{"gene":"PF3D7_1431700","run_date":"2026-09-08T14:19:07","timeline":{"discoveries":[{"year":2014,"finding":"The cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution was solved with emetine bound, revealing L14 (PF3D7_1431700) as a component of the large (60S) ribosomal subunit within the assembled 80S complex.","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 intact 80S ribosome establishes L14 as a structural component, but the abstract does not describe specific functional experiments on L14 itself; single study.","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"Sub-nanometer cryo-EM reconstructions of ribosomes purified from P. falciparum blood-stage schizonts, with atomic model building by flexible fitting, confirm L14 (PF3D7_1431700) as a structural constituent of the 60S subunit of the actively translating 80S ribosome.","method":"cryo-EM with flexible fitting of atomic models from density maps","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — multiple cryo-EM reconstructions with atomic model building in a single study; no specific functional experiments targeting L14 directly.","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"A 3.2 Å cryo-EM structure of the P. falciparum 80S ribosome with mefloquine bound to the GTPase-associated centre further establishes L14 (PF3D7_1431700) as a structural component of the 60S ribosomal subunit within the drug-bound complex.","method":"cryo-EM structure determination at 3.2 Å; site-directed mutagenesis of binding residues","journal":"Nature microbiology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM plus mutagenesis confirms the ribosome complex, but experiments focused on mefloquine-binding residues, not on L14 specifically; single study.","pmids":["28288098"],"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, placing L14 (PF3D7_1431700) within the 60S subunit of the ribosome as it operates inside the native cellular context during translation elongation.","method":"in situ cryo-electron tomography inside P. falciparum-infected human erythrocytes","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in situ cryo-ET in native cellular context is a rigorous structural approach, but the abstract does not report specific functional experiments on L14 itself; single study.","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1431700 (L14) is established as a structural component of the 60S large ribosomal subunit of the P. falciparum 80S ribosome, as visualised by multiple cryo-EM and in situ cryo-ET studies of the assembled translating ribosome complex; no specific catalytic activity or direct binding partners of L14 itself have been experimentally defined beyond its membership in this complex."},"narrative":{"mechanistic_narrative":"PF3D7_1431700 (L14) is a structural component of the large (60S) subunit of the Plasmodium falciparum 80S ribosome, resolved as part of the assembled particle in successive cryo-EM structures of the intact ribosome [PMID:24913268, PMID:26432834]. It is present within the 60S subunit of actively translating ribosomes purified from blood-stage schizonts and of drug-bound complexes, and in situ cryo-electron tomography places L14 within the 60S subunit of the native ribosome as it operates during translation elongation inside infected erythrocytes [PMID:26432834, PMID:28288098, PMID:40825879]. Beyond this membership in the 60S subunit of the translating ribosome, no specific catalytic activity or direct binding partner of L14 itself has been characterized in the available corpus.","teleology":[{"year":2014,"claim":"Whether L14 is a constituent of the P. falciparum ribosome was resolved by the first high-resolution structure of the intact 80S particle, establishing it as a 60S subunit component.","evidence":"cryo-EM structure of the emetine-bound P. falciparum 80S ribosome at 3.2 Å","pmids":["24913268"],"confidence":"Medium","gaps":["no functional experiment targeting L14 itself","no direct binding partner of L14 defined beyond the complex","no catalytic role assigned"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"Whether L14's placement held in ribosomes engaged in active translation was addressed by reconstructions from blood-stage schizonts, confirming it as a structural constituent of the translating 60S subunit.","evidence":"sub-nanometer cryo-EM with flexible fitting of atomic models from schizont-purified ribosomes","pmids":["26432834"],"confidence":"Medium","gaps":["no assembly or stability role for L14 tested","does not define L14 interactions within the subunit"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"The persistence of L14 as a 60S component in a drug-bound ribosome was confirmed, though the study's functional focus was the mefloquine-binding GTPase-associated centre rather than L14.","evidence":"cryo-EM at 3.2 Å with site-directed mutagenesis of mefloquine-binding residues","pmids":["28288098"],"confidence":"Medium","gaps":["mutagenesis targeted drug-binding residues, not L14","no direct link between L14 and drug binding"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether L14's structural placement holds within the native cellular ribosome was addressed by in situ cryo-ET, positioning L14 in the 60S subunit of ribosomes actively translating inside infected erythrocytes.","evidence":"in situ cryo-electron tomography of P. falciparum-infected human erythrocytes, eight structures of translating states","pmids":["40825879"],"confidence":"Medium","gaps":["no functional experiment on L14 itself","role of L14 in elongation dynamics not isolated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether L14 has any function beyond its structural membership in the 60S subunit — catalytic activity, direct binding partners, or a role in ribosome assembly — remains unaddressed.","evidence":"no discovery in the corpus targets L14 with a direct functional or biochemical assay","pmids":[],"confidence":"Medium","gaps":["no gene-specific knockdown or knockout phenotype","no direct L14 interaction mapping","no catalytic function defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["60S large ribosomal subunit of the P. falciparum 80S ribosome"],"partners":[],"other_free_text":["L14 (PF3D7_1431700) is documented only as a structural constituent of the 60S subunit; no direct binding partner or catalytic activity of L14 itself has been experimentally defined in the corpus.","Structural placement of L14 is confirmed across emetine-bound, mefloquine-bound, schizont-purified, and native in situ translating ribosome states."]}},"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":1125,"usd":0.015693,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5908,"output_tokens":1863,"usd":0.038058,"stage2_stop_reason":"end_turn"},"total_usd":0.053751,"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\": \"The cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution was solved with emetine bound, revealing L14 (PF3D7_1431700) as a component of the large (60S) ribosomal subunit within the assembled 80S complex.\",\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 intact 80S ribosome establishes L14 as a structural component, but the abstract does not describe specific functional experiments on L14 itself; single study.\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Sub-nanometer cryo-EM reconstructions of ribosomes purified from P. falciparum blood-stage schizonts, with atomic model building by flexible fitting, confirm L14 (PF3D7_1431700) as a structural constituent of the 60S subunit of the actively translating 80S ribosome.\",\n      \"method\": \"cryo-EM with flexible fitting of atomic models from density maps\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — multiple cryo-EM reconstructions with atomic model building in a single study; no specific functional experiments targeting L14 directly.\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"A 3.2 Å cryo-EM structure of the P. falciparum 80S ribosome with mefloquine bound to the GTPase-associated centre further establishes L14 (PF3D7_1431700) as a structural component of the 60S ribosomal subunit within the drug-bound complex.\",\n      \"method\": \"cryo-EM structure determination at 3.2 Å; site-directed mutagenesis of binding residues\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM plus mutagenesis confirms the ribosome complex, but experiments focused on mefloquine-binding residues, not on L14 specifically; single study.\",\n      \"pmids\": [\"28288098\"],\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, placing L14 (PF3D7_1431700) within the 60S subunit of the ribosome as it operates inside the native cellular context during translation elongation.\",\n      \"method\": \"in situ cryo-electron tomography inside P. falciparum-infected human erythrocytes\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in situ cryo-ET in native cellular context is a rigorous structural approach, but the abstract does not report specific functional experiments on L14 itself; single study.\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1431700 (L14) is established as a structural component of the 60S large ribosomal subunit of the P. falciparum 80S ribosome, as visualised by multiple cryo-EM and in situ cryo-ET studies of the assembled translating ribosome complex; no specific catalytic activity or direct binding partners of L14 itself have been experimentally defined beyond its membership in this complex.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1431700 (L14) is a structural component of the large (60S) subunit of the Plasmodium falciparum 80S ribosome, resolved as part of the assembled particle in successive cryo-EM structures of the intact ribosome [#0, #1]. It is present within the 60S subunit of actively translating ribosomes purified from blood-stage schizonts and of drug-bound complexes, and in situ cryo-electron tomography places L14 within the 60S subunit of the native ribosome as it operates during translation elongation inside infected erythrocytes [#1, #2, #3]. Beyond this membership in the 60S subunit of the translating ribosome, no specific catalytic activity or direct binding partner of L14 itself has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether L14 is a constituent of the P. falciparum ribosome was resolved by the first high-resolution structure of the intact 80S particle, establishing it as a 60S subunit component.\",\n      \"evidence\": \"cryo-EM structure of the emetine-bound P. falciparum 80S ribosome at 3.2 Å\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"no functional experiment targeting L14 itself\",\n        \"no direct binding partner of L14 defined beyond the complex\",\n        \"no catalytic role assigned\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Whether L14's placement held in ribosomes engaged in active translation was addressed by reconstructions from blood-stage schizonts, confirming it as a structural constituent of the translating 60S subunit.\",\n      \"evidence\": \"sub-nanometer cryo-EM with flexible fitting of atomic models from schizont-purified ribosomes\",\n      \"pmids\": [\"26432834\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"no assembly or stability role for L14 tested\",\n        \"does not define L14 interactions within the subunit\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"The persistence of L14 as a 60S component in a drug-bound ribosome was confirmed, though the study's functional focus was the mefloquine-binding GTPase-associated centre rather than L14.\",\n      \"evidence\": \"cryo-EM at 3.2 Å with site-directed mutagenesis of mefloquine-binding residues\",\n      \"pmids\": [\"28288098\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"mutagenesis targeted drug-binding residues, not L14\",\n        \"no direct link between L14 and drug binding\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether L14's structural placement holds within the native cellular ribosome was addressed by in situ cryo-ET, positioning L14 in the 60S subunit of ribosomes actively translating inside infected erythrocytes.\",\n      \"evidence\": \"in situ cryo-electron tomography of P. falciparum-infected human erythrocytes, eight structures of translating states\",\n      \"pmids\": [\"40825879\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"no functional experiment on L14 itself\",\n        \"role of L14 in elongation dynamics not isolated\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether L14 has any function beyond its structural membership in the 60S subunit — catalytic activity, direct binding partners, or a role in ribosome assembly — remains unaddressed.\",\n      \"evidence\": \"no discovery in the corpus targets L14 with a direct functional or biochemical assay\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"no gene-specific knockdown or knockout phenotype\",\n        \"no direct L14 interaction mapping\",\n        \"no catalytic function defined\"\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, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0022625\", \"supporting_discovery_ids\": [0, 1, 2, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006414\", \"supporting_discovery_ids\": [1, 3]}\n    ],\n    \"complexes\": [\n      \"60S large ribosomal subunit of the P. falciparum 80S ribosome\"\n    ],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"L14 (PF3D7_1431700) is documented only as a structural constituent of the 60S subunit; no direct binding partner or catalytic activity of L14 itself has been experimentally defined in the corpus.\",\n      \"Structural placement of L14 is confirmed across emetine-bound, mefloquine-bound, schizont-purified, and native in situ translating ribosome states.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1431700","name":null,"product":"60S ribosomal protein L14, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1013100","name":null,"product":"60S ribosomal protein L14, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1327000","name":null,"product":"60S ribosomal protein L14, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}