{"gene":"PF3D7_0519400","run_date":"2026-09-07T10:55:52","timeline":{"discoveries":[{"year":2014,"finding":"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the small (40S) subunit architecture, within which RPS24 (PF3D7_0519400) is a constituent protein; the structure showed emetine binding at the E-site of the small subunit and blocking mRNA/tRNA translocation.","method":"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome in complex with emetine","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM structure with functional drug-binding validation, but RPS24 itself is only identified as a subunit component; no specific functional data reported for RPS24 individually beyond complex membership","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"Sub-nanometer cryo-EM reconstructions of the P. falciparum 80S ribosome purified from blood-stage schizonts captured multiple translational states; RPS24 (PF3D7_0519400) is a structural component of the small subunit in these atomic models, and structural/dynamic features differentiating the parasite ribosome from mammalian ribosomes were identified.","method":"Cryo-EM with multiple reconstructions and flexible-fitting atomic model building from P. falciparum schizont-purified ribosomes","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — multiple cryo-EM reconstructions with atomic models from a single lab; RPS24 is identified as a 40S subunit component but no specific functional experiment targets it individually","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"In situ cryo-electron tomography of P. falciparum-infected human erythrocytes determined eight high-resolution structures of the native malarial 80S ribosome in actively translating states; RPS24 (PF3D7_0519400) is a component of the 40S subunit visualized in these native cellular structures. Treatment with a Plasmodium-specific translation inhibitor decreased elongation factor-bound ribosomal states and was associated with apparent upregulation of ribosome biogenesis.","method":"In situ cryo-electron tomography of P. falciparum-infected erythrocytes; high-resolution structural determination of eight translating ribosome states; drug perturbation experiments","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution in situ cryo-ET with functional drug perturbation, but RPS24 is only identified as a 40S subunit component with no individual functional data","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"RPS24 (PF3D7_0519400) is a structural component of the P. falciparum 40S ribosomal small subunit, as established by multiple cryo-EM and in situ cryo-ET structures of the P. falciparum 80S ribosome; no specific enzymatic, regulatory, or interaction function has been experimentally attributed to RPS24 individually beyond its membership in the small subunit complex."},"narrative":{"mechanistic_narrative":"RPS24 (PF3D7_0519400) is a structural component of the 40S small subunit of the Plasmodium falciparum 80S ribosome, identified as a constituent protein within the small-subunit architecture resolved by cryo-EM of the parasite ribosome [PMID:24913268, PMID:26432834]. It is present in the 40S subunit across multiple captured translational states of both purified schizont ribosomes and native ribosomes visualized in situ within infected erythrocytes [PMID:26432834, PMID:40825879]. Beyond its membership in the small subunit complex, no enzymatic, regulatory, or individual interaction function has been experimentally attributed to RPS24 itself in the available corpus; the structural studies characterize the 40S subunit and drug-binding events (e.g., emetine at the small-subunit E-site) at the level of the ribosome as a whole rather than assigning any specific role to RPS24 [PMID:24913268, PMID:40825879].","teleology":[{"year":2014,"claim":"The first high-resolution structure of the P. falciparum 80S ribosome placed RPS24 within the 40S small-subunit architecture, establishing it as a constituent protein of the parasite ribosome rather than a free-standing factor.","evidence":"Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome in complex with emetine, resolving the small subunit and the emetine-bound E-site","pmids":["24913268"],"confidence":"Medium","gaps":["No functional experiment targets RPS24 individually; its role is inferred only from complex membership","No interaction, enzymatic, or regulatory activity assigned to RPS24"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"Multiple cryo-EM reconstructions of schizont-purified ribosomes confirmed RPS24 as a small-subunit component across distinct translational states and distinguished parasite-specific structural features from the mammalian ribosome.","evidence":"Sub-nanometer cryo-EM with flexible-fitting atomic model building from P. falciparum schizont-purified 80S ribosomes","pmids":["26432834"],"confidence":"Medium","gaps":["RPS24 is modeled as part of the 40S but no dynamics or function specific to it are described","Whether RPS24 contributes to any parasite-specific structural feature is not addressed"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"In situ cryo-ET showed RPS24 as part of the 40S subunit in natively assembled, actively translating ribosomes within infected erythrocytes, extending its structural assignment from purified particles to the cellular context.","evidence":"In situ cryo-electron tomography of P. falciparum-infected erythrocytes yielding eight translating 80S ribosome states, with translation-inhibitor perturbation","pmids":["40825879"],"confidence":"Medium","gaps":["Drug perturbation acts on the whole translating ribosome, not RPS24 specifically","No individual contribution of RPS24 to elongation-factor engagement or ribosome biogenesis is defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether RPS24 has any function beyond being a structural subunit of the 40S — including a role in subunit assembly, mRNA/tRNA handling, or parasite-specific translational regulation — remains unaddressed in the corpus.","evidence":"No experiment in the timeline isolates or perturbs RPS24 individually","pmids":[],"confidence":"Medium","gaps":["No knockdown, knockout, or mutational analysis of RPS24","No RPS24-specific interaction or biochemical assay","No evidence on essentiality or druggability of RPS24 itself"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["40S small ribosomal subunit of the P. falciparum 80S ribosome"],"partners":[],"other_free_text":["RPS24 (PF3D7_0519400) is characterized in the corpus only as a structural constituent of the 40S subunit; no function specific to RPS24 beyond complex membership has been experimentally established.","Drug-binding and perturbation findings (emetine E-site binding; Plasmodium-specific translation inhibitor effects) pertain to the ribosome as a whole, not to RPS24 individually [#0, #2]."]}},"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":276,"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":46,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19595793","id":"PMC_19595793","title":"Induction of mucosal and systemic humoral immune responses in murine system by intranasal immunization with peptide antigens of P. vivax and CpG oligodeoxynucleotide (ODN) in microparticle delivery.","date":"2009","source":"International immunopharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/19595793","citation_count":19,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PvS24"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"20450288","id":"PMC_20450288","title":"Induction of cell-mediated immune responses to peptide antigens of P. vivax in microparticles using intranasal immunization.","date":"2010","source":"Immunological investigations","url":"https://pubmed.ncbi.nlm.nih.gov/20450288","citation_count":15,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PvS24"],"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":10,"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":4,"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":5493,"output_tokens":1014,"usd":0.015845,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5739,"output_tokens":1829,"usd":0.03721,"stage2_stop_reason":"end_turn"},"total_usd":0.053055,"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\": \"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the small (40S) subunit architecture, within which RPS24 (PF3D7_0519400) is a constituent protein; the structure showed emetine binding at the E-site of the small subunit and blocking mRNA/tRNA translocation.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome in complex with emetine\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM structure with functional drug-binding validation, but RPS24 itself is only identified as a subunit component; no specific functional data reported for RPS24 individually beyond complex membership\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Sub-nanometer cryo-EM reconstructions of the P. falciparum 80S ribosome purified from blood-stage schizonts captured multiple translational states; RPS24 (PF3D7_0519400) is a structural component of the small subunit in these atomic models, and structural/dynamic features differentiating the parasite ribosome from mammalian ribosomes were identified.\",\n      \"method\": \"Cryo-EM with multiple reconstructions and flexible-fitting atomic model building from P. falciparum schizont-purified ribosomes\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — multiple cryo-EM reconstructions with atomic models from a single lab; RPS24 is identified as a 40S subunit component but no specific functional experiment targets it individually\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"In situ cryo-electron tomography of P. falciparum-infected human erythrocytes determined eight high-resolution structures of the native malarial 80S ribosome in actively translating states; RPS24 (PF3D7_0519400) is a component of the 40S subunit visualized in these native cellular structures. Treatment with a Plasmodium-specific translation inhibitor decreased elongation factor-bound ribosomal states and was associated with apparent upregulation of ribosome biogenesis.\",\n      \"method\": \"In situ cryo-electron tomography of P. falciparum-infected erythrocytes; high-resolution structural determination of eight translating ribosome states; drug perturbation experiments\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution in situ cryo-ET with functional drug perturbation, but RPS24 is only identified as a 40S subunit component with no individual functional data\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"RPS24 (PF3D7_0519400) is a structural component of the P. falciparum 40S ribosomal small subunit, as established by multiple cryo-EM and in situ cryo-ET structures of the P. falciparum 80S ribosome; no specific enzymatic, regulatory, or interaction function has been experimentally attributed to RPS24 individually beyond its membership in the small subunit complex.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"RPS24 (PF3D7_0519400) is a structural component of the 40S small subunit of the Plasmodium falciparum 80S ribosome, identified as a constituent protein within the small-subunit architecture resolved by cryo-EM of the parasite ribosome [#0, #1]. It is present in the 40S subunit across multiple captured translational states of both purified schizont ribosomes and native ribosomes visualized in situ within infected erythrocytes [#1, #2]. Beyond its membership in the small subunit complex, no enzymatic, regulatory, or individual interaction function has been experimentally attributed to RPS24 itself in the available corpus; the structural studies characterize the 40S subunit and drug-binding events (e.g., emetine at the small-subunit E-site) at the level of the ribosome as a whole rather than assigning any specific role to RPS24 [#0, #2].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"The first high-resolution structure of the P. falciparum 80S ribosome placed RPS24 within the 40S small-subunit architecture, establishing it as a constituent protein of the parasite ribosome rather than a free-standing factor.\",\n      \"evidence\": \"Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome in complex with emetine, resolving the small subunit and the emetine-bound E-site\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No functional experiment targets RPS24 individually; its role is inferred only from complex membership\", \"No interaction, enzymatic, or regulatory activity assigned to RPS24\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Multiple cryo-EM reconstructions of schizont-purified ribosomes confirmed RPS24 as a small-subunit component across distinct translational states and distinguished parasite-specific structural features from the mammalian ribosome.\",\n      \"evidence\": \"Sub-nanometer cryo-EM with flexible-fitting atomic model building from P. falciparum schizont-purified 80S ribosomes\",\n      \"pmids\": [\"26432834\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"RPS24 is modeled as part of the 40S but no dynamics or function specific to it are described\", \"Whether RPS24 contributes to any parasite-specific structural feature is not addressed\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"In situ cryo-ET showed RPS24 as part of the 40S subunit in natively assembled, actively translating ribosomes within infected erythrocytes, extending its structural assignment from purified particles to the cellular context.\",\n      \"evidence\": \"In situ cryo-electron tomography of P. falciparum-infected erythrocytes yielding eight translating 80S ribosome states, with translation-inhibitor perturbation\",\n      \"pmids\": [\"40825879\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Drug perturbation acts on the whole translating ribosome, not RPS24 specifically\", \"No individual contribution of RPS24 to elongation-factor engagement or ribosome biogenesis is defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether RPS24 has any function beyond being a structural subunit of the 40S — including a role in subunit assembly, mRNA/tRNA handling, or parasite-specific translational regulation — remains unaddressed in the corpus.\",\n      \"evidence\": \"No experiment in the timeline isolates or perturbs RPS24 individually\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No knockdown, knockout, or mutational analysis of RPS24\", \"No RPS24-specific interaction or biochemical assay\", \"No evidence on essentiality or druggability of RPS24 itself\"],\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:0022627\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006412\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"complexes\": [\"40S small ribosomal subunit of the P. falciparum 80S ribosome\"],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"RPS24 (PF3D7_0519400) is characterized in the corpus only as a structural constituent of the 40S subunit; no function specific to RPS24 beyond complex membership has been experimentally established.\",\n      \"Drug-binding and perturbation findings (emetine E-site binding; Plasmodium-specific translation inhibitor effects) pertain to the ribosome as a whole, not to RPS24 individually [#0, #2].\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0519400","name":null,"product":"40S ribosomal protein S24","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1234200","name":null,"product":"40S ribosomal protein S24, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1013700","name":null,"product":"40S ribosomal protein S24, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"RPS24","evaluation":null}