication in BPIFB3-silenced cells, defining BPIFB3 as a negative regulator of a noncanonical autophagy pathway independent of core autophagy initiation machinery.\",\n      \"method\": \"RNAi silencing, overexpression, fluorescence microscopy (LC3B-positive vesicle morphology), rapamycin-induced autophagy assay, double-silencing epistasis experiments\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (RNAi, overexpression, epistasis), replicated across conditions; single lab but rigorous genetic epistasis placing BPIFB3 in a defined pathway\",\n      \"pmids\": [\"25491355\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"BPIFB3 localizes exclusively to the ER (confirmed independently) and associates with other BPIFB family members including BPIFB6 at the ER.\",\n      \"method\": \"Fluorescence localization (confocal microscopy), co-localization/association assays with BPIFB family members\",\n      \"journal\": \"Journal of virology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — localization confirmed independently, association inferred from co-localization; single lab, supporting prior finding\",\n      \"pmids\": [\"26962226\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"BPIFB3 positively regulates dengue virus (DENV) and Zika virus (ZIKV) replication by suppressing RETREG1 (FAM134B)-dependent reticulophagy; depletion of BPIFB3 enhances RETREG1-dependent ER turnover and inhibits formation of flavivirus replication organelles, while silencing RETREG1 rescues the antiviral effect of BPIFB3 depletion.\",\n      \"method\": \"RNAi silencing, double-silencing epistasis (BPIFB3 + RETREG1), viral replication assays, fluorescence microscopy of replication organelles\",\n      \"journal\": \"Journal of virology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis with double KD rescue, multiple orthogonal assays; single lab but rigorous pathway placement via RETREG1 suppressor experiment\",\n      \"pmids\": [\"32102874\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Using proximity-dependent biotinylation (BioID) followed by mass spectrometry, ARFGAP1 and TMED9 were identified as direct interactors of ER-localized BPIFB3. These interactions are functionally required for BPIFB3-regulated noncanonical autophagy and for its role in controlling enterovirus and flavivirus replication.\",\n      \"method\": \"BioID proximity-dependent biotinylation, mass spectrometry, RNAi silencing of ARFGAP1 and TMED9, viral replication assays, autophagy assays\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — BioID/MS interaction discovery validated by functional RNAi knockdown of interactors with defined phenotypic readouts; single lab, two orthogonal methods\",\n      \"pmids\": [\"33277377\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"BPIFB3 is an ER-resident protein that negatively regulates a noncanonical autophagy pathway (independent of core autophagy initiation machinery) through interactions with ARFGAP1 and TMED9; it suppresses enterovirus (CVB) replication by restricting autophagosome formation, while positively supporting flavivirus (DENV/ZIKV) replication by restraining RETREG1-dependent reticulophagy to preserve ER membranes needed for viral replication organelles.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"BPIFB3 is an endoplasmic reticulum-resident protein that functions as a negative regulator of a noncanonical autophagy pathway operating independently of the core autophagy initiation machinery [#0]. Silencing BPIFB3 enhances basal and virus-induced autophagy, and epistasis with core initiation components establishes that the BPIFB3-controlled pathway bypasses canonical autophagy initiation [#0]. Through this control of membrane turnover, BPIFB3 exerts opposing effects on distinct viruses: it restricts coxsackievirus B replication by suppressing autophagosome formation [#0], yet positively supports dengue and Zika virus replication by restraining RETREG1 (FAM134B)-dependent reticulophagy, thereby preserving ER membranes required for assembly of flavivirus replication organelles [#2]. Its regulatory activity depends on the ER-localized interactors ARFGAP1 and TMED9, identified by proximity biotinylation and functionally required for both BPIFB3-regulated noncanonical autophagy and its control of enterovirus and flavivirus replication [#3]. BPIFB3 localizes exclusively to the ER and associates with other BPIFB family members [#1]. Beyond these findings, the biochemical mechanism by which BPIFB3 restrains autophagic membrane turnover has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Established that BPIFB3 is an ER protein that negatively regulates autophagy through a pathway distinct from canonical autophagy initiation, answering where it acts and how it intersects with virus replication.\",\n      \"evidence\": \"RNAi, overexpression, LC3B vesicle microscopy, and double-silencing epistasis with core autophagy components during CVB infection\",\n      \"pmids\": [\"25491355\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"The molecular activity by which BPIFB3 suppresses noncanonical autophagy is undefined\", \"No interacting partners were identified at this stage\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Confirmed exclusive ER localization independently and placed BPIFB3 in physical proximity to other BPIFB family members at the ER, defining its subcellular context.\",\n      \"evidence\": \"Confocal localization and co-localization/association assays with BPIFB family members including BPIFB6\",\n      \"pmids\": [\"26962226\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Family-member association inferred from co-localization rather than direct binding assays\", \"Functional consequence of BPIFB family association unknown\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Revealed that BPIFB3 has a virus-dependent dual role, promoting flavivirus replication by restraining RETREG1-dependent reticulophagy, answering how ER membrane turnover is coupled to viral replication organelle formation.\",\n      \"evidence\": \"BPIFB3 + RETREG1 double-knockdown epistasis with rescue, viral replication assays, and replication-organelle microscopy in DENV/ZIKV infection\",\n      \"pmids\": [\"32102874\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"The direct molecular link between BPIFB3 and the RETREG1 reticulophagy machinery is not defined\", \"Whether BPIFB3 acts directly on RETREG1 or upstream remains unresolved\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Identified ARFGAP1 and TMED9 as ER interactors functionally required for BPIFB3 activity, providing the first molecular partners through which it regulates autophagy and viral replication.\",\n      \"evidence\": \"BioID proximity biotinylation with mass spectrometry, followed by RNAi of interactors with autophagy and viral replication readouts\",\n      \"pmids\": [\"33277377\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether interactions are direct binary contacts versus proximity-based is not resolved by BioID alone\", \"The biochemical step ARFGAP1/TMED9 perform with BPIFB3 is undefined\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The catalytic or biochemical mechanism by which BPIFB3, with ARFGAP1 and TMED9, restrains autophagic and reticulophagic ER membrane turnover remains unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No defined enzymatic or molecular activity for BPIFB3\", \"No structural model of BPIFB3 or its complexes\", \"Mechanism distinguishing autophagy suppression from reticulophagy restraint unresolved\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [0, 1, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9612973\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [0, 2, 3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"ARFGAP1\", \"TMED9\", \"BPIFB6\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":5,"faith_pct":80.0}}