{"gene":"PHYH","run_date":"2026-06-10T06:43:35","timeline":{"discoveries":[{"year":1997,"finding":"PAHX (PHYH) encodes a phytanoyl-CoA alpha-hydroxylase with intrinsic dioxygenase activity that requires iron as a cofactor and 2-oxoglutarate as a cosubstrate, catalyzing the alpha-hydroxylation step of phytanic acid oxidation in peroxisomes.","method":"In vitro enzymatic assay demonstrating phytanoyl-CoA alpha-hydroxylase activity; cofactor requirement established by biochemical characterization","journal":"Nature genetics","confidence":"High","confidence_rationale":"Tier 1 / Strong — direct in vitro enzymatic activity demonstrated with cofactor identification, plus functional validation via disease-causing inactivating mutations","pmids":["9326939"],"is_preprint":false},{"year":1997,"finding":"PHYH is targeted to peroxisomes via a type-2 peroxisomal targeting signal (PTS2) and requires the PTS2 receptor PEX7 for its peroxisomal localization.","method":"Peroxisomal targeting demonstrated by cell-based localization studies; PEX7 dependence shown by loss of localization in PEX7-deficient cells; yeast two-hybrid assay confirmed interaction between PAHX and PEX7","journal":"Nature genetics","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal yeast two-hybrid interaction plus functional localization experiments with PEX7-deficient cells, replicated in subsequent literature","pmids":["9326939"],"is_preprint":false},{"year":1997,"finding":"Homozygous inactivating mutations in PHYH (PAHX) cause Refsum disease, establishing PHYH as the enzyme defective in classic Refsum disease.","method":"Mutation analysis in Refsum disease patients showing homozygous inactivating mutations; loss-of-function with phytanic acid accumulation phenotype","journal":"Nature genetics","confidence":"High","confidence_rationale":"Tier 2 / Strong — direct patient mutation analysis with biochemical phenotype confirmation, independently replicated across multiple subsequent studies","pmids":["9326939","14974078"],"is_preprint":false},{"year":2004,"finding":"Refsum disease is genetically heterogeneous, caused by mutations in either PHYH (encoding phytanoyl-CoA hydroxylase) or PEX7 (encoding the PTS2 receptor required for PHYH peroxisomal targeting), both disrupting peroxisomal alpha-oxidation of phytanic acid.","method":"Molecular genetic analysis of Refsum disease patients identifying mutations in PHYH or PEX7; mechanistic review of alpha-oxidation pathway","journal":"Human mutation","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic pathway placement across multiple patients, single review/analysis study consolidating prior findings","pmids":["14974078"],"is_preprint":false},{"year":2024,"finding":"The PHYH splice-site variant c.678+5G>T causes in-frame skipping of exons 5 and 6 (and to a lesser extent exon 6 alone) in the canonical transcript, resulting in an attenuated form of Refsum disease with milder biochemical and clinical phenotype.","method":"RNA extracted from patient blood, reverse transcription to cDNA, PCR amplification, Oxford Nanopore single-molecule amplicon sequencing to characterize splicing outcome","journal":"Investigative ophthalmology & visual science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct RNA-level characterization with single-molecule sequencing in multiple patients, single lab study","pmids":["38411969"],"is_preprint":false}],"current_model":"PHYH (PAHX) encodes a peroxisomal phytanoyl-CoA alpha-hydroxylase that is targeted to peroxisomes via a PTS2 signal recognized by the receptor PEX7; once in peroxisomes, it catalyzes the iron- and 2-oxoglutarate-dependent dioxygenase reaction that alpha-hydroxylates phytanoyl-CoA as the key step in phytanic acid alpha-oxidation, and inactivating mutations in PHYH cause the autosomal recessive lipid storage disorder Refsum disease."},"narrative":{"mechanistic_narrative":"PHYH (PAHX) encodes phytanoyl-CoA alpha-hydroxylase, the enzyme that catalyzes the committed alpha-hydroxylation step of peroxisomal phytanic acid alpha-oxidation [PMID:9326939]. It is an iron-dependent dioxygenase that uses 2-oxoglutarate as a cosubstrate to alpha-hydroxylate phytanoyl-CoA [PMID:9326939]. Catalytic function requires correct subcellular delivery: PHYH carries a type-2 peroxisomal targeting signal (PTS2) and depends on the PTS2 receptor PEX7 for import into peroxisomes, an interaction confirmed by direct binding and by loss of localization in PEX7-deficient cells [PMID:9326939]. Inactivating mutations in PHYH cause autosomal recessive Refsum disease, with phytanic acid accumulation as the biochemical hallmark, and the same disorder also arises from PEX7 mutations that abolish PHYH peroxisomal targeting—placing both genes on a single alpha-oxidation axis [PMID:9326939, PMID:14974078].","teleology":[{"year":1997,"claim":"Established the molecular identity and catalytic mechanism of the enzyme defective in Refsum disease by showing PHYH is an iron- and 2-oxoglutarate-dependent dioxygenase acting on phytanoyl-CoA.","evidence":"in vitro enzymatic assay with cofactor characterization","pmids":["9326939"],"confidence":"High","gaps":["No structural model of the catalytic site reported in the corpus","Kinetic regulation of the enzyme not characterized"]},{"year":1997,"claim":"Resolved how the enzyme reaches its compartment, demonstrating PHYH uses a PTS2 signal and the receptor PEX7 for peroxisomal import.","evidence":"cell-based localization in PEX7-deficient cells plus yeast two-hybrid interaction","pmids":["9326939"],"confidence":"High","gaps":["Stoichiometry and structural basis of the PHYH-PEX7 interaction not defined","Cargo release mechanism inside the peroxisome not addressed"]},{"year":1997,"claim":"Linked the gene to disease by showing homozygous inactivating PHYH mutations cause classic Refsum disease with phytanic acid accumulation.","evidence":"patient mutation analysis with biochemical phenotyping","pmids":["9326939","14974078"],"confidence":"High","gaps":["Genotype-phenotype relationships across mutation classes not enumerated here"]},{"year":2004,"claim":"Placed PHYH within a genetically heterogeneous disease framework, showing Refsum disease results from disruption of phytanic acid alpha-oxidation by either PHYH or PEX7 mutations.","evidence":"molecular genetic analysis across patients with mechanistic pathway review","pmids":["14974078"],"confidence":"Medium","gaps":["Relative frequency of PHYH versus PEX7 etiology not quantified here","Single consolidating analysis"]},{"year":2024,"claim":"Refined genotype-phenotype understanding by showing a splice-site variant produces in-frame exon skipping and an attenuated disease form, linking partial transcript function to milder phenotype.","evidence":"patient-derived RNA reverse transcription and Oxford Nanopore single-molecule amplicon sequencing","pmids":["38411969"],"confidence":"Medium","gaps":["Residual enzymatic activity of the skipped-exon protein not measured","Single-lab study"]},{"year":null,"claim":"How PHYH catalytic output and import are regulated, and the structural basis of substrate and cofactor engagement, remain open.","evidence":"no direct evidence in the available corpus","pmids":[],"confidence":"Low","gaps":["No structural data","No regulation or post-translational control characterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0016491","term_label":"oxidoreductase activity","supporting_discovery_ids":[0]},{"term_id":"GO:0016740","term_label":"transferase activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005777","term_label":"peroxisome","supporting_discovery_ids":[0,1]}],"pathway":[{"term_id":"R-HSA-1430728","term_label":"Metabolism","supporting_discovery_ids":[0]}],"complexes":[],"partners":["PEX7"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O14832","full_name":"Phytanoyl-CoA dioxygenase, peroxisomal","aliases":["Phytanic acid oxidase","Phytanoyl-CoA alpha-hydroxylase","PhyH"],"length_aa":338,"mass_kda":38.5,"function":"Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (PubMed:10744784, PubMed:12031666, PubMed:12923223, PubMed:9326939). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl- and 4-methyl-branched acyl-CoAs (PubMed:10744784, PubMed:12923223)","subcellular_location":"Peroxisome","url":"https://www.uniprot.org/uniprotkb/O14832/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/PHYH","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/PHYH","total_profiled":1310},"omim":[{"mim_id":"621410","title":"PEROXISOME BIOGENESIS FACTOR 39; PEX39","url":"https://www.omim.org/entry/621410"},{"mim_id":"620042","title":"PHYTANOYL-CoA DIOXYGENASE DOMAIN-CONTAINING PROTEIN 1; PHYHD1","url":"https://www.omim.org/entry/620042"},{"mim_id":"614879","title":"PEROXISOME BIOGENESIS DISORDER 9B; PBD9B","url":"https://www.omim.org/entry/614879"},{"mim_id":"604443","title":"ACYL-CoA SYNTHETASE LONG CHAIN FAMILY, MEMBER 6; ACSL6","url":"https://www.omim.org/entry/604443"},{"mim_id":"602026","title":"PHYTANOYL-CoA HYDROXYLASE; PHYH","url":"https://www.omim.org/entry/602026"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"liver","ntpm":624.2},{"tissue":"skeletal muscle","ntpm":453.0},{"tissue":"tongue","ntpm":385.4}],"url":"https://www.proteinatlas.org/search/PHYH"},"hgnc":{"alias_symbol":["PAHX","RD","PHYH1"],"prev_symbol":[]},"alphafold":{"accession":"O14832","domains":[{"cath_id":"2.60.120.620","chopping":"56-333","consensus_level":"high","plddt":90.1983,"start":56,"end":333}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O14832","model_url":"https://alphafold.ebi.ac.uk/files/AF-O14832-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O14832-F1-predicted_aligned_error_v6.png","plddt_mean":85.44},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=PHYH","jax_strain_url":"https://www.jax.org/strain/search?query=PHYH"},"sequence":{"accession":"O14832","fasta_url":"https://rest.uniprot.org/uniprotkb/O14832.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O14832/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O14832"}},"corpus_meta":[{"pmid":"9326939","id":"PMC_9326939","title":"Identification of PAHX, a Refsum disease gene.","date":"1997","source":"Nature genetics","url":"https://pubmed.ncbi.nlm.nih.gov/9326939","citation_count":177,"is_preprint":false},{"pmid":"14974078","id":"PMC_14974078","title":"Molecular basis of Refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7).","date":"2004","source":"Human mutation","url":"https://pubmed.ncbi.nlm.nih.gov/14974078","citation_count":77,"is_preprint":false},{"pmid":"15694837","id":"PMC_15694837","title":"Dual-specificity tyrosine-phosphorylated and regulated kinase 1A (DYRK1A) interacts with the phytanoyl-CoA alpha-hydroxylase associated protein 1 (PAHX-AP1), a brain specific protein.","date":"2005","source":"The international journal of biochemistry & cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/15694837","citation_count":19,"is_preprint":false},{"pmid":"17905308","id":"PMC_17905308","title":"Refsum disease due to the splice-site mutation c.135-2A>G before exon 3 of the PHYH gene, diagnosed eight years after detection of retinitis pigmentosa.","date":"2007","source":"Journal of the neurological sciences","url":"https://pubmed.ncbi.nlm.nih.gov/17905308","citation_count":7,"is_preprint":false},{"pmid":"38411969","id":"PMC_38411969","title":"PHYH c.678+5G>T Leads to In-Frame Exon Skipping and Is Associated With Attenuated Refsum Disease.","date":"2024","source":"Investigative ophthalmology & visual science","url":"https://pubmed.ncbi.nlm.nih.gov/38411969","citation_count":5,"is_preprint":false},{"pmid":"35276556","id":"PMC_35276556","title":"Single cell sequencing coupled with bioinformatics reveals PHYH as a potential biomarker in kidney ischemia reperfusion injury.","date":"2022","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/35276556","citation_count":3,"is_preprint":false},{"pmid":"29095154","id":"PMC_29095154","title":"Crystallization and X-ray diffraction analysis of native and selenomethionine-substituted PhyH-DI from Bacillus sp. HJB17.","date":"2017","source":"Acta crystallographica. Section F, Structural biology communications","url":"https://pubmed.ncbi.nlm.nih.gov/29095154","citation_count":1,"is_preprint":false},{"pmid":"18612766","id":"PMC_18612766","title":"Non-manifesting Refsum heterozygotes carrying the c.135-2A>G PAHX gene transition.","date":"2008","source":"Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology","url":"https://pubmed.ncbi.nlm.nih.gov/18612766","citation_count":1,"is_preprint":false},{"pmid":"41290216","id":"PMC_41290216","title":"Identification of novel pathogenic variants in the PHYH gene and extending the phenotypic range in Refsum disease.","date":"2025","source":"Ophthalmic genetics","url":"https://pubmed.ncbi.nlm.nih.gov/41290216","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6476,"output_tokens":1217,"usd":0.018842,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7879,"output_tokens":1719,"usd":0.041185,"stage2_stop_reason":"end_turn"},"total_usd":0.060027,"stage1_batch_id":"msgbatch_01CNoDbkChHEkgrJnL7BwtGJ","stage2_batch_id":"msgbatch_016Y4x9E9Wg5VQDANj9quSQD","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1997,\n      \"finding\": \"PAHX (PHYH) encodes a phytanoyl-CoA alpha-hydroxylase with intrinsic dioxygenase activity that requires iron as a cofactor and 2-oxoglutarate as a cosubstrate, catalyzing the alpha-hydroxylation step of phytanic acid oxidation in peroxisomes.\",\n      \"method\": \"In vitro enzymatic assay demonstrating phytanoyl-CoA alpha-hydroxylase activity; cofactor requirement established by biochemical characterization\",\n      \"journal\": \"Nature genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — direct in vitro enzymatic activity demonstrated with cofactor identification, plus functional validation via disease-causing inactivating mutations\",\n      \"pmids\": [\"9326939\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1997,\n      \"finding\": \"PHYH is targeted to peroxisomes via a type-2 peroxisomal targeting signal (PTS2) and requires the PTS2 receptor PEX7 for its peroxisomal localization.\",\n      \"method\": \"Peroxisomal targeting demonstrated by cell-based localization studies; PEX7 dependence shown by loss of localization in PEX7-deficient cells; yeast two-hybrid assay confirmed interaction between PAHX and PEX7\",\n      \"journal\": \"Nature genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal yeast two-hybrid interaction plus functional localization experiments with PEX7-deficient cells, replicated in subsequent literature\",\n      \"pmids\": [\"9326939\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1997,\n      \"finding\": \"Homozygous inactivating mutations in PHYH (PAHX) cause Refsum disease, establishing PHYH as the enzyme defective in classic Refsum disease.\",\n      \"method\": \"Mutation analysis in Refsum disease patients showing homozygous inactivating mutations; loss-of-function with phytanic acid accumulation phenotype\",\n      \"journal\": \"Nature genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — direct patient mutation analysis with biochemical phenotype confirmation, independently replicated across multiple subsequent studies\",\n      \"pmids\": [\"9326939\", \"14974078\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"Refsum disease is genetically heterogeneous, caused by mutations in either PHYH (encoding phytanoyl-CoA hydroxylase) or PEX7 (encoding the PTS2 receptor required for PHYH peroxisomal targeting), both disrupting peroxisomal alpha-oxidation of phytanic acid.\",\n      \"method\": \"Molecular genetic analysis of Refsum disease patients identifying mutations in PHYH or PEX7; mechanistic review of alpha-oxidation pathway\",\n      \"journal\": \"Human mutation\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic pathway placement across multiple patients, single review/analysis study consolidating prior findings\",\n      \"pmids\": [\"14974078\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"The PHYH splice-site variant c.678+5G>T causes in-frame skipping of exons 5 and 6 (and to a lesser extent exon 6 alone) in the canonical transcript, resulting in an attenuated form of Refsum disease with milder biochemical and clinical phenotype.\",\n      \"method\": \"RNA extracted from patient blood, reverse transcription to cDNA, PCR amplification, Oxford Nanopore single-molecule amplicon sequencing to characterize splicing outcome\",\n      \"journal\": \"Investigative ophthalmology & visual science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct RNA-level characterization with single-molecule sequencing in multiple patients, single lab study\",\n      \"pmids\": [\"38411969\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"PHYH (PAHX) encodes a peroxisomal phytanoyl-CoA alpha-hydroxylase that is targeted to peroxisomes via a PTS2 signal recognized by the receptor PEX7; once in peroxisomes, it catalyzes the iron- and 2-oxoglutarate-dependent dioxygenase reaction that alpha-hydroxylates phytanoyl-CoA as the key step in phytanic acid alpha-oxidation, and inactivating mutations in PHYH cause the autosomal recessive lipid storage disorder Refsum disease.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PHYH (PAHX) encodes phytanoyl-CoA alpha-hydroxylase, the enzyme that catalyzes the committed alpha-hydroxylation step of peroxisomal phytanic acid alpha-oxidation [#0]. It is an iron-dependent dioxygenase that uses 2-oxoglutarate as a cosubstrate to alpha-hydroxylate phytanoyl-CoA [#0]. Catalytic function requires correct subcellular delivery: PHYH carries a type-2 peroxisomal targeting signal (PTS2) and depends on the PTS2 receptor PEX7 for import into peroxisomes, an interaction confirmed by direct binding and by loss of localization in PEX7-deficient cells [#1]. Inactivating mutations in PHYH cause autosomal recessive Refsum disease, with phytanic acid accumulation as the biochemical hallmark, and the same disorder also arises from PEX7 mutations that abolish PHYH peroxisomal targeting—placing both genes on a single alpha-oxidation axis [#2, #3].\",\n  \"teleology\": [\n    {\n      \"year\": 1997,\n      \"claim\": \"Established the molecular identity and catalytic mechanism of the enzyme defective in Refsum disease by showing PHYH is an iron- and 2-oxoglutarate-dependent dioxygenase acting on phytanoyl-CoA.\",\n      \"evidence\": \"in vitro enzymatic assay with cofactor characterization\",\n      \"pmids\": [\"9326939\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No structural model of the catalytic site reported in the corpus\", \"Kinetic regulation of the enzyme not characterized\"]\n    },\n    {\n      \"year\": 1997,\n      \"claim\": \"Resolved how the enzyme reaches its compartment, demonstrating PHYH uses a PTS2 signal and the receptor PEX7 for peroxisomal import.\",\n      \"evidence\": \"cell-based localization in PEX7-deficient cells plus yeast two-hybrid interaction\",\n      \"pmids\": [\"9326939\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Stoichiometry and structural basis of the PHYH-PEX7 interaction not defined\", \"Cargo release mechanism inside the peroxisome not addressed\"]\n    },\n    {\n      \"year\": 1997,\n      \"claim\": \"Linked the gene to disease by showing homozygous inactivating PHYH mutations cause classic Refsum disease with phytanic acid accumulation.\",\n      \"evidence\": \"patient mutation analysis with biochemical phenotyping\",\n      \"pmids\": [\"9326939\", \"14974078\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Genotype-phenotype relationships across mutation classes not enumerated here\"]\n    },\n    {\n      \"year\": 2004,\n      \"claim\": \"Placed PHYH within a genetically heterogeneous disease framework, showing Refsum disease results from disruption of phytanic acid alpha-oxidation by either PHYH or PEX7 mutations.\",\n      \"evidence\": \"molecular genetic analysis across patients with mechanistic pathway review\",\n      \"pmids\": [\"14974078\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Relative frequency of PHYH versus PEX7 etiology not quantified here\", \"Single consolidating analysis\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Refined genotype-phenotype understanding by showing a splice-site variant produces in-frame exon skipping and an attenuated disease form, linking partial transcript function to milder phenotype.\",\n      \"evidence\": \"patient-derived RNA reverse transcription and Oxford Nanopore single-molecule amplicon sequencing\",\n      \"pmids\": [\"38411969\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Residual enzymatic activity of the skipped-exon protein not measured\", \"Single-lab study\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How PHYH catalytic output and import are regulated, and the structural basis of substrate and cofactor engagement, remain open.\",\n      \"evidence\": \"no direct evidence in the available corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structural data\", \"No regulation or post-translational control characterized\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0016491\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0016740\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005777\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1430728\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"PEX7\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}