{"gene":"PF3D7_0721600","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2014,"finding":"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution placed PF3D7_0721600 (40S ribosomal protein S5) as a structural component of the small subunit; the structure revealed emetine binds the E-site of the small subunit to block mRNA/tRNA translocation.","method":"Cryo-EM structure determination at 3.2 Å resolution of native P. falciparum 80S ribosome in complex with emetine","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM structure establishes ribosome composition including S5, but S5-specific mechanistic detail is not individually reported; single study","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"Five cryo-EM reconstructions of ribosomes purified from P. falciparum blood-stage schizonts at sub-nanometer resolution confirmed that PF3D7_0721600 (S5) is a component of the 40S small subunit, and atomic models were built by flexible fitting; structural and dynamic features differentiating the P. falciparum ribosome from mammalian ribosomes were identified.","method":"Cryo-EM reconstruction of native P. falciparum ribosomes purified from blood-stage schizonts; flexible fitting to build atomic models","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — multiple cryo-EM structures establish ribosome composition including S5, but no S5-specific functional experiment is reported; single study","pmids":["26432834"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å with (+)-mefloquine bound to the GTPase-associated centre confirmed PF3D7_0721600 (S5) as a structural constituent of the small subunit; mefloquine binding site on the large subunit was resolved, and mutagenesis of binding residues conferred resistance.","method":"Cryo-EM structure determination at 3.2 Å; site-directed mutagenesis of mefloquine-binding residues; parasite resistance assay","journal":"Nature microbiology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution structure with mutagenesis validation; S5 is a structural component of the resolved ribosome but no S5-specific experiment performed","pmids":["28288098"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"In situ cryo-electron tomography of actively translating ribosomes inside P. falciparum-infected erythrocytes resolved eight high-resolution structures of the native malarial ribosome, confirming PF3D7_0721600 (S5) as a component of the 40S small subunit in its native cellular context; drug treatment (Plasmodium-specific translation inhibitor) caused a decrease in elongation-factor-bound ribosomal states.","method":"In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes; high-resolution structure determination of translating ribosomes","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in situ cryo-ET in native cellular context; S5 membership in the ribosome confirmed but no S5-specific experiment reported; single study","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"Meltome-assisted profiling of protein complexes (MAP-X) across seven timepoints of the P. falciparum intraerythrocytic developmental cycle predicted PF3D7_0721600 (S5) as part of the 40S ribosomal complex, with 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 screen; S5 is listed as part of the ribosomal complex but no individual mechanistic experiment performed on S5 specifically","pmids":["41315737"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_0721600 (40S ribosomal protein S5) is established as a structural component of the P. falciparum 40S small ribosomal subunit, as confirmed by multiple high-resolution cryo-EM structures of the native Pf80S ribosome; no experiment in the available literature has assigned a specific molecular function or interaction to S5 beyond its membership in the ribosomal complex."},"narrative":{"mechanistic_narrative":"PF3D7_0721600 (40S ribosomal protein S5) is a structural component of the small (40S) subunit of the Plasmodium falciparum 80S ribosome, resolved as a constituent of the native ribosome in multiple high-resolution cryo-EM structures spanning blood-stage schizonts and, most recently, in situ within infected erythrocytes [PMID:24913268, PMID:26432834, PMID:40825879]. Its placement in the small subunit is consistent across structures determined in the context of antimalarial translation inhibitors that act on the ribosome, including emetine bound at the small-subunit E-site and mefloquine bound at the large-subunit GTPase-associated centre [PMID:24913268, PMID:28288098]. Beyond its confirmed membership in the 40S subunit and its dynamic association with that complex across the intraerythrocytic developmental cycle [PMID:41315737], no experiment in the available corpus assigns S5 an individual molecular function, interaction, or phenotype distinct from the ribosomal complex.","teleology":[{"year":2014,"claim":"Establishing whether the P. falciparum ribosome could be resolved at near-atomic detail mattered for antimalarial target definition; the first cryo-EM structure placed S5 as a structural constituent of the small subunit.","evidence":"Cryo-EM at 3.2 Å of native Pf80S ribosome in complex with emetine","pmids":["24913268"],"confidence":"Medium","gaps":["No S5-specific functional experiment performed","No S5 interaction or substrate assigned beyond ribosome membership","Emetine binding is a small-subunit E-site property, not attributed to S5"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"To distinguish the parasite ribosome from the mammalian host, multiple reconstructions from blood-stage schizonts confirmed S5 as a small-subunit component within atomically modeled ribosomes.","evidence":"Cryo-EM reconstructions of native ribosomes from blood-stage schizonts with flexible-fitting atomic modeling","pmids":["26432834"],"confidence":"Medium","gaps":["S5 confirmed structurally but no individual role tested","Species-differentiating features not attributed specifically to S5"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"Resolving another antimalarial's binding site further validated the Pf80S model and again positioned S5 as a structural constituent of the small subunit.","evidence":"Cryo-EM at 3.2 Å with (+)-mefloquine bound; site-directed mutagenesis and parasite resistance assay","pmids":["28288098"],"confidence":"Medium","gaps":["Mefloquine site is on the large subunit, not linked to S5","No S5-specific mutagenesis or functional assay"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether S5's ribosomal placement holds during active translation in the native cell was addressed by in situ cryo-ET, confirming S5 in the 40S subunit within infected erythrocytes and capturing drug-induced shifts in translating states.","evidence":"In situ cryo-electron tomography of translating ribosomes inside P. falciparum-infected human erythrocytes","pmids":["40825879"],"confidence":"Medium","gaps":["S5-specific contribution to translation dynamics not isolated","Drug effect measured at the ribosome level, not attributed to S5"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether S5's association with the 40S complex varies across the parasite life cycle was probed by thermal proteome profiling, which predicted S5 within the 40S complex with dynamic compositional changes across blood stages.","evidence":"Meltome-assisted profiling of protein complexes (MAP-X) across seven IDC timepoints in intact cells","pmids":["41315737"],"confidence":"Low","gaps":["Proteome-wide prediction, not an S5-specific validated experiment","Functional consequence of dynamic complex composition unknown","No reciprocal or orthogonal confirmation for S5 individually"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"No experiment has yet assigned S5 an individual molecular function, direct interaction partner, or loss-of-function phenotype distinct from its role as a subunit of the 40S ribosome.","evidence":"","pmids":[],"confidence":"Low","gaps":["No S5-specific knockdown/knockout or rescue reported","No direct interaction mapping for S5 beyond bulk ribosome","No S5-targeted mechanistic role in translation defined"],"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":["S5 is resolved as a structural component of the native Pf80S ribosome in multiple cryo-EM structures (including in situ cryo-ET inside infected erythrocytes) but no S5-specific function, interaction, or phenotype is established in the available corpus beyond membership in the 40S subunit.","Antimalarial drug-binding sites resolved alongside S5-containing structures (emetine at the small-subunit E-site; mefloquine at the large-subunit GTPase-associated centre) are properties of the ribosome, not attributed to S5 itself."]}},"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":"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":"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":"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":"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":"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}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7152,"output_tokens":1486,"usd":0.021873,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6424,"output_tokens":2327,"usd":0.045148,"stage2_stop_reason":"end_turn"},"total_usd":0.067021,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","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 placed PF3D7_0721600 (40S ribosomal protein S5) as a structural component of the small subunit; the structure revealed emetine binds the E-site of the small subunit to block mRNA/tRNA translocation.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution of native 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 establishes ribosome composition including S5, but S5-specific mechanistic detail is not individually reported; single study\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Five cryo-EM reconstructions of ribosomes purified from P. falciparum blood-stage schizonts at sub-nanometer resolution confirmed that PF3D7_0721600 (S5) is a component of the 40S small subunit, and atomic models were built by flexible fitting; structural and dynamic features differentiating the P. falciparum ribosome from mammalian ribosomes were identified.\",\n      \"method\": \"Cryo-EM reconstruction of native P. falciparum ribosomes purified from blood-stage schizonts; flexible fitting to build atomic models\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — multiple cryo-EM structures establish ribosome composition including S5, but no S5-specific functional experiment is reported; single study\",\n      \"pmids\": [\"26432834\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å with (+)-mefloquine bound to the GTPase-associated centre confirmed PF3D7_0721600 (S5) as a structural constituent of the small subunit; mefloquine binding site on the large subunit was resolved, and mutagenesis of binding residues conferred resistance.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å; site-directed mutagenesis of mefloquine-binding residues; parasite resistance assay\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution structure with mutagenesis validation; S5 is a structural component of the resolved ribosome but no S5-specific experiment performed\",\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 actively translating ribosomes inside P. falciparum-infected erythrocytes resolved eight high-resolution structures of the native malarial ribosome, confirming PF3D7_0721600 (S5) as a component of the 40S small subunit in its native cellular context; drug treatment (Plasmodium-specific translation inhibitor) caused a decrease in elongation-factor-bound ribosomal states.\",\n      \"method\": \"In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes; high-resolution structure determination of translating ribosomes\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in situ cryo-ET in native cellular context; S5 membership in the ribosome confirmed but no S5-specific experiment reported; single study\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Meltome-assisted profiling of protein complexes (MAP-X) across seven timepoints of the P. falciparum intraerythrocytic developmental cycle predicted PF3D7_0721600 (S5) as part of the 40S ribosomal complex, with 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 screen; S5 is listed as part of the ribosomal complex but no individual mechanistic experiment performed on S5 specifically\",\n      \"pmids\": [\"41315737\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_0721600 (40S ribosomal protein S5) is established as a structural component of the P. falciparum 40S small ribosomal subunit, as confirmed by multiple high-resolution cryo-EM structures of the native Pf80S ribosome; no experiment in the available literature has assigned a specific molecular function or interaction to S5 beyond its membership in the ribosomal complex.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0721600 (40S ribosomal protein S5) is a structural component of the small (40S) subunit of the Plasmodium falciparum 80S ribosome, resolved as a constituent of the native ribosome in multiple high-resolution cryo-EM structures spanning blood-stage schizonts and, most recently, in situ within infected erythrocytes [#0, #1, #3]. Its placement in the small subunit is consistent across structures determined in the context of antimalarial translation inhibitors that act on the ribosome, including emetine bound at the small-subunit E-site and mefloquine bound at the large-subunit GTPase-associated centre [#0, #2]. Beyond its confirmed membership in the 40S subunit and its dynamic association with that complex across the intraerythrocytic developmental cycle [#4], no experiment in the available corpus assigns S5 an individual molecular function, interaction, or phenotype distinct from the ribosomal complex.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing whether the P. falciparum ribosome could be resolved at near-atomic detail mattered for antimalarial target definition; the first cryo-EM structure placed S5 as a structural constituent of the small subunit.\",\n      \"evidence\": \"Cryo-EM at 3.2 Å of native Pf80S ribosome in complex with emetine\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No S5-specific functional experiment performed\",\n        \"No S5 interaction or substrate assigned beyond ribosome membership\",\n        \"Emetine binding is a small-subunit E-site property, not attributed to S5\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"To distinguish the parasite ribosome from the mammalian host, multiple reconstructions from blood-stage schizonts confirmed S5 as a small-subunit component within atomically modeled ribosomes.\",\n      \"evidence\": \"Cryo-EM reconstructions of native ribosomes from blood-stage schizonts with flexible-fitting atomic modeling\",\n      \"pmids\": [\"26432834\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"S5 confirmed structurally but no individual role tested\",\n        \"Species-differentiating features not attributed specifically to S5\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Resolving another antimalarial's binding site further validated the Pf80S model and again positioned S5 as a structural constituent of the small subunit.\",\n      \"evidence\": \"Cryo-EM at 3.2 Å with (+)-mefloquine bound; site-directed mutagenesis and parasite resistance assay\",\n      \"pmids\": [\"28288098\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mefloquine site is on the large subunit, not linked to S5\",\n        \"No S5-specific mutagenesis or functional assay\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether S5's ribosomal placement holds during active translation in the native cell was addressed by in situ cryo-ET, confirming S5 in the 40S subunit within infected erythrocytes and capturing drug-induced shifts in translating states.\",\n      \"evidence\": \"In situ cryo-electron tomography of translating ribosomes inside P. falciparum-infected human erythrocytes\",\n      \"pmids\": [\"40825879\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"S5-specific contribution to translation dynamics not isolated\",\n        \"Drug effect measured at the ribosome level, not attributed to S5\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether S5's association with the 40S complex varies across the parasite life cycle was probed by thermal proteome profiling, which predicted S5 within the 40S complex with dynamic compositional changes across blood stages.\",\n      \"evidence\": \"Meltome-assisted profiling of protein complexes (MAP-X) across seven IDC timepoints in intact cells\",\n      \"pmids\": [\"41315737\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Proteome-wide prediction, not an S5-specific validated experiment\",\n        \"Functional consequence of dynamic complex composition unknown\",\n        \"No reciprocal or orthogonal confirmation for S5 individually\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"No experiment has yet assigned S5 an individual molecular function, direct interaction partner, or loss-of-function phenotype distinct from its role as a subunit of the 40S ribosome.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No S5-specific knockdown/knockout or rescue reported\",\n        \"No direct interaction mapping for S5 beyond bulk ribosome\",\n        \"No S5-targeted mechanistic role in translation 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, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0022627\", \"supporting_discovery_ids\": [0, 1, 2, 3, 4]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006412\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [\n      \"40S small ribosomal subunit of the P. falciparum 80S ribosome\"\n    ],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"S5 is resolved as a structural component of the native Pf80S ribosome in multiple cryo-EM structures (including in situ cryo-ET inside infected erythrocytes) but no S5-specific function, interaction, or phenotype is established in the available corpus beyond membership in the 40S subunit.\",\n      \"Antimalarial drug-binding sites resolved alongside S5-containing structures (emetine at the small-subunit E-site; mefloquine at the large-subunit GTPase-associated centre) are properties of the ribosome, not attributed to S5 itself.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0721600","name":null,"product":"40S ribosomal protein S5, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0619100","name":null,"product":"40S ribosomal protein S5, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0317000","name":null,"product":"40S ribosomal protein S5, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}