{"gene":"PF3D7_0307200","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2014,"finding":"PF3D7_0307200 (L7), as a component of the P. falciparum 80S ribosome large subunit, was visualized at 3.2 Å resolution by cryo-EM in a structure of the P. falciparum 80S ribosome bound to emetine. The structure established the molecular architecture of the cytoplasmic ribosome, within which L7 resides as part of the 60S subunit.","method":"Cryo-EM structure determination at 3.2 Å resolution","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM structure of the whole ribosome complex; L7 membership in the 60S subunit is established structurally, but no functional experiment was performed specifically on L7 itself; single study","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"PF3D7_0307200 (L7), as part of the P. falciparum 60S large ribosomal subunit, was resolved in five cryo-EM reconstructions of ribosomes purified from P. falciparum blood-stage schizonts at sub-nanometer resolution, revealing structural and dynamic features that differentiate the P. falciparum ribosome from mammalian ribosomes.","method":"Cryo-EM reconstruction with flexible-fitting atomic model building; ribosome purification from blood-stage schizonts","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — sub-nanometer cryo-EM with atomic modeling; L7's role established only through complex membership, no L7-specific functional assay; single study","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"PF3D7_0307200 (L7), as part of the P. falciparum 80S ribosome 60S subunit, was resolved in a 3.2 Å cryo-EM structure of the ribosome bound to (+)-mefloquine; the structure was used to guide mutagenesis of binding-site residues and design structure-based derivatives, placing the 60S large subunit in the context of mefloquine's mode of action.","method":"Cryo-EM structure at 3.2 Å; site-directed mutagenesis of ribosome-binding residues; structure-guided drug derivative design","journal":"Nature microbiology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM with mutagenesis validation; L7 is established as a large-subunit component but no experiment specifically interrogates L7 itself; single study","pmids":["28288098"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"finding":"PF3D7_0307200 (L7) was identified as a component of the P. falciparum 60S ribosomal large subunit that exhibits heterogeneity and potential specialization across Plasmodium parasite life-cycle stages.","method":"Ribosome profiling and structural analysis described in a review/analysis of ribosome heterogeneity","journal":"PLoS pathogens","confidence":"Low","confidence_rationale":"Tier 3 / Weak — abstract does not describe specific experiments on L7; inference from ribosome heterogeneity analysis; single paper, methods not detailed in abstract","pmids":["37053161"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"PF3D7_0307200 (L7), as a 60S large-subunit component of the P. falciparum 80S ribosome, was visualized in eight high-resolution in situ cryo-electron tomography structures of the native malarial ribosome in actively translating states inside P. falciparum-infected human erythrocytes, revealing new molecular details of the translation elongation cycle and showing that a Plasmodium-specific translation inhibitor decreases elongation factor-bound ribosomal states.","method":"In situ cryo-electron tomography of P. falciparum-infected erythrocytes; eight high-resolution structures determined","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — rigorous in situ cryo-ET with multiple structures; L7 established only as a large-subunit component in the native translating ribosome complex; no L7-specific functional experiment; single study","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"PF3D7_0307200 (L7), as a component of the P. falciparum 80S ribosome, was detected in meltome-assisted profiling of protein complexes (MAP-X) across seven timepoints of the P. falciparum intraerythrocytic developmental cycle, confirming its participation in the 80S ribosome complex and revealing dynamic alterations in complex composition across blood stages.","method":"Thermal proteome profiling (MAP-X) in intact P. falciparum cells across IDC timepoints","journal":"Nature microbiology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — proteome-wide complexome profiling; L7 complex membership inferred from profiling data; no L7-specific functional experiment; single study","pmids":["41315737"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_0307200 (L7) is a component of the 60S large subunit of the P. falciparum cytoplasmic 80S ribosome, as established by multiple cryo-EM and in situ cryo-ET structures; beyond its membership in this complex, no experiment in the available literature has established a specific enzymatic activity, binding partner, post-translational modification, or loss-of-function phenotype directly attributable to L7 itself."},"narrative":{"mechanistic_narrative":"PF3D7_0307200 (L7) is a structural component of the 60S large subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, established through successive high-resolution cryo-EM structures of the parasite ribosome [PMID:24913268, PMID:26432834]. It is resolved as an integral large-subunit protein in structures of the ribosome bound to translation-targeting antimalarials, including emetine [PMID:24913268] and (+)-mefloquine [PMID:28288098], and in eight in situ cryo-electron tomography reconstructions of the native, actively translating ribosome inside infected erythrocytes [PMID:40825879]. Complexome and thermal-proteome profiling across the intraerythrocytic developmental cycle confirm L7's participation in the 80S ribosome and place it among 60S components exhibiting compositional heterogeneity across blood stages [PMID:37053161, PMID:41315737]. Beyond its membership in the 60S large subunit of the P. falciparum ribosome, no experiment in the available corpus has established a specific enzymatic activity, direct binding partner, post-translational modification, or loss-of-function phenotype attributable to L7 itself.","teleology":[{"year":2014,"claim":"The first high-resolution view of the P. falciparum ribosome placed L7 within the 60S subunit, establishing where this protein sits in the cytoplasmic translation machine.","evidence":"Cryo-EM structure of the P. falciparum 80S ribosome bound to emetine at 3.2 Å","pmids":["24913268"],"confidence":"Medium","gaps":["No functional experiment performed specifically on L7","No evidence for L7-specific binding partners beyond ribosomal context","No loss-of-function phenotype established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"Resolving L7 in ribosomes purified from blood-stage schizonts confirmed its membership in the 60S subunit and situated it among structural features distinguishing the parasite ribosome from the mammalian ribosome.","evidence":"Sub-nanometer cryo-EM reconstructions with flexible-fitting atomic modeling of schizont-derived ribosomes","pmids":["26432834"],"confidence":"Medium","gaps":["L7 role inferred only from complex membership","Parasite-specific features not localized to L7 specifically","No functional consequence of the structural differences tested for L7"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"A drug-bound structure kept L7 in the 60S subunit while guiding mutagenesis of ribosomal binding-site residues, framing the large subunit in the context of antimalarial mode of action.","evidence":"3.2 Å cryo-EM of the ribosome bound to (+)-mefloquine with site-directed mutagenesis and structure-guided derivative design","pmids":["28288098"],"confidence":"Medium","gaps":["Mutagenesis targeted the drug-binding site, not L7 itself","No direct role of L7 in drug binding or resistance established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"claim":"Analysis of ribosome heterogeneity across the life cycle raised the possibility that 60S components including L7 contribute to stage-specific ribosome specialization.","evidence":"Ribosome profiling and structural analysis reported in a review/analysis of ribosome heterogeneity","pmids":["37053161"],"confidence":"Low","gaps":["Abstract does not describe experiments specific to L7","Specialization is inferred, not demonstrated functionally for L7","No mechanism for stage-specific behavior established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"In situ cryo-ET of native translating ribosomes and thermal-proteome complexome profiling confirmed L7 as a 60S component within actively elongating ribosomes and tracked its complex participation across blood-stage timepoints.","evidence":"Eight in situ cryo-ET structures in infected erythrocytes [#4] and MAP-X thermal proteome profiling across seven IDC timepoints [#5]","pmids":["40825879","41315737"],"confidence":"Medium","gaps":["L7 established only as a large-subunit component of the translating ribosome","No L7-specific functional assay in the elongation cycle","Dynamic complex changes not resolved to L7-specific behavior"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether L7 has any function, interaction, modification, or phenotype beyond its structural membership in the 60S subunit remains unaddressed by the available corpus.","evidence":"No experiment in the timeline interrogates L7 directly","pmids":[],"confidence":"Low","gaps":["No L7-specific enzymatic activity or binding partner identified","No genetic loss-of-function or knockdown of L7","No post-translational modification characterized for L7"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["P. falciparum 80S cytoplasmic ribosome","60S large ribosomal subunit"],"partners":[],"other_free_text":["L7 is characterized in the corpus solely as a structural component of the P. falciparum 60S large ribosomal subunit; no direct binding partner, enzymatic activity, PTM, or loss-of-function phenotype attributable to L7 itself has been established.","Structures placing L7 within the ribosome were determined in the context of antimalarial mechanism studies (emetine, (+)-mefloquine, a Plasmodium-specific elongation inhibitor), but no experiment implicates L7 directly in drug binding.","Complexome and heterogeneity profiling indicate 60S composition varies across the intraerythrocytic developmental cycle, without demonstrating L7-specific specialization."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"24913268","id":"PMC_24913268","title":"Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine.","date":"2014","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/24913268","citation_count":272,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28288098","id":"PMC_28288098","title":"Mefloquine targets the Plasmodium falciparum 80S ribosome to inhibit protein synthesis.","date":"2017","source":"Nature microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/28288098","citation_count":136,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26432834","id":"PMC_26432834","title":"Dynamical features of the Plasmodium falciparum ribosome during translation.","date":"2015","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/26432834","citation_count":45,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40825879","id":"PMC_40825879","title":"Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug.","date":"2025","source":"Nature structural & molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/40825879","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40480224","id":"PMC_40480224","title":"Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome.","date":"2025","source":"Structure (London, England : 1993)","url":"https://pubmed.ncbi.nlm.nih.gov/40480224","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"29626096","id":"PMC_29626096","title":"The mitochondrial ribosomal protein L13 is critical for the structural and functional integrity of the mitochondrion in Plasmodium falciparum.","date":"2018","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/29626096","citation_count":53,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32273345","id":"PMC_32273345","title":"Genetic ablation of the mitoribosome in the malaria parasite Plasmodium falciparum sensitizes it to antimalarials that target mitochondrial functions.","date":"2020","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/32273345","citation_count":27,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32469313","id":"PMC_32469313","title":"Plasmodium falciparum translational machinery condones polyadenosine repeats.","date":"2020","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/32469313","citation_count":21,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"29190277","id":"PMC_29190277","title":"malERA: An updated research agenda for basic science and enabling technologies in malaria elimination and eradication.","date":"2017","source":"PLoS medicine","url":"https://pubmed.ncbi.nlm.nih.gov/29190277","citation_count":21,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37053161","id":"PMC_37053161","title":"Ribosome heterogeneity and specialization of Plasmodium parasites.","date":"2023","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/37053161","citation_count":13,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"31866984","id":"PMC_31866984","title":"Adaptation of Translational Machinery in Malaria Parasites to Accommodate Translation of Poly-Adenosine Stretches Throughout Its Life Cycle.","date":"2019","source":"Frontiers in microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/31866984","citation_count":11,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"27732881","id":"PMC_27732881","title":"Receptor for Activated C-Kinase 1 (PfRACK1) is required for Plasmodium falciparum intra-erythrocytic proliferation.","date":"2016","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/27732881","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34017052","id":"PMC_34017052","title":"Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation.","date":"2021","source":"Communications biology","url":"https://pubmed.ncbi.nlm.nih.gov/34017052","citation_count":6,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35452681","id":"PMC_35452681","title":"Association of the receptor for activated C-kinase 1 with ribosomes in Plasmodium falciparum.","date":"2022","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/35452681","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"41315737","id":"PMC_41315737","title":"MAP-X reveals distinct protein complex dynamics across Plasmodium falciparum blood stages.","date":"2025","source":"Nature microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/41315737","citation_count":2,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28540920","id":"PMC_28540920","title":"Parasite physiology: No longer lost in translation.","date":"2017","source":"Nature microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/28540920","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"42001110","id":"PMC_42001110","title":"Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.","date":"2026","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/42001110","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":9643,"output_tokens":1797,"usd":0.027942,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6824,"output_tokens":2537,"usd":0.048773,"stage2_stop_reason":"end_turn"},"total_usd":0.076715,"stage1_batch_id":"msgbatch_01DbiymDmubkPpYvdbAu5a7V","stage2_batch_id":"msgbatch_012TbrWvMRH129T7PQ4SmvrJ","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"PF3D7_0307200 (L7), as a component of the P. falciparum 80S ribosome large subunit, was visualized at 3.2 Å resolution by cryo-EM in a structure of the P. falciparum 80S ribosome bound to emetine. The structure established the molecular architecture of the cytoplasmic ribosome, within which L7 resides as part of the 60S subunit.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM structure of the whole ribosome complex; L7 membership in the 60S subunit is established structurally, but no functional experiment was performed specifically on L7 itself; single study\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"PF3D7_0307200 (L7), as part of the P. falciparum 60S large ribosomal subunit, was resolved in five cryo-EM reconstructions of ribosomes purified from P. falciparum blood-stage schizonts at sub-nanometer resolution, revealing structural and dynamic features that differentiate the P. falciparum ribosome from mammalian ribosomes.\",\n      \"method\": \"Cryo-EM reconstruction with flexible-fitting atomic model building; ribosome purification from blood-stage schizonts\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — sub-nanometer cryo-EM with atomic modeling; L7's role established only through complex membership, no L7-specific functional assay; single study\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"PF3D7_0307200 (L7), as part of the P. falciparum 80S ribosome 60S subunit, was resolved in a 3.2 Å cryo-EM structure of the ribosome bound to (+)-mefloquine; the structure was used to guide mutagenesis of binding-site residues and design structure-based derivatives, placing the 60S large subunit in the context of mefloquine's mode of action.\",\n      \"method\": \"Cryo-EM structure at 3.2 Å; site-directed mutagenesis of ribosome-binding residues; structure-guided drug derivative design\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM with mutagenesis validation; L7 is established as a large-subunit component but no experiment specifically interrogates L7 itself; single study\",\n      \"pmids\": [\"28288098\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"PF3D7_0307200 (L7) was identified as a component of the P. falciparum 60S ribosomal large subunit that exhibits heterogeneity and potential specialization across Plasmodium parasite life-cycle stages.\",\n      \"method\": \"Ribosome profiling and structural analysis described in a review/analysis of ribosome heterogeneity\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — abstract does not describe specific experiments on L7; inference from ribosome heterogeneity analysis; single paper, methods not detailed in abstract\",\n      \"pmids\": [\"37053161\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"PF3D7_0307200 (L7), as a 60S large-subunit component of the P. falciparum 80S ribosome, was visualized in eight high-resolution in situ cryo-electron tomography structures of the native malarial ribosome in actively translating states inside P. falciparum-infected human erythrocytes, revealing new molecular details of the translation elongation cycle and showing that a Plasmodium-specific translation inhibitor decreases elongation factor-bound ribosomal states.\",\n      \"method\": \"In situ cryo-electron tomography of P. falciparum-infected erythrocytes; eight high-resolution structures determined\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — rigorous in situ cryo-ET with multiple structures; L7 established only as a large-subunit component in the native translating ribosome complex; no L7-specific functional experiment; single study\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"PF3D7_0307200 (L7), as a component of the P. falciparum 80S ribosome, was detected in meltome-assisted profiling of protein complexes (MAP-X) across seven timepoints of the P. falciparum intraerythrocytic developmental cycle, confirming its participation in the 80S ribosome complex and revealing dynamic alterations in complex composition across blood stages.\",\n      \"method\": \"Thermal proteome profiling (MAP-X) in intact P. falciparum cells across IDC timepoints\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — proteome-wide complexome profiling; L7 complex membership inferred from profiling data; no L7-specific functional experiment; single study\",\n      \"pmids\": [\"41315737\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_0307200 (L7) is a component of the 60S large subunit of the P. falciparum cytoplasmic 80S ribosome, as established by multiple cryo-EM and in situ cryo-ET structures; beyond its membership in this complex, no experiment in the available literature has established a specific enzymatic activity, binding partner, post-translational modification, or loss-of-function phenotype directly attributable to L7 itself.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0307200 (L7) is a structural component of the 60S large subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, established through successive high-resolution cryo-EM structures of the parasite ribosome [#0, #1]. It is resolved as an integral large-subunit protein in structures of the ribosome bound to translation-targeting antimalarials, including emetine [#0] and (+)-mefloquine [#2], and in eight in situ cryo-electron tomography reconstructions of the native, actively translating ribosome inside infected erythrocytes [#4]. Complexome and thermal-proteome profiling across the intraerythrocytic developmental cycle confirm L7's participation in the 80S ribosome and place it among 60S components exhibiting compositional heterogeneity across blood stages [#3, #5]. Beyond its membership in the 60S large subunit of the P. falciparum ribosome, no experiment in the available corpus has established a specific enzymatic activity, direct binding partner, post-translational modification, or loss-of-function phenotype attributable to L7 itself.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"The first high-resolution view of the P. falciparum ribosome placed L7 within the 60S subunit, establishing where this protein sits in the cytoplasmic translation machine.\",\n      \"evidence\": \"Cryo-EM structure of the P. falciparum 80S ribosome bound to emetine at 3.2 Å\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No functional experiment performed specifically on L7\",\n        \"No evidence for L7-specific binding partners beyond ribosomal context\",\n        \"No loss-of-function phenotype established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Resolving L7 in ribosomes purified from blood-stage schizonts confirmed its membership in the 60S subunit and situated it among structural features distinguishing the parasite ribosome from the mammalian ribosome.\",\n      \"evidence\": \"Sub-nanometer cryo-EM reconstructions with flexible-fitting atomic modeling of schizont-derived ribosomes\",\n      \"pmids\": [\"26432834\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"L7 role inferred only from complex membership\",\n        \"Parasite-specific features not localized to L7 specifically\",\n        \"No functional consequence of the structural differences tested for L7\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"A drug-bound structure kept L7 in the 60S subunit while guiding mutagenesis of ribosomal binding-site residues, framing the large subunit in the context of antimalarial mode of action.\",\n      \"evidence\": \"3.2 Å cryo-EM of the ribosome bound to (+)-mefloquine with site-directed mutagenesis and structure-guided derivative design\",\n      \"pmids\": [\"28288098\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mutagenesis targeted the drug-binding site, not L7 itself\",\n        \"No direct role of L7 in drug binding or resistance established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Analysis of ribosome heterogeneity across the life cycle raised the possibility that 60S components including L7 contribute to stage-specific ribosome specialization.\",\n      \"evidence\": \"Ribosome profiling and structural analysis reported in a review/analysis of ribosome heterogeneity\",\n      \"pmids\": [\"37053161\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Abstract does not describe experiments specific to L7\",\n        \"Specialization is inferred, not demonstrated functionally for L7\",\n        \"No mechanism for stage-specific behavior established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"In situ cryo-ET of native translating ribosomes and thermal-proteome complexome profiling confirmed L7 as a 60S component within actively elongating ribosomes and tracked its complex participation across blood-stage timepoints.\",\n      \"evidence\": \"Eight in situ cryo-ET structures in infected erythrocytes [#4] and MAP-X thermal proteome profiling across seven IDC timepoints [#5]\",\n      \"pmids\": [\"40825879\", \"41315737\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"L7 established only as a large-subunit component of the translating ribosome\",\n        \"No L7-specific functional assay in the elongation cycle\",\n        \"Dynamic complex changes not resolved to L7-specific behavior\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether L7 has any function, interaction, modification, or phenotype beyond its structural membership in the 60S subunit remains unaddressed by the available corpus.\",\n      \"evidence\": \"No experiment in the timeline interrogates L7 directly\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No L7-specific enzymatic activity or binding partner identified\",\n        \"No genetic loss-of-function or knockdown of L7\",\n        \"No post-translational modification characterized for L7\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003735\", \"supporting_discovery_ids\": [0, 1, 4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0022625\", \"supporting_discovery_ids\": [0, 1, 2, 4]},\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006412\", \"supporting_discovery_ids\": [0, 4]},\n      {\"term_id\": \"GO:0006414\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"complexes\": [\n      \"P. falciparum 80S cytoplasmic ribosome\",\n      \"60S large ribosomal subunit\"\n    ],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"L7 is characterized in the corpus solely as a structural component of the P. falciparum 60S large ribosomal subunit; no direct binding partner, enzymatic activity, PTM, or loss-of-function phenotype attributable to L7 itself has been established.\",\n      \"Structures placing L7 within the ribosome were determined in the context of antimalarial mechanism studies (emetine, (+)-mefloquine, a Plasmodium-specific elongation inhibitor), but no experiment implicates L7 directly in drug binding.\",\n      \"Complexome and heterogeneity profiling indicate 60S composition varies across the intraerythrocytic developmental cycle, without demonstrating L7-specific specialization.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0307200","name":null,"product":"60S ribosomal protein L7, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0405500","name":null,"product":"60S ribosomal protein L7, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0835500","name":null,"product":"60S ribosomal protein L7, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}