{"gene":"PF3D7_1107500","run_date":"2026-09-08T12:51:28","timeline":{"discoveries":[{"year":2022,"finding":"P. falciparum prefoldin subunit 6 (PfPFD-6) physically interacts with merozoite surface protein-1 (MSP-1), as demonstrated by pull-down assay, with in silico analysis identifying critical interface residues involved in the interaction.","method":"Pull-down assay; in silico docking analysis","journal":"FEBS open bio","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single pull-down method; in silico analysis is supporting only, no reciprocal Co-IP or functional mutagenesis validation","pmids":["33145997"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"PfPFD-6 is significantly expressed at the trophozoite and schizont stages of the asexual blood stage cycle, as determined by expression analysis.","method":"Stage-specific expression analysis (protein level)","journal":"FEBS open bio","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single method; localization/expression without functional consequence linked","pmids":["33145997"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"finding":"All six PfPrefoldin subunits (PFD1-6), including PfPFD6, interact with the Kelch13 protein (a key ART-resistance factor), as demonstrated by immunoprecipitation coupled MS/MS analysis, establishing PfPFDs as molecular participants in the artemisinin resistance mechanism.","method":"Immunoprecipitation coupled MS/MS","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — IP-MS with functional corroboration via yeast complementation, single lab","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"finding":"PfPFD6 subunits have the potential to form a heteromeric prefoldin complex with other PfPFD subunits (PFD1-6), as shown by systematic biophysical interaction analysis between all subunits.","method":"Biophysical interaction analysis (systematic pairwise)","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — systematic biophysical analysis across all subunit pairs, single lab","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"finding":"Expression of PfPFD6 in yeast PFD6 orthologous mutants reverted the yeast phenotype to artemisinin resistance, establishing a causative role of PfPFD6 in the ART resistance mechanism via functional complementation.","method":"Yeast complementation assay (orthologous PFD6 mutant rescue)","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis via cross-species complementation, single lab, single method","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"finding":"PfPFD6 interacts with α-tubulin-I (in addition to MSP-1) as a substrate, and the FDA-approved drug Biperiden blocks PfPFD6 complex formation and inhibits these interactions, suppressing parasite growth in both artemisinin-sensitive (Pf3D7) and resistant (Pf3D7k13R539T) strains.","method":"Immunoprecipitation; drug inhibition assay; parasite growth assay; ring survival assay","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (IP, growth assay, ring survival assay), single lab","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]}],"current_model":"PF3D7_1107500 (PfPFD6), a subunit of the P. falciparum heterohexameric prefoldin complex, is expressed at trophozoite and schizont stages; interacts with merozoite surface protein-1 (MSP-1), α-tubulin-I, and the artemisinin-resistance factor Kelch13 as substrates or binding partners; participates with other PfPFD subunits in complex formation; plays a causative role in artemisinin resistance (demonstrated by yeast complementation); and can be pharmacologically inhibited by Biperiden, which disrupts complex formation and kills both sensitive and resistant parasites."},"narrative":{"mechanistic_narrative":"PF3D7_1107500 (PfPFD6) is a subunit of the Plasmodium falciparum prefoldin complex that functions in protein-substrate handling and has been implicated in artemisinin resistance [PMID:38925325]. It has the capacity to assemble into a heteromeric prefoldin complex through systematic pairwise interactions with the other five PfPFD subunits (PFD1-6) [PMID:38925325]. Together with all six prefoldin subunits, PfPFD6 associates with the artemisinin-resistance factor Kelch13, and expression of PfPFD6 in yeast PFD6-orthologous mutants reverts the phenotype to artemisinin resistance, establishing a causative genetic role for this subunit in the resistance mechanism [PMID:38925325]. PfPFD6 engages client proteins, interacting with α-tubulin-I as a substrate, and its complex formation and interactions are blocked by the FDA-approved drug Biperiden, which suppresses growth of both artemisinin-sensitive (Pf3D7) and resistant (Pf3D7k13R539T) parasites [PMID:38925325]. A separate report using pull-down and in silico analysis records a physical interaction with merozoite surface protein-1 (MSP-1) and expression at the trophozoite and schizont stages [PMID:33145997]. Beyond these findings, no further mechanistic detail for PfPFD6 has been characterized in the available corpus.","teleology":[{"year":2022,"claim":"Whether PfPFD6 physically engages a defined parasite protein, and when it is expressed, was addressed to give the subunit a candidate binding partner and a stage context.","evidence":"Pull-down assay with in silico docking, plus stage-specific protein expression analysis in P. falciparum","pmids":["33145997"],"confidence":"Low","gaps":["Single pull-down without reciprocal Co-IP or functional mutagenesis validation","MSP-1 interaction interface predicted only in silico, not experimentally confirmed","Expression at trophozoite/schizont stages not linked to a functional consequence"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"claim":"Whether PfPFD6 assembles into a bona fide prefoldin complex and connects to artemisinin resistance was resolved, moving the subunit from an isolated interactor to a defined member of a resistance-associated complex.","evidence":"Systematic pairwise biophysical interaction analysis across PFD1-6 and immunoprecipitation-MS/MS against Kelch13 in P. falciparum 3D7","pmids":["38925325"],"confidence":"Medium","gaps":["Complex stoichiometry and architecture of the assembled hexamer not resolved","Whether Kelch13 is a substrate or a regulatory partner not distinguished","Single lab; no structural model of the PfPFD6-containing complex"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"claim":"Whether PfPFD6 causally contributes to artemisinin resistance was tested by cross-species genetic complementation, converting a correlative complex association into a causal claim.","evidence":"Yeast PFD6-orthologous mutant rescue by PfPFD6 expression, reverting the phenotype to artemisinin resistance","pmids":["38925325"],"confidence":"Medium","gaps":["Complementation is cross-species; direct requirement of PfPFD6 in resistant parasites not shown by parasite genetics","Molecular step by which prefoldin activity confers resistance not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"claim":"Whether PfPFD6 handles cytoskeletal clients and whether its complex is pharmacologically druggable was addressed, identifying a substrate and a candidate inhibitor active against resistant parasites.","evidence":"Immunoprecipitation identifying α-tubulin-I as substrate, plus Biperiden inhibition, parasite growth and ring survival assays in Pf3D7 and Pf3D7k13R539T","pmids":["38925325"],"confidence":"Medium","gaps":["Whether Biperiden acts directly on PfPFD6 or elsewhere in the complex not resolved","Selectivity of Biperiden over host prefoldin not established","Consequence of disrupted α-tubulin-I handling on parasite cytoskeleton not characterized"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":null,"claim":"The individual contribution of PfPFD6 to prefoldin chaperone function, its full substrate repertoire, and the mechanistic link between prefoldin activity and Kelch13-mediated artemisinin resistance remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the P. falciparum prefoldin complex or of PfPFD6","Direct parasite knockdown/knockout phenotype of PfPFD6 not reported","Mechanism connecting prefoldin substrate folding to artemisinin resistance not defined"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Prefoldin complex (PfPFD1-6 heterohexamer)"],"partners":["KELCH13 (PFK13)","PFPFD1-5 (OTHER PREFOLDIN SUBUNITS)","ALPHA-TUBULIN-I","MSP-1 (MEROZOITE SURFACE PROTEIN-1)"],"other_free_text":["Expressed at trophozoite and schizont asexual blood stages [#1]","Causative role in artemisinin resistance shown by yeast PFD6-mutant complementation [#4]","Complex formation and interactions blocked by the FDA-approved drug Biperiden, which kills both ART-sensitive (Pf3D7) and resistant (Pf3D7k13R539T) parasites [#5]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"33145997","id":"PMC_33145997","title":"Prefoldin subunit 6 of Plasmodium falciparum binds merozoite surface protein-1.","date":"2022","source":"FEBS open bio","url":"https://pubmed.ncbi.nlm.nih.gov/33145997","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["prefoldin"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38009402","id":"PMC_38009402","title":"Putative prefoldin complex subunit 5 of Plasmodium berghei is crucial for microtubule formation and parasite development in the mosquito.","date":"2023","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/38009402","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["prefoldin"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40050397","id":"PMC_40050397","title":"Targeting the mosquito prefoldin-chaperonin complex blocks Plasmodium transmission.","date":"2025","source":"Nature microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/40050397","citation_count":2,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["prefoldin"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38925325","id":"PMC_38925325","title":"Prefoldins are novel regulators of the unfolded protein response in artemisinin resistant Plasmodium falciparum malaria.","date":"2024","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/38925325","citation_count":1,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["prefoldin"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33272134","id":"PMC_33272134","title":"Comparative structural insight into prefoldin subunints of archaea and eukaryotes with special emphasis on unexplored prefoldin of Plasmodium falciparum.","date":"2020","source":"Journal of biomolecular structure & dynamics","url":"https://pubmed.ncbi.nlm.nih.gov/33272134","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["prefoldin"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5327,"output_tokens":1774,"usd":0.021295,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6384,"output_tokens":2447,"usd":0.046547,"stage2_stop_reason":"end_turn"},"total_usd":0.067842,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"I need to identify which papers are about PF3D7_1107500 (prefoldin subunit 6, PfPFD6) specifically, versus other prefoldin subunits or mosquito prefoldins.\n\n- Paper [1]: About PfPFD-6 (prefoldin subunit 6) in P. falciparum — likely PF3D7_1107500. INCLUDE.\n- Paper [2]: About PbPCS5 (prefoldin complex subunit 5) in P. berghei — this is subunit 5, not subunit 6. EXCLUDE as it's a sibling family member (different subunit).\n- Paper [3]: About mosquito (Anopheles) prefoldin complex — this is the mosquito host gene, not the Plasmodium gene. EXCLUDE (wrong organism gene).\n- Paper [4]: About all PfPFD subunits (PFD1-6), with specific functional characterization of PfPFD6. Relevant findings about PfPFD6 should be INCLUDED.\n- Paper [5]: Review/in silico analysis of PfPFD subunits — computational/structural modeling only. Only in silico findings — Tier 4. LOW confidence at best.\n\nNow extracting findings specifically about PF3D7_1107500 (PfPFD6):\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2022,\n      \"finding\": \"P. falciparum prefoldin subunit 6 (PfPFD-6) physically interacts with merozoite surface protein-1 (MSP-1), as demonstrated by pull-down assay, with in silico analysis identifying critical interface residues involved in the interaction.\",\n      \"method\": \"Pull-down assay; in silico docking analysis\",\n      \"journal\": \"FEBS open bio\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single pull-down method; in silico analysis is supporting only, no reciprocal Co-IP or functional mutagenesis validation\",\n      \"pmids\": [\"33145997\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"PfPFD-6 is significantly expressed at the trophozoite and schizont stages of the asexual blood stage cycle, as determined by expression analysis.\",\n      \"method\": \"Stage-specific expression analysis (protein level)\",\n      \"journal\": \"FEBS open bio\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single method; localization/expression without functional consequence linked\",\n      \"pmids\": [\"33145997\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"All six PfPrefoldin subunits (PFD1-6), including PfPFD6, interact with the Kelch13 protein (a key ART-resistance factor), as demonstrated by immunoprecipitation coupled MS/MS analysis, establishing PfPFDs as molecular participants in the artemisinin resistance mechanism.\",\n      \"method\": \"Immunoprecipitation coupled MS/MS\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — IP-MS with functional corroboration via yeast complementation, single lab\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"PfPFD6 subunits have the potential to form a heteromeric prefoldin complex with other PfPFD subunits (PFD1-6), as shown by systematic biophysical interaction analysis between all subunits.\",\n      \"method\": \"Biophysical interaction analysis (systematic pairwise)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — systematic biophysical analysis across all subunit pairs, single lab\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Expression of PfPFD6 in yeast PFD6 orthologous mutants reverted the yeast phenotype to artemisinin resistance, establishing a causative role of PfPFD6 in the ART resistance mechanism via functional complementation.\",\n      \"method\": \"Yeast complementation assay (orthologous PFD6 mutant rescue)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis via cross-species complementation, single lab, single method\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"PfPFD6 interacts with α-tubulin-I (in addition to MSP-1) as a substrate, and the FDA-approved drug Biperiden blocks PfPFD6 complex formation and inhibits these interactions, suppressing parasite growth in both artemisinin-sensitive (Pf3D7) and resistant (Pf3D7k13R539T) strains.\",\n      \"method\": \"Immunoprecipitation; drug inhibition assay; parasite growth assay; ring survival assay\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (IP, growth assay, ring survival assay), single lab\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1107500 (PfPFD6), a subunit of the P. falciparum heterohexameric prefoldin complex, is expressed at trophozoite and schizont stages; interacts with merozoite surface protein-1 (MSP-1), α-tubulin-I, and the artemisinin-resistance factor Kelch13 as substrates or binding partners; participates with other PfPFD subunits in complex formation; plays a causative role in artemisinin resistance (demonstrated by yeast complementation); and can be pharmacologically inhibited by Biperiden, which disrupts complex formation and kills both sensitive and resistant parasites.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1107500 (PfPFD6) is a subunit of the Plasmodium falciparum prefoldin complex that functions in protein-substrate handling and has been implicated in artemisinin resistance [#2, #4]. It has the capacity to assemble into a heteromeric prefoldin complex through systematic pairwise interactions with the other five PfPFD subunits (PFD1-6) [#3]. Together with all six prefoldin subunits, PfPFD6 associates with the artemisinin-resistance factor Kelch13, and expression of PfPFD6 in yeast PFD6-orthologous mutants reverts the phenotype to artemisinin resistance, establishing a causative genetic role for this subunit in the resistance mechanism [#2, #4]. PfPFD6 engages client proteins, interacting with \\u03b1-tubulin-I as a substrate, and its complex formation and interactions are blocked by the FDA-approved drug Biperiden, which suppresses growth of both artemisinin-sensitive (Pf3D7) and resistant (Pf3D7k13R539T) parasites [#5]. A separate report using pull-down and in silico analysis records a physical interaction with merozoite surface protein-1 (MSP-1) and expression at the trophozoite and schizont stages [#0, #1]. Beyond these findings, no further mechanistic detail for PfPFD6 has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2022,\n      \"claim\": \"Whether PfPFD6 physically engages a defined parasite protein, and when it is expressed, was addressed to give the subunit a candidate binding partner and a stage context.\",\n      \"evidence\": \"Pull-down assay with in silico docking, plus stage-specific protein expression analysis in P. falciparum\",\n      \"pmids\": [\"33145997\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single pull-down without reciprocal Co-IP or functional mutagenesis validation\",\n        \"MSP-1 interaction interface predicted only in silico, not experimentally confirmed\",\n        \"Expression at trophozoite/schizont stages not linked to a functional consequence\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Whether PfPFD6 assembles into a bona fide prefoldin complex and connects to artemisinin resistance was resolved, moving the subunit from an isolated interactor to a defined member of a resistance-associated complex.\",\n      \"evidence\": \"Systematic pairwise biophysical interaction analysis across PFD1-6 and immunoprecipitation-MS/MS against Kelch13 in P. falciparum 3D7\",\n      \"pmids\": [\"38925325\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Complex stoichiometry and architecture of the assembled hexamer not resolved\",\n        \"Whether Kelch13 is a substrate or a regulatory partner not distinguished\",\n        \"Single lab; no structural model of the PfPFD6-containing complex\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Whether PfPFD6 causally contributes to artemisinin resistance was tested by cross-species genetic complementation, converting a correlative complex association into a causal claim.\",\n      \"evidence\": \"Yeast PFD6-orthologous mutant rescue by PfPFD6 expression, reverting the phenotype to artemisinin resistance\",\n      \"pmids\": [\"38925325\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Complementation is cross-species; direct requirement of PfPFD6 in resistant parasites not shown by parasite genetics\",\n        \"Molecular step by which prefoldin activity confers resistance not defined\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Whether PfPFD6 handles cytoskeletal clients and whether its complex is pharmacologically druggable was addressed, identifying a substrate and a candidate inhibitor active against resistant parasites.\",\n      \"evidence\": \"Immunoprecipitation identifying \\u03b1-tubulin-I as substrate, plus Biperiden inhibition, parasite growth and ring survival assays in Pf3D7 and Pf3D7k13R539T\",\n      \"pmids\": [\"38925325\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether Biperiden acts directly on PfPFD6 or elsewhere in the complex not resolved\",\n        \"Selectivity of Biperiden over host prefoldin not established\",\n        \"Consequence of disrupted \\u03b1-tubulin-I handling on parasite cytoskeleton not characterized\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The individual contribution of PfPFD6 to prefoldin chaperone function, its full substrate repertoire, and the mechanistic link between prefoldin activity and Kelch13-mediated artemisinin resistance remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of the P. falciparum prefoldin complex or of PfPFD6\",\n        \"Direct parasite knockdown/knockout phenotype of PfPFD6 not reported\",\n        \"Mechanism connecting prefoldin substrate folding to artemisinin resistance not defined\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051082\", \"supporting_discovery_ids\": [3, 5]},\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [0, 2, 5]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006457\", \"supporting_discovery_ids\": [3, 5]}\n    ],\n    \"complexes\": [\"Prefoldin complex (PfPFD1-6 heterohexamer)\"],\n    \"partners\": [\n      \"Kelch13 (PfK13)\",\n      \"PfPFD1-5 (other prefoldin subunits)\",\n      \"alpha-tubulin-I\",\n      \"MSP-1 (merozoite surface protein-1)\"\n    ],\n    \"other_free_text\": [\n      \"Expressed at trophozoite and schizont asexual blood stages [#1]\",\n      \"Causative role in artemisinin resistance shown by yeast PFD6-mutant complementation [#4]\",\n      \"Complex formation and interactions blocked by the FDA-approved drug Biperiden, which kills both ART-sensitive (Pf3D7) and resistant (Pf3D7k13R539T) parasites [#5]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1107500","name":null,"product":"prefoldin, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0939400","name":null,"product":"prefoldin, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0905100","name":null,"product":"prefoldin, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}