{"gene":"PF3D7_0217800","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2014,"finding":"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution revealed the structural context of the small (40S) subunit, within which RPS26 (PF3D7_0217800) resides as a component. The structure established that emetine binds the E-site of the small subunit and blocks mRNA/tRNA translocation.","method":"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome–emetine complex","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM structure of the ribosome complex, but RPS26 itself is not individually characterized; its role is inferred solely from membership in the 40S subunit as visualized in the structure","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"Five cryo-EM reconstructions of the P. falciparum 80S ribosome from blood-stage schizonts at sub-nanometer resolution provided atomic models of the ribosome, establishing the structural context in which RPS26 (PF3D7_0217800) functions as part of the 40S small subunit. Structural and dynamic features differentiating the P. falciparum ribosome from mammalian ribosomes were identified.","method":"Cryo-EM with flexible fitting of atomic models from multiple ribosome conformational states purified from P. falciparum blood-stage schizonts","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — rigorous cryo-EM with multiple reconstructions, but RPS26 is not individually characterized; findings pertain to the ribosome complex as a whole","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"Eight high-resolution in situ cryo-ET structures of the native P. falciparum ribosome in actively translating states inside infected erythrocytes were determined, providing molecular details of the translation elongation cycle. RPS26 (PF3D7_0217800), as a component of the 40S subunit, is present in these native ribosomal complexes. Drug perturbation with a Plasmodium-specific translation inhibitor led to decreased elongation-factor-bound ribosomal states and apparent upregulation of ribosome biogenesis.","method":"In situ cryo-electron tomography (cryo-ET) at high resolution inside P. falciparum-infected human erythrocytes, with drug perturbation experiments","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — state-of-the-art in situ cryo-ET providing native ribosome structures, but RPS26 is not individually characterized; its role is inferred from membership in the 40S subunit","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_0217800 (RPS26) is established as a component of the P. falciparum 40S ribosomal small subunit, which has been structurally characterized by cryo-EM and in situ cryo-ET at high resolution; no experiment in the available literature has directly characterized the specific molecular function, interactions, or modifications of RPS26 itself beyond its membership in the 40S subunit of the malarial ribosome."},"narrative":{"mechanistic_narrative":"PF3D7_0217800 (RPS26) is a component of the small (40S) subunit of the P. falciparum 80S ribosome, within which it has been visualized structurally but not individually characterized [PMID:24913268, PMID:26432834, PMID:40825879]. High-resolution cryo-EM of the blood-stage ribosome placed RPS26 in its structural context within the 40S subunit and defined features distinguishing the malarial ribosome from its mammalian counterpart [PMID:24913268, PMID:26432834], and in situ cryo-ET of native, actively translating ribosomes inside infected erythrocytes confirmed its presence in functional 40S complexes engaged in the translation elongation cycle [PMID:40825879]. Beyond its membership in the 40S subunit, no experiment in the available corpus has directly characterized the specific molecular function, interactions, or post-translational modifications of RPS26 itself.","teleology":[{"year":2014,"claim":"Establishing the atomic architecture of the P. falciparum small ribosomal subunit was needed to place RPS26 in structural context; the first high-resolution cryo-EM structure of the 80S ribosome accomplished this and localized the drug-binding site on the small subunit.","evidence":"Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome–emetine complex","pmids":["24913268"],"confidence":"Medium","gaps":["RPS26 is resolved only as part of the 40S subunit; its individual function is not tested","No RPS26-specific interactions or modifications are addressed","Single conformational state captured with a bound inhibitor"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"Whether the malarial ribosome adopts multiple conformational states and differs structurally from the mammalian ribosome was addressed by multiple cryo-EM reconstructions, reinforcing the structural context in which RPS26 sits as a 40S component.","evidence":"Cryo-EM with flexible fitting across multiple ribosome conformational states from P. falciparum blood-stage schizonts","pmids":["26432834"],"confidence":"Medium","gaps":["Findings pertain to the ribosome as a whole, not RPS26 individually","No functional perturbation of RPS26 performed","Dynamics of RPS26 relative to the rest of the 40S not isolated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether the ribosome, and thus RPS26, could be observed in native translating states in situ was resolved by high-resolution cryo-ET inside infected erythrocytes, confirming RPS26's presence in actively elongating 40S complexes and revealing drug-induced shifts toward ribosome biogenesis.","evidence":"In situ cryo-ET at high resolution inside P. falciparum-infected human erythrocytes with translation-inhibitor perturbation","pmids":["40825879"],"confidence":"Medium","gaps":["RPS26 is inferred from 40S membership, not directly characterized","No RPS26-specific role in elongation or biogenesis demonstrated","Interactions and modifications of RPS26 remain undefined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The specific molecular function, binding partners beyond the 40S subunit, and any post-translational modifications of RPS26 (PF3D7_0217800) itself remain uncharacterized in the available corpus.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No experiment isolates RPS26's individual contribution to translation","No RPS26-specific interactome or modification data","No genetic perturbation of RPS26 in P. falciparum reported"],"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":["RPS26 (PF3D7_0217800) is established only as a component of the 40S small ribosomal subunit visualized by cryo-EM and in situ cryo-ET [#0, #1, #2]; no direct characterization of its individual molecular function, interactions, or modifications exists in the available corpus."]}},"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":"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":4452,"output_tokens":1050,"usd":0.014553,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5772,"output_tokens":1679,"usd":0.035417,"stage2_stop_reason":"end_turn"},"total_usd":0.04997,"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 structural context of the small (40S) subunit, within which RPS26 (PF3D7_0217800) resides as a component. The structure established that emetine binds the E-site of the small subunit and blocks mRNA/tRNA translocation.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution of the P. falciparum 80S ribosome–emetine complex\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM structure of the ribosome complex, but RPS26 itself is not individually characterized; its role is inferred solely from membership in the 40S subunit as visualized in the structure\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Five cryo-EM reconstructions of the P. falciparum 80S ribosome from blood-stage schizonts at sub-nanometer resolution provided atomic models of the ribosome, establishing the structural context in which RPS26 (PF3D7_0217800) functions as part of the 40S small subunit. Structural and dynamic features differentiating the P. falciparum ribosome from mammalian ribosomes were identified.\",\n      \"method\": \"Cryo-EM with flexible fitting of atomic models from multiple ribosome conformational states purified from P. falciparum blood-stage schizonts\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — rigorous cryo-EM with multiple reconstructions, but RPS26 is not individually characterized; findings pertain to the ribosome complex as a whole\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Eight high-resolution in situ cryo-ET structures of the native P. falciparum ribosome in actively translating states inside infected erythrocytes were determined, providing molecular details of the translation elongation cycle. RPS26 (PF3D7_0217800), as a component of the 40S subunit, is present in these native ribosomal complexes. Drug perturbation with a Plasmodium-specific translation inhibitor led to decreased elongation-factor-bound ribosomal states and apparent upregulation of ribosome biogenesis.\",\n      \"method\": \"In situ cryo-electron tomography (cryo-ET) at high resolution inside P. falciparum-infected human erythrocytes, with drug perturbation experiments\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — state-of-the-art in situ cryo-ET providing native ribosome structures, but RPS26 is not individually characterized; its role is inferred from membership in the 40S subunit\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"PF3D7_0217800 (RPS26) is established as a component of the P. falciparum 40S ribosomal small subunit, which has been structurally characterized by cryo-EM and in situ cryo-ET at high resolution; no experiment in the available literature has directly characterized the specific molecular function, interactions, or modifications of RPS26 itself beyond its membership in the 40S subunit of the malarial ribosome.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0217800 (RPS26) is a component of the small (40S) subunit of the P. falciparum 80S ribosome, within which it has been visualized structurally but not individually characterized [#0, #1, #2]. High-resolution cryo-EM of the blood-stage ribosome placed RPS26 in its structural context within the 40S subunit and defined features distinguishing the malarial ribosome from its mammalian counterpart [#0, #1], and in situ cryo-ET of native, actively translating ribosomes inside infected erythrocytes confirmed its presence in functional 40S complexes engaged in the translation elongation cycle [#2]. Beyond its membership in the 40S subunit, no experiment in the available corpus has directly characterized the specific molecular function, interactions, or post-translational modifications of RPS26 itself.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing the atomic architecture of the P. falciparum small ribosomal subunit was needed to place RPS26 in structural context; the first high-resolution cryo-EM structure of the 80S ribosome accomplished this and localized the drug-binding site on the small subunit.\",\n      \"evidence\": \"Cryo-EM at 3.2 Å of the P. falciparum 80S ribosome–emetine complex\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"RPS26 is resolved only as part of the 40S subunit; its individual function is not tested\",\n        \"No RPS26-specific interactions or modifications are addressed\",\n        \"Single conformational state captured with a bound inhibitor\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Whether the malarial ribosome adopts multiple conformational states and differs structurally from the mammalian ribosome was addressed by multiple cryo-EM reconstructions, reinforcing the structural context in which RPS26 sits as a 40S component.\",\n      \"evidence\": \"Cryo-EM with flexible fitting across multiple ribosome conformational states from P. falciparum blood-stage schizonts\",\n      \"pmids\": [\"26432834\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Findings pertain to the ribosome as a whole, not RPS26 individually\",\n        \"No functional perturbation of RPS26 performed\",\n        \"Dynamics of RPS26 relative to the rest of the 40S not isolated\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether the ribosome, and thus RPS26, could be observed in native translating states in situ was resolved by high-resolution cryo-ET inside infected erythrocytes, confirming RPS26's presence in actively elongating 40S complexes and revealing drug-induced shifts toward ribosome biogenesis.\",\n      \"evidence\": \"In situ cryo-ET at high resolution inside P. falciparum-infected human erythrocytes with translation-inhibitor perturbation\",\n      \"pmids\": [\"40825879\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"RPS26 is inferred from 40S membership, not directly characterized\",\n        \"No RPS26-specific role in elongation or biogenesis demonstrated\",\n        \"Interactions and modifications of RPS26 remain undefined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The specific molecular function, binding partners beyond the 40S subunit, and any post-translational modifications of RPS26 (PF3D7_0217800) itself remain uncharacterized in the available corpus.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No experiment isolates RPS26's individual contribution to translation\",\n        \"No RPS26-specific interactome or modification data\",\n        \"No genetic perturbation of RPS26 in P. falciparum reported\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [],\n    \"pathway\": [],\n    \"complexes\": [\"40S small ribosomal subunit of the P. falciparum 80S ribosome\"],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"RPS26 (PF3D7_0217800) is established only as a component of the 40S small ribosomal subunit visualized by cryo-EM and in situ cryo-ET [#0, #1, #2]; no direct characterization of its individual molecular function, interactions, or modifications exists in the available corpus.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0217800","name":null,"product":"40S ribosomal protein S26","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0314500","name":null,"product":"40S ribosomal protein S26, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0403100","name":null,"product":"40S ribosomal protein S26, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"RPS26","evaluation":null}