{"gene":"PF3D7_1309100","run_date":"2026-09-08T14:19:06","timeline":{"discoveries":[{"year":2014,"finding":"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the structural context of L24 (PF3D7_1309100) as a component of the 60S large subunit within the cytoplasmic ribosome; the structure establishes L24's membership in the assembled 80S complex but does not assign a specific mechanistic role to L24 beyond this membership.","method":"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome","journal":"eLife","confidence":"Low","confidence_rationale":"Tier 3 / Weak — structural assignment of L24 as a ribosomal component is implicit in the 80S structure but no experiment specifically probed L24 function or interactions; single study","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"Cryo-EM reconstructions of P. falciparum blood-stage schizont ribosomes at sub-nanometer resolution with atomic model building confirmed the presence and structural position of 60S subunit proteins including L24 (PF3D7_1309100) within the 80S ribosome during translation, establishing its membership in the translating ribosome.","method":"Cryo-EM reconstruction with flexible-fitting atomic model building of ribosomes purified from P. falciparum blood-stage schizonts","journal":"Nucleic acids research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — structural localization of L24 as a 60S component is inferred from the overall ribosome structure; no experiment specifically probed L24 function; single study","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"In situ cryo-electron tomography of P. falciparum-infected erythrocytes determined eight high-resolution structures of the native malarial ribosome in actively translating states, confirming L24 (PF3D7_1309100) as a structural component of the 60S subunit within the native cellular translation machinery; no specific mechanistic role for L24 beyond complex membership was established.","method":"In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes","journal":"Nature structural & molecular biology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — L24 membership in the native translating ribosome is established structurally but no experiment specifically dissects L24 function; single study","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1309100 (L24) is established as a structural component of the 60S large subunit of the P. falciparum 80S cytoplasmic ribosome, as confirmed by multiple cryo-EM and cryo-ET structures of the translating malarial ribosome, but no experiment in the available literature has assigned a specific catalytic, binding, or regulatory function to L24 beyond its membership in this complex."},"narrative":{"mechanistic_narrative":"PF3D7_1309100 (L24) is a structural component of the 60S large subunit of the Plasmodium falciparum 80S cytoplasmic ribosome, resolved as part of the assembled translation machinery in successive cryo-EM structures of the malarial ribosome [PMID:24913268, PMID:26432834]. In situ cryo-electron tomography inside P. falciparum-infected erythrocytes confirms L24 as a 60S component of the native ribosome captured in actively translating states [PMID:40825879]. Beyond this membership in the assembled 80S ribosome, no experiment in the available corpus assigns L24 a specific catalytic, binding, or regulatory function distinct from the ribosome as a whole; its individual mechanistic role has not been characterized.","teleology":[{"year":2014,"claim":"Establishing whether L24 is part of the assembled malarial ribosome required a structure of the P. falciparum 80S particle, which placed L24 within the 60S large subunit.","evidence":"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome","pmids":["24913268"],"confidence":"Low","gaps":["structural membership does not assign L24 a specific catalytic, binding, or regulatory function","no experiment probed L24 individually","no direct interaction partners of L24 mapped beyond the ribosome context"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"Confirming L24 is present during active translation extended the static structural placement by resolving its position in ribosomes purified from blood-stage schizonts.","evidence":"Cryo-EM reconstruction with flexible-fitting atomic model building of ribosomes from P. falciparum blood-stage schizonts","pmids":["26432834"],"confidence":"Low","gaps":["membership in the translating ribosome does not reveal a stage-specific or L24-specific function","no functional perturbation of L24 performed","contribution of L24 to subunit assembly or stability untested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Determining whether L24's placement holds in the native cellular environment was addressed by in situ tomography, confirming L24 as a 60S component of ribosomes actively translating inside infected erythrocytes.","evidence":"In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes yielding eight structures of actively translating ribosomes","pmids":["40825879"],"confidence":"Low","gaps":["native structural confirmation still does not define an L24-specific mechanistic role","no genetic or biochemical dissection of L24 function","no assignment of L24-specific interactions with mRNA, tRNA, or translation factors"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether L24 has any function beyond being a constituent of the 60S subunit — a role in ribosome assembly, translational regulation, or stage-specific translation — remains unaddressed in the available corpus.","evidence":"","pmids":[],"confidence":"Low","gaps":["no loss-of-function or knockdown study of L24","no biochemical characterization of L24-specific binding partners or activity","no evidence distinguishing L24's contribution from that of the ribosome as a whole"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["60S large ribosomal subunit of the P. falciparum 80S cytoplasmic ribosome"],"partners":[],"other_free_text":["L24 is established only as a structural constituent of the 60S subunit; the corpus assigns no L24-specific catalytic, binding, or regulatory function beyond ribosome membership."]}},"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}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4837,"output_tokens":935,"usd":0.014268,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5626,"output_tokens":1672,"usd":0.034965,"stage2_stop_reason":"end_turn"},"total_usd":0.049233,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the structural context of L24 (PF3D7_1309100) as a component of the 60S large subunit within the cytoplasmic ribosome; the structure establishes L24's membership in the assembled 80S complex but does not assign a specific mechanistic role to L24 beyond this membership.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — structural assignment of L24 as a ribosomal component is implicit in the 80S structure but no experiment specifically probed L24 function or interactions; single study\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Cryo-EM reconstructions of P. falciparum blood-stage schizont ribosomes at sub-nanometer resolution with atomic model building confirmed the presence and structural position of 60S subunit proteins including L24 (PF3D7_1309100) within the 80S ribosome during translation, establishing its membership in the translating ribosome.\",\n      \"method\": \"Cryo-EM reconstruction with flexible-fitting atomic model building of ribosomes purified from P. falciparum blood-stage schizonts\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — structural localization of L24 as a 60S component is inferred from the overall ribosome structure; no experiment specifically probed L24 function; single study\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"In situ cryo-electron tomography of P. falciparum-infected erythrocytes determined eight high-resolution structures of the native malarial ribosome in actively translating states, confirming L24 (PF3D7_1309100) as a structural component of the 60S subunit within the native cellular translation machinery; no specific mechanistic role for L24 beyond complex membership was established.\",\n      \"method\": \"In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — L24 membership in the native translating ribosome is established structurally but no experiment specifically dissects L24 function; single study\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1309100 (L24) is established as a structural component of the 60S large subunit of the P. falciparum 80S cytoplasmic ribosome, as confirmed by multiple cryo-EM and cryo-ET structures of the translating malarial ribosome, but no experiment in the available literature has assigned a specific catalytic, binding, or regulatory function to L24 beyond its membership in this complex.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1309100 (L24) is a structural component of the 60S large subunit of the Plasmodium falciparum 80S cytoplasmic ribosome, resolved as part of the assembled translation machinery in successive cryo-EM structures of the malarial ribosome [#0, #1]. In situ cryo-electron tomography inside P. falciparum-infected erythrocytes confirms L24 as a 60S component of the native ribosome captured in actively translating states [#2]. Beyond this membership in the assembled 80S ribosome, no experiment in the available corpus assigns L24 a specific catalytic, binding, or regulatory function distinct from the ribosome as a whole; its individual mechanistic role has not been characterized.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing whether L24 is part of the assembled malarial ribosome required a structure of the P. falciparum 80S particle, which placed L24 within the 60S large subunit.\",\n      \"evidence\": \"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"structural membership does not assign L24 a specific catalytic, binding, or regulatory function\",\n        \"no experiment probed L24 individually\",\n        \"no direct interaction partners of L24 mapped beyond the ribosome context\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Confirming L24 is present during active translation extended the static structural placement by resolving its position in ribosomes purified from blood-stage schizonts.\",\n      \"evidence\": \"Cryo-EM reconstruction with flexible-fitting atomic model building of ribosomes from P. falciparum blood-stage schizonts\",\n      \"pmids\": [\"26432834\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"membership in the translating ribosome does not reveal a stage-specific or L24-specific function\",\n        \"no functional perturbation of L24 performed\",\n        \"contribution of L24 to subunit assembly or stability untested\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Determining whether L24's placement holds in the native cellular environment was addressed by in situ tomography, confirming L24 as a 60S component of ribosomes actively translating inside infected erythrocytes.\",\n      \"evidence\": \"In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes yielding eight structures of actively translating ribosomes\",\n      \"pmids\": [\"40825879\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"native structural confirmation still does not define an L24-specific mechanistic role\",\n        \"no genetic or biochemical dissection of L24 function\",\n        \"no assignment of L24-specific interactions with mRNA, tRNA, or translation factors\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether L24 has any function beyond being a constituent of the 60S subunit — a role in ribosome assembly, translational regulation, or stage-specific translation — remains unaddressed in the available corpus.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"no loss-of-function or knockdown study of L24\",\n        \"no biochemical characterization of L24-specific binding partners or activity\",\n        \"no evidence distinguishing L24's contribution from that of the ribosome as a whole\"\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, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0022625\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006412\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"complexes\": [\n      \"60S large ribosomal subunit of the P. falciparum 80S cytoplasmic ribosome\"\n    ],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"L24 is established only as a structural constituent of the 60S subunit; the corpus assigns no L24-specific catalytic, binding, or regulatory function beyond ribosome membership.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1309100","name":null,"product":"60S ribosomal protein L24, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1407600","name":null,"product":"60S ribosomal protein L24, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1409500","name":null,"product":"60S ribosomal protein L24, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}