{"gene":"PF3D7_1026800","run_date":"2026-09-08T12:51:28","timeline":{"discoveries":[{"year":2014,"finding":"The cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution, which includes the 40S small subunit (containing S2/PF3D7_1026800 as a component), was solved in complex with emetine; emetine binds at the E-site of the small subunit and blocks mRNA/tRNA translocation.","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 ribosome complex, but S2 is only one of many ribosomal proteins visualized; no specific functional experiment targets S2 individually","pmids":["24913268"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"The cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution (which includes S2/PF3D7_1026800 as a small-subunit component) was solved with (+)-mefloquine bound to the GTPase-associated centre; the structure confirmed mefloquine inhibits protein synthesis by binding the ribosome.","method":"Cryo-EM structure determination at 3.2 Å resolution with mutagenesis of binding residues","journal":"Nature microbiology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-resolution cryo-EM with mutagenesis validation, but S2 is one component of the intact ribosome and is not individually targeted or functionally characterized","pmids":["28288098"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"In situ cryo-electron tomography of P. falciparum-infected erythrocytes resolved eight high-resolution structures of the native malarial ribosome (containing S2/PF3D7_1026800 as a small-subunit component) in actively translating states, revealing molecular details of the translation elongation cycle and drug-induced changes in ribosome localization.","method":"In situ cryo-electron tomography inside infected erythrocytes","journal":"Nature structural & molecular biology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in situ structural approach in native cellular context, but S2 is one of many ribosomal proteins and is not individually characterized","pmids":["40825879"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"finding":"Ribosome heterogeneity and specialization across Plasmodium parasite life-cycle stages involves differential composition of the 40S small subunit (which contains S2/PF3D7_1026800), suggesting stage-specific ribosome variants exist in Plasmodium.","method":"Ribosome fractionation and structural/proteomic analysis across life-cycle stages","journal":"PLoS pathogens","confidence":"Low","confidence_rationale":"Tier 3 / Weak — abstract does not describe specific methods in detail; S2 is inferred as a small-subunit component but is not individually studied","pmids":["37053161"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"MAP-X (meltome-assisted profiling of protein complexes) detected S2/PF3D7_1026800 as part of the ribosome complex across multiple timepoints in the P. falciparum intraerythrocytic developmental cycle, consistent with its role as a constitutive 40S small-subunit component; the approach predicted dynamic alterations in complex composition across the IDC.","method":"Thermal proteome profiling in intact cells (MAP-X) across seven IDC timepoints","journal":"Nature microbiology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — pan-complexome profiling study; S2 membership in the ribosome is confirmed by proteomic co-melting but no specific functional experiment is performed on S2 itself","pmids":["41315737"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1026800 (S2) is established as a component of the P. falciparum 40S ribosomal small subunit within the 80S cytoplasmic ribosome, whose structure has been solved by cryo-EM at atomic resolution and in situ cryo-ET in the native cellular context; beyond its membership in this complex, no specific mechanistic function has been attributed to S2 individually in the available literature."},"narrative":{"mechanistic_narrative":"PF3D7_1026800 (S2) is a component of the 40S small subunit of the P. falciparum 80S cytoplasmic ribosome, resolved as one of many small-subunit proteins in high-resolution cryo-EM structures of the intact ribosome [PMID:24913268, PMID:28288098]. These structures were determined in complex with translation-inhibiting antimalarials—emetine bound at the small-subunit E-site to block mRNA/tRNA translocation [PMID:24913268] and (+)-mefloquine bound at the GTPase-associated centre [PMID:28288098]—and the native ribosome containing S2 has been captured in actively translating elongation states by in situ cryo-electron tomography inside infected erythrocytes [PMID:40825879]. Proteomic co-melting profiling confirms S2 as a constitutive member of the ribosome complex across the intraerythrocytic developmental cycle [PMID:41315737]. Beyond its membership in the 40S subunit within the translating ribosome, no mechanistic function has been attributed to S2 individually in the available corpus; all findings characterize the ribosome as a whole rather than S2 in isolation.","teleology":[{"year":2014,"claim":"Establishing whether S2 could be placed structurally required an atomic model of the P. falciparum ribosome; the first cryo-EM structure resolved the 80S ribosome including the 40S subunit that contains S2, and localized emetine at the small-subunit E-site where it blocks translocation.","evidence":"Cryo-EM structure determination of the 80S ribosome at 3.2 Å in complex with emetine","pmids":["24913268"],"confidence":"Medium","gaps":["S2 is visualized only as one of many small-subunit proteins; no S2-specific function or interaction is tested","does not establish any role for S2 distinct from the assembled subunit"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"To define a second antimalarial's ribosomal target, the 80S structure containing S2 was solved with (+)-mefloquine bound to the GTPase-associated centre, confirming inhibition of protein synthesis at the ribosome.","evidence":"Cryo-EM at 3.2 Å with mutagenesis of the binding residues","pmids":["28288098"],"confidence":"Medium","gaps":["The drug binding site is not on or attributed to S2","S2 remains uncharacterized as an individual protein"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"claim":"The question of whether ribosome composition is uniform across the parasite life cycle was addressed by profiling 40S subunit heterogeneity, raising the possibility of stage-specific ribosome variants that include the S2-containing small subunit.","evidence":"Ribosome fractionation and structural/proteomic analysis across life-cycle stages","pmids":["37053161"],"confidence":"Low","gaps":["Methods are not described in detail in the abstract","S2 is inferred as a small-subunit member but not individually shown to vary","no functional consequence of any compositional change is demonstrated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"To move from purified structures to the native context, in situ cryo-ET resolved the S2-containing ribosome in multiple actively translating states inside infected erythrocytes, capturing elongation-cycle intermediates and drug-induced changes in ribosome localization.","evidence":"In situ cryo-electron tomography in P. falciparum-infected erythrocytes yielding eight ribosome structures","pmids":["40825879"],"confidence":"Medium","gaps":["S2 is one of many resolved proteins with no individual functional assignment","no perturbation of S2 specifically is performed"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether S2 is a stable versus dynamic ribosome component was probed by complexome-wide thermal proteome profiling, which detected S2 co-melting with the ribosome across the intraerythrocytic cycle, consistent with constitutive 40S membership.","evidence":"Meltome-assisted profiling of protein complexes (MAP-X) across seven IDC timepoints in intact cells","pmids":["41315737"],"confidence":"Low","gaps":["Membership is inferred from co-melting, not from a direct functional assay on S2","no S2-specific interaction, modification, or activity is measured"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"No experiment in the available corpus has assigned any function, interaction, or phenotype to S2/PF3D7_1026800 as an individual protein distinct from its structural membership in the 40S subunit; whether S2 has any specialized role remains unaddressed.","evidence":"Gap across the timeline","pmids":[],"confidence":"Low","gaps":["No S2-specific knockdown, knockout, or complementation","no S2-specific binding partner or post-translational regulation identified","no evidence that S2 contributes to any stage-specific ribosome specialization"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["40S small ribosomal subunit (P. falciparum)","80S cytoplasmic ribosome (P. falciparum)"],"partners":[],"other_free_text":["S2/PF3D7_1026800 is characterized only as a constitutive structural component of the 40S small subunit within the translating 80S ribosome; the cited studies target the ribosome as a whole and its antimalarial-binding sites (emetine at the small-subunit E-site [#0]; mefloquine at the GTPase-associated centre [#1]), not S2 individually.","No individual function, binding partner, or loss-of-function phenotype for S2 is established 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":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":"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":"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":"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":6766,"output_tokens":1389,"usd":0.020567,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6294,"output_tokens":2418,"usd":0.04596,"stage2_stop_reason":"end_turn"},"total_usd":0.066527,"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\": \"The cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution, which includes the 40S small subunit (containing S2/PF3D7_1026800 as a component), was solved in complex with emetine; emetine binds at the E-site of the small subunit and blocks mRNA/tRNA translocation.\",\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 ribosome complex, but S2 is only one of many ribosomal proteins visualized; no specific functional experiment targets S2 individually\",\n      \"pmids\": [\"24913268\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"The cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution (which includes S2/PF3D7_1026800 as a small-subunit component) was solved with (+)-mefloquine bound to the GTPase-associated centre; the structure confirmed mefloquine inhibits protein synthesis by binding the ribosome.\",\n      \"method\": \"Cryo-EM structure determination at 3.2 Å resolution with mutagenesis of binding residues\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-resolution cryo-EM with mutagenesis validation, but S2 is one component of the intact ribosome and is not individually targeted or functionally characterized\",\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 resolved eight high-resolution structures of the native malarial ribosome (containing S2/PF3D7_1026800 as a small-subunit component) in actively translating states, revealing molecular details of the translation elongation cycle and drug-induced changes in ribosome localization.\",\n      \"method\": \"In situ cryo-electron tomography inside infected erythrocytes\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in situ structural approach in native cellular context, but S2 is one of many ribosomal proteins and is not individually characterized\",\n      \"pmids\": [\"40825879\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Ribosome heterogeneity and specialization across Plasmodium parasite life-cycle stages involves differential composition of the 40S small subunit (which contains S2/PF3D7_1026800), suggesting stage-specific ribosome variants exist in Plasmodium.\",\n      \"method\": \"Ribosome fractionation and structural/proteomic analysis across life-cycle stages\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — abstract does not describe specific methods in detail; S2 is inferred as a small-subunit component but is not individually studied\",\n      \"pmids\": [\"37053161\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"MAP-X (meltome-assisted profiling of protein complexes) detected S2/PF3D7_1026800 as part of the ribosome complex across multiple timepoints in the P. falciparum intraerythrocytic developmental cycle, consistent with its role as a constitutive 40S small-subunit component; the approach predicted dynamic alterations in complex composition across the IDC.\",\n      \"method\": \"Thermal proteome profiling in intact cells (MAP-X) across seven IDC timepoints\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — pan-complexome profiling study; S2 membership in the ribosome is confirmed by proteomic co-melting but no specific functional experiment is performed on S2 itself\",\n      \"pmids\": [\"41315737\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1026800 (S2) is established as a component of the P. falciparum 40S ribosomal small subunit within the 80S cytoplasmic ribosome, whose structure has been solved by cryo-EM at atomic resolution and in situ cryo-ET in the native cellular context; beyond its membership in this complex, no specific mechanistic function has been attributed to S2 individually in the available literature.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1026800 (S2) is a component of the 40S small subunit of the P. falciparum 80S cytoplasmic ribosome, resolved as one of many small-subunit proteins in high-resolution cryo-EM structures of the intact ribosome [#0, #1]. These structures were determined in complex with translation-inhibiting antimalarials—emetine bound at the small-subunit E-site to block mRNA/tRNA translocation [#0] and (+)-mefloquine bound at the GTPase-associated centre [#1]—and the native ribosome containing S2 has been captured in actively translating elongation states by in situ cryo-electron tomography inside infected erythrocytes [#2]. Proteomic co-melting profiling confirms S2 as a constitutive member of the ribosome complex across the intraerythrocytic developmental cycle [#4]. Beyond its membership in the 40S subunit within the translating ribosome, no mechanistic function has been attributed to S2 individually in the available corpus; all findings characterize the ribosome as a whole rather than S2 in isolation.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Establishing whether S2 could be placed structurally required an atomic model of the P. falciparum ribosome; the first cryo-EM structure resolved the 80S ribosome including the 40S subunit that contains S2, and localized emetine at the small-subunit E-site where it blocks translocation.\",\n      \"evidence\": \"Cryo-EM structure determination of the 80S ribosome at 3.2 Å in complex with emetine\",\n      \"pmids\": [\"24913268\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"S2 is visualized only as one of many small-subunit proteins; no S2-specific function or interaction is tested\", \"does not establish any role for S2 distinct from the assembled subunit\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"To define a second antimalarial's ribosomal target, the 80S structure containing S2 was solved with (+)-mefloquine bound to the GTPase-associated centre, confirming inhibition of protein synthesis at the ribosome.\",\n      \"evidence\": \"Cryo-EM at 3.2 Å with mutagenesis of the binding residues\",\n      \"pmids\": [\"28288098\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"The drug binding site is not on or attributed to S2\", \"S2 remains uncharacterized as an individual protein\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"The question of whether ribosome composition is uniform across the parasite life cycle was addressed by profiling 40S subunit heterogeneity, raising the possibility of stage-specific ribosome variants that include the S2-containing small subunit.\",\n      \"evidence\": \"Ribosome fractionation and structural/proteomic analysis across life-cycle stages\",\n      \"pmids\": [\"37053161\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Methods are not described in detail in the abstract\", \"S2 is inferred as a small-subunit member but not individually shown to vary\", \"no functional consequence of any compositional change is demonstrated\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"To move from purified structures to the native context, in situ cryo-ET resolved the S2-containing ribosome in multiple actively translating states inside infected erythrocytes, capturing elongation-cycle intermediates and drug-induced changes in ribosome localization.\",\n      \"evidence\": \"In situ cryo-electron tomography in P. falciparum-infected erythrocytes yielding eight ribosome structures\",\n      \"pmids\": [\"40825879\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"S2 is one of many resolved proteins with no individual functional assignment\", \"no perturbation of S2 specifically is performed\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether S2 is a stable versus dynamic ribosome component was probed by complexome-wide thermal proteome profiling, which detected S2 co-melting with the ribosome across the intraerythrocytic cycle, consistent with constitutive 40S membership.\",\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\": [\"Membership is inferred from co-melting, not from a direct functional assay on S2\", \"no S2-specific interaction, modification, or activity is measured\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"No experiment in the available corpus has assigned any function, interaction, or phenotype to S2/PF3D7_1026800 as an individual protein distinct from its structural membership in the 40S subunit; whether S2 has any specialized role remains unaddressed.\",\n      \"evidence\": \"Gap across the timeline\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No S2-specific knockdown, knockout, or complementation\", \"no S2-specific binding partner or post-translational regulation identified\", \"no evidence that S2 contributes to any stage-specific ribosome specialization\"],\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, 4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0022627\", \"supporting_discovery_ids\": [0, 1, 3, 4]},\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006414\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"complexes\": [\n      \"40S small ribosomal subunit (P. falciparum)\",\n      \"80S cytoplasmic ribosome (P. falciparum)\"\n    ],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"S2/PF3D7_1026800 is characterized only as a constitutive structural component of the 40S small subunit within the translating 80S ribosome; the cited studies target the ribosome as a whole and its antimalarial-binding sites (emetine at the small-subunit E-site [#0]; mefloquine at the GTPase-associated centre [#1]), not S2 individually.\",\n      \"No individual function, binding partner, or loss-of-function phenotype for S2 is established in the available corpus.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1026800","name":null,"product":"40S ribosomal protein S2","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0510900","name":null,"product":"40S ribosomal protein S2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0611200","name":null,"product":"40S ribosomal protein S2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}