{"gene":"RPS11","run_date":"2026-06-10T07:46:27","timeline":{"discoveries":[{"year":2003,"finding":"RPS11 (bacterial S11) physically interacts with ribosomal protein S7 at the E site of the 30S subunit, connecting the head to the platform and forming the mRNA exit channel; disruption of this interaction by site-directed mutagenesis increases frameshifting, readthrough of nonsense codons, codon misreading, and enhanced mRNA binding to 30S subunits, demonstrating a functional role in translational fidelity and ribosome dynamics.","method":"Site-directed mutagenesis, in vivo translational fidelity assays (frameshifting, readthrough, misreading), toeprinting assays, filter-binding assays","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 / Moderate — multiple orthogonal methods (mutagenesis + in vivo fidelity assays + toeprinting + filter-binding) in a single focused study on this specific protein interaction","pmids":["12937172"],"is_preprint":false},{"year":1988,"finding":"RPS11 (eukaryotic S11) interacts with the 690-720 and 790 loop regions of 16S rRNA in a cooperative manner with proteins S6 and S18, as shown by chemical probing of rRNA reactivities upon protein assembly into the 30S subunit; these proteins interact with residues near P-site nucleotides in 16S rRNA.","method":"Chemical probing of 16S rRNA with chemical probes during ribosome assembly","journal":"Journal of molecular biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct RNA chemical probing with assembly-dependent controls, single lab but well-defined methodology","pmids":["2459389"],"is_preprint":false},{"year":1987,"finding":"E. coli ribosomal protein S11 is cross-linked to 16S rRNA within an oligonucleotide encompassing positions 693-697, placing it in the central domain of the 30S subunit platform.","method":"RNA-protein cross-linking with bis-(2-chloroethyl)-methylamine followed by partial nuclease digestion and RNA/protein analysis","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 2 / Strong — replicated by two independent cross-linking studies (PMID 2437528 and 2437527) using different chemical cross-linkers, both mapping S11 to the same 693-705 region of 16S rRNA","pmids":["2437528","2437527"],"is_preprint":false},{"year":1978,"finding":"E. coli ribosomal proteins S1, S11, and S21 are directly required for tRNA binding to the 30S ribosome; reconstitution experiments showed that unmodified S11 restores phe-tRNA binding activity to tetranitromethane-inactivated 30S ribosomes.","method":"Ribosome reconstitution with tetranitromethane-inactivated 30S subunits and individual purified proteins, phe-tRNA binding assay","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — reconstitution assay establishing direct functional role, but single lab, single method","pmids":["25421"],"is_preprint":false},{"year":1984,"finding":"Eukaryotic ribosomal protein S11 is cross-linked to mRNA within the 48S pre-initiation complex, identifying it as part of the mRNA-binding domain of the small ribosomal subunit during translation initiation.","method":"Chemical cross-linking with diepoxybutane of native 48S pre-initiation complexes formed with 125I-labeled globin mRNA, followed by isolation and identification of covalent mRNA-protein complexes","journal":"Nucleic acids research","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct biochemical cross-linking in a functional complex, single lab, single method","pmids":["6514574"],"is_preprint":false},{"year":1977,"finding":"E. coli ribosomal protein S11 has a unique N-terminal isopeptide bond between N-alpha-monomethylalanine and the epsilon-amino group of the N-terminal lysine residue, creating a branching point — a post-translational modification not previously observed in ribosomal proteins.","method":"Direct protein N-terminal sequence analysis and chemical characterization of the isopeptide bond","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — direct chemical characterization of PTM, single lab, single study","pmids":["337304"],"is_preprint":false},{"year":1999,"finding":"E. coli ribosomal protein S11 accumulates near-stoichiometric levels of isoaspartate (estimated 0.5 mol per mol S11) during logarithmic growth, representing a post-translational modification that may be functionally important; expression of rat PIMT in E. coli reduced isoaspartate levels in cellular proteins.","method":"Isoaspartate quantification in E. coli protein fractions, identification of isoaspartate-containing protein by mass analysis, plasmid-based expression of rat PIMT","journal":"Journal of bacteriology","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct biochemical identification of isoaspartate modification in S11 with quantification, single lab","pmids":["10217780"],"is_preprint":false},{"year":1997,"finding":"In E. coli 70S ribosomes, the D loop (nucleotide U20) of P-site bound tRNA(Phe) is directly cross-linked to ribosomal protein S11, mapping the D loop to the platform of the 30S subunit.","method":"Photoaffinity cross-linking with 4-thiouridine-substituted tRNA(Phe) at the ribosomal P site, irradiation at 300 nm, identification of cross-linked proteins","journal":"RNA (New York, N.Y.)","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — direct photoaffinity cross-linking establishing spatial contact between S11 and P-site tRNA, single lab, single method","pmids":["9292501"],"is_preprint":false},{"year":2020,"finding":"Loss of human RPS11 via CRISPR knockout confers resistance to topoisomerase II poisons (etoposide and doxorubicin) in glioma cells and impairs induction of the proapoptotic gene APAF1 following treatment, establishing RPS11 as a factor required for the DNA damage-induced apoptotic response to TOP2 poisons.","method":"Genome-scale CRISPR knockout screen with etoposide, validation by individual RPS11 knockout, measurement of APAF1 expression by immunoblot/qPCR, cell viability assays","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — CRISPR screen plus targeted validation with defined molecular readout (APAF1 induction), single lab but two orthogonal approaches","pmids":["32528131"],"is_preprint":false},{"year":2017,"finding":"Plant 30S ribosomal protein S11 (NbRPS11) physically interacts with the CMV 2b protein (LS2b); knockdown of NbRPS11 by TRV-based gene silencing reduced CMV viral RNA replication, decreased CMV infection levels, and reduced the RNA silencing suppressor activity of CMV 2b protein in Nicotiana benthamiana.","method":"Yeast two-hybrid, bimolecular fluorescence complementation (BiFC) by confocal microscopy, GST pull-down assay, TRV-based gene silencing knockdown, immunoblot analysis of viral RNA and protein levels","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal interaction methods (Y2H, BiFC, GST pull-down) plus functional knockdown with defined readouts, single lab","pmids":["28806733"],"is_preprint":false},{"year":2025,"finding":"Enterococcus faecalis ribosomal protein RPS11 induces trained immunity in innate immune cells through TLR4-TET2 signaling-mediated ribosomal biogenesis inhibition, resulting in enhanced MHC molecule expression on antigen-presenting cells; RPS11 conjugated to superparamagnetic iron oxide nanoparticles boosted influenza vaccine efficacy.","method":"Bioactivity-guided fractionation, Galleria mellonella larval phenotypic model, mechanistic pathway analysis (TLR4-TET2 signaling), MHC expression measurement, in vivo vaccine efficacy testing","journal":"International journal of biological macromolecules","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, mechanistic pathway identification by fractionation and signaling analysis, but abstract lacks detail on direct reconstitution or mutagenesis confirming TLR4-TET2 pathway","pmids":["40381785"],"is_preprint":false},{"year":2026,"finding":"RPS11 knockdown in human pulmonary microvascular endothelial cells (HPMECs) blocked the ability of hUCMSC-derived exosomes to suppress ferroptosis and restore mitochondrial function; mechanistically, hUCMSC-Exos upregulate RPS11 to promote mitochondria-encoded protein translation.","method":"Proteomic sequencing of mitochondria from treated HPMECs, RPS11 knockdown, assessment of ferroptosis markers and mitochondrial function, multi-omics analysis","journal":"Journal of nanobiotechnology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, knockdown with functional readout but mechanistic link to mitochondrial translation is inferred from proteomics without direct reconstitution","pmids":["42174606"],"is_preprint":false},{"year":1999,"finding":"Human RPS11 and RPL13A genes are tandemly located in the genome separated by only 4.6 kb, with four snoRNA genes (U32, U33, U34 in RPL13A introns; U35 in both RPL13A intron 6 and RPS11 intron 3) encoded within their introns, a conserved organization also found in mouse.","method":"Genomic sequencing and gene structure analysis of human and mouse RPS11/RPL13A loci","journal":"Gene","confidence":"Low","confidence_rationale":"Tier 3 / Weak — genomic structural characterization without direct functional experiment on RPS11 protein mechanism","pmids":["10580157"],"is_preprint":false}],"current_model":"RPS11 is a conserved 40S small ribosomal subunit protein that binds to the platform region of the ribosome (contacting 16S/18S rRNA at positions 693-705), directly participates in mRNA and tRNA binding at the ribosomal P site, and functionally interacts with ribosomal protein S7 to maintain the mRNA exit channel and translational fidelity (suppressing frameshifting, readthrough, and misreading); in human cells, RPS11 is additionally required for the proapoptotic response to topoisomerase II poisons through APAF1 induction, and has been implicated in mitochondrial protein translation and ferroptosis suppression, while carrying unusual post-translational modifications (N-terminal isopeptide bond and isoaspartate) whose functional significance remains incompletely understood."},"narrative":{"mechanistic_narrative":"RPS11 is a conserved small ribosomal subunit protein that localizes to the platform/central domain of the small subunit, where it directly contacts rRNA, mRNA, and tRNA to support translation [PMID:12937172, PMID:2459389, PMID:2437528, PMID:2437527]. Cross-linking and chemical-probing studies place RPS11 in contact with the 693-705 and 690-720/790 loop regions of small-subunit rRNA near P-site nucleotides, assembling cooperatively with neighboring proteins S6 and S18 [PMID:2459389, PMID:2437528, PMID:2437527], and reconstitution assays establish it as directly required for tRNA binding to the small subunit [PMID:25421], with photoaffinity mapping confirming contact between the D loop of P-site tRNA and RPS11 [PMID:9292501]. RPS11 also participates directly in mRNA binding, being cross-linked to mRNA within the 48S pre-initiation complex [PMID:6514574], and its physical interaction with protein S7 forms the mRNA exit channel; disrupting this interaction increases frameshifting, nonsense readthrough, and codon misreading, defining a role in translational fidelity and ribosome dynamics [PMID:12937172]. RPS11 carries unusual post-translational modifications including an N-terminal isopeptide bond and near-stoichiometric isoaspartate [PMID:337304, PMID:10217780]. Beyond the ribosome, human RPS11 is required for the proapoptotic response to topoisomerase II poisons, with its loss conferring resistance to etoposide and doxorubicin and impairing induction of APAF1 [PMID:32528131].","teleology":[{"year":1977,"claim":"Initial characterization revealed that RPS11 carries an unusual covalent modification, raising the question of what post-translational chemistry distinguishes this ribosomal protein.","evidence":"N-terminal protein sequencing and chemical characterization of an isopeptide bond in E. coli S11","pmids":["337304"],"confidence":"Medium","gaps":["Functional consequence of the N-terminal isopeptide bond is unresolved","Conservation of the modification in eukaryotic RPS11 not established"]},{"year":1978,"claim":"Reconstitution experiments addressed whether RPS11 is functionally required for ribosome activity, showing it is directly needed for tRNA binding to the small subunit.","evidence":"Reconstitution of tetranitromethane-inactivated 30S subunits with purified S11 and phe-tRNA binding assay","pmids":["25421"],"confidence":"Medium","gaps":["Single method/single lab","Does not localize the binding contact at nucleotide resolution"]},{"year":1984,"claim":"Cross-linking in the initiation complex established that RPS11 contacts mRNA, placing it within the mRNA-binding domain of the small subunit during translation initiation.","evidence":"Diepoxybutane cross-linking of native 48S pre-initiation complexes formed with labeled globin mRNA","pmids":["6514574"],"confidence":"Medium","gaps":["Does not define mRNA channel residues","Single cross-linking method"]},{"year":1987,"claim":"RNA-protein cross-linking localized RPS11 to a specific rRNA region, anchoring it to the central platform domain of the small subunit.","evidence":"Chemical cross-linking to 16S rRNA positions 693-697, replicated across two independent cross-linkers","pmids":["2437528","2437527"],"confidence":"Medium","gaps":["Static contact map only","Does not address dynamics during translation"]},{"year":1988,"claim":"Assembly-dependent rRNA probing showed RPS11 binds rRNA cooperatively with S6 and S18 near P-site nucleotides, integrating it into the platform assembly pathway.","evidence":"Chemical probing of 16S rRNA reactivities during 30S subunit assembly","pmids":["2459389"],"confidence":"Medium","gaps":["Cooperativity inferred from probing, not structural data","Order of assembly events not fully resolved"]},{"year":1997,"claim":"Photoaffinity cross-linking resolved a direct spatial contact between P-site tRNA and RPS11, linking its platform position to tRNA accommodation.","evidence":"4-thiouridine photoaffinity cross-linking of P-site tRNA(Phe) D loop to S11 in 70S ribosomes","pmids":["9292501"],"confidence":"Medium","gaps":["Snapshot of one functional state","Does not quantify contribution to tRNA selection"]},{"year":1999,"claim":"Quantification of isoaspartate identified a second abundant modification of RPS11, extending the question of how modification chemistry affects this protein.","evidence":"Isoaspartate quantification and PIMT expression in E. coli protein fractions","pmids":["10217780"],"confidence":"Medium","gaps":["Functional significance of isoaspartate unknown","Whether modification is regulated or stochastic damage unclear"]},{"year":2003,"claim":"Mutagenesis of the RPS11-S7 interface tied a specific physical contact to translational accuracy, defining RPS11's role in suppressing frameshifting, readthrough, and misreading via the mRNA exit channel.","evidence":"Site-directed mutagenesis with in vivo fidelity assays, toeprinting, and filter-binding","pmids":["12937172"],"confidence":"High","gaps":["Structural basis of how the contact constrains the mRNA path not resolved","Eukaryotic conservation of the fidelity role not directly tested"]},{"year":2017,"claim":"A plant study extended RPS11 beyond core translation, showing it physically binds a viral suppressor protein and supports viral replication, implying extra-ribosomal interactions.","evidence":"Y2H, BiFC, GST pull-down and TRV gene silencing of NbRPS11 with CMV 2b in Nicotiana benthamiana","pmids":["28806733"],"confidence":"Medium","gaps":["Mechanism of how RPS11 supports 2b silencing-suppressor activity unclear","Relevance to human RPS11 not established"]},{"year":2020,"claim":"A CRISPR screen revealed an unexpected requirement for human RPS11 in DNA-damage-induced apoptosis, linking it to APAF1 induction after topoisomerase II poisoning.","evidence":"Genome-scale CRISPR knockout screen with etoposide plus validation knockout and APAF1 readout in glioma cells","pmids":["32528131"],"confidence":"Medium","gaps":["Whether the effect is via canonical translation or an extra-ribosomal function unresolved","Molecular mechanism connecting RPS11 to APAF1 transcription unknown"]},{"year":2025,"claim":"A bacterial RPS11 was reported to induce trained immunity via TLR4-TET2 signaling, raising the possibility of immunomodulatory activity distinct from translation.","evidence":"Bioactivity-guided fractionation, Galleria model, pathway analysis, and vaccine adjuvant testing","pmids":["40381785"],"confidence":"Low","gaps":["No reconstitution or mutagenesis confirming the TLR4-TET2 pathway","Single lab, abstract-level mechanism only"]},{"year":2026,"claim":"RPS11 was implicated in mitochondrial protein translation and ferroptosis suppression downstream of MSC exosomes, but the mechanism is inferred rather than directly demonstrated.","evidence":"Mitochondrial proteomics and RPS11 knockdown with ferroptosis/mitochondrial readouts in HPMECs","pmids":["42174606"],"confidence":"Low","gaps":["Link to mitochondrial translation inferred from proteomics without reconstitution","Direct role of cytoplasmic RPS11 in mitochondrial translation not established"]},{"year":null,"claim":"It remains unresolved whether the human extra-ribosomal roles of RPS11 (APAF1-dependent apoptosis, mitochondrial translation, ferroptosis) reflect a moonlighting function or secondary consequences of altered ribosome biogenesis, and the functional purpose of its conserved post-translational modifications is unknown.","evidence":"","pmids":[],"confidence":"Low","gaps":["No mechanism connecting ribosomal RPS11 to APAF1 transcription","Functional role of N-terminal isopeptide and isoaspartate modifications undefined","No human structural model of the RPS11-S7 exit channel in the timeline"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[1,2,4]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0,3]}],"localization":[{"term_id":"GO:0005840","term_label":"ribosome","supporting_discovery_ids":[0,1,2,3]}],"pathway":[],"complexes":["40S small ribosomal subunit"],"partners":["RPS7","RPS6","RPS18"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P62280","full_name":"Small ribosomal subunit protein uS17","aliases":["40S ribosomal protein S11"],"length_aa":158,"mass_kda":18.4,"function":"Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)","subcellular_location":"Cytoplasm; Nucleus, nucleolus","url":"https://www.uniprot.org/uniprotkb/P62280/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/RPS11","classification":"Common Essential","n_dependent_lines":1208,"n_total_lines":1208,"dependency_fraction":1.0},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000142534","cell_line_id":"CID000867","localizations":[{"compartment":"cytoplasmic","grade":3},{"compartment":"nucleolus_gc","grade":1}],"interactors":[{"gene":"CTCF","stoichiometry":10.0},{"gene":"EIF2S3","stoichiometry":10.0},{"gene":"EIF3B","stoichiometry":10.0},{"gene":"ENY2","stoichiometry":10.0},{"gene":"RBM8A","stoichiometry":10.0},{"gene":"RPL11","stoichiometry":10.0},{"gene":"RPL19","stoichiometry":10.0},{"gene":"RPL4","stoichiometry":10.0},{"gene":"RPL5","stoichiometry":10.0},{"gene":"NCL","stoichiometry":10.0}],"url":"https://opencell.sf.czbiohub.org/target/CID000867","total_profiled":1310},"omim":[{"mim_id":"619225","title":"RIBOSOMAL PROTEIN L13A; RPL13A","url":"https://www.omim.org/entry/619225"},{"mim_id":"180471","title":"RIBOSOMAL PROTEIN S11; RPS11","url":"https://www.omim.org/entry/180471"},{"mim_id":"180466","title":"RIBOSOMAL PROTEIN L19; RPL19","url":"https://www.omim.org/entry/180466"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Cytosol","reliability":"Approved"},{"location":"Nucleoli","reliability":"Additional"},{"location":"Endoplasmic reticulum","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/RPS11"},"hgnc":{"alias_symbol":["S11","uS17"],"prev_symbol":[]},"alphafold":{"accession":"P62280","domains":[{"cath_id":"2.40.50.1000","chopping":"32-145","consensus_level":"high","plddt":93.7718,"start":32,"end":145}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P62280","model_url":"https://alphafold.ebi.ac.uk/files/AF-P62280-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P62280-F1-predicted_aligned_error_v6.png","plddt_mean":88.06},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=RPS11","jax_strain_url":"https://www.jax.org/strain/search?query=RPS11"},"sequence":{"accession":"P62280","fasta_url":"https://rest.uniprot.org/uniprotkb/P62280.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P62280/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P62280"}},"corpus_meta":[{"pmid":"3003688","id":"PMC_3003688","title":"Spinach plastid genes coding for initiation factor IF-1, ribosomal protein S11 and RNA polymerase alpha-subunit.","date":"1986","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/3003688","citation_count":96,"is_preprint":false},{"pmid":"2459389","id":"PMC_2459389","title":"Interaction of ribosomal proteins S5, S6, S11, S12, S18 and S21 with 16 S rRNA.","date":"1988","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/2459389","citation_count":94,"is_preprint":false},{"pmid":"925037","id":"PMC_925037","title":"Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 40 S ribosomal subunit proteins Sa, Sc, S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18, S19, S20, S21, S26, S27', and S29.","date":"1977","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/925037","citation_count":60,"is_preprint":false},{"pmid":"6514574","id":"PMC_6514574","title":"Cross-linking of mRNA to initiation factor eIF-3, 24 kDa cap binding protein and ribosomal proteins S1, S3/3a, S6 and S11 within the 48S pre-initiation complex.","date":"1984","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/6514574","citation_count":58,"is_preprint":false},{"pmid":"2437528","id":"PMC_2437528","title":"RNA-protein cross-linking in Escherichia coli 30S ribosomal subunits; determination of sites on 16S RNA that are cross-linked to proteins S3, S4, S7, S9, S10, S11, S17, S18 and S21 by treatment with bis-(2-chloroethyl)-methylamine.","date":"1987","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/2437528","citation_count":54,"is_preprint":false},{"pmid":"2496109","id":"PMC_2496109","title":"Gene encoding the alpha core subunit of Bacillus subtilis RNA polymerase is cotranscribed with the genes for initiation factor 1 and ribosomal proteins B, S13, S11, and L17.","date":"1989","source":"Journal of bacteriology","url":"https://pubmed.ncbi.nlm.nih.gov/2496109","citation_count":54,"is_preprint":false},{"pmid":"2437527","id":"PMC_2437527","title":"RNA-protein cross-linking in Escherichia coli 30S ribosomal subunits; determination of sites on 16S RNA that are cross-linked to proteins S3, S4, S5, S7, S8, S9, S11, S13, S19 and S21 by treatment with methyl p-azidophenyl acetimidate.","date":"1987","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/2437527","citation_count":53,"is_preprint":false},{"pmid":"1697501","id":"PMC_1697501","title":"Noncoordinated expression of S6, S11, and S14 ribosomal protein genes in leukemic blast cells.","date":"1990","source":"Cancer research","url":"https://pubmed.ncbi.nlm.nih.gov/1697501","citation_count":51,"is_preprint":false},{"pmid":"8155878","id":"PMC_8155878","title":"The S11 and S13 self incompatibility alleles in Solanum chacoense Bitt. are remarkably similar.","date":"1994","source":"Plant molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/8155878","citation_count":45,"is_preprint":false},{"pmid":"8760884","id":"PMC_8760884","title":"Molecular cloning of a RNA binding protein, S1-1.","date":"1996","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/8760884","citation_count":38,"is_preprint":false},{"pmid":"12937172","id":"PMC_12937172","title":"A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome.","date":"2003","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/12937172","citation_count":38,"is_preprint":false},{"pmid":"3838984","id":"PMC_3838984","title":"Nucleotide sequence of cloned cDNA specific for rat ribosomal protein S11.","date":"1985","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/3838984","citation_count":37,"is_preprint":false},{"pmid":"26660465","id":"PMC_26660465","title":"Identification and molecular mapping of Rps11, a novel gene conferring resistance to Phytophthora sojae in soybean.","date":"2015","source":"TAG. 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IB5).","date":"1993","source":"Medical microbiology and immunology","url":"https://pubmed.ncbi.nlm.nih.gov/8232067","citation_count":6,"is_preprint":false},{"pmid":"17027259","id":"PMC_17027259","title":"Improvement of carbonyl reductase production of Geotrichum candidum for the transformation of 1-acetonaphthone to S(-)-1-(1'-napthyl) ethanol.","date":"2006","source":"Bioresource technology","url":"https://pubmed.ncbi.nlm.nih.gov/17027259","citation_count":5,"is_preprint":false},{"pmid":"36444477","id":"PMC_36444477","title":"Phosphorylation of S11 in PHR1 negatively controls its transcriptional activity.","date":"2022","source":"Physiologia plantarum","url":"https://pubmed.ncbi.nlm.nih.gov/36444477","citation_count":4,"is_preprint":false},{"pmid":"2505863","id":"PMC_2505863","title":"Crosslinking of ribosomal proteins S4, S5, S7, S8, S11, S12 and S18 to domains 1 and 2 of 16S rRNA in the Escherichia coli 30S 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diseases","url":"https://pubmed.ncbi.nlm.nih.gov/29619429","citation_count":1,"is_preprint":false},{"pmid":"8093055","id":"PMC_8093055","title":"Xenopus laevis ribosomal protein S11: cloning and sequencing of the cDNA and primary structure of the protein.","date":"1994","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/8093055","citation_count":0,"is_preprint":false},{"pmid":"42093637","id":"PMC_42093637","title":"E. coli-generated dsRNA targeting ribosomal protein L10, S11, and arginine kinase via oral administration impairs larval development in Tuta absoluta.","date":"2026","source":"Bulletin of entomological research","url":"https://pubmed.ncbi.nlm.nih.gov/42093637","citation_count":0,"is_preprint":false},{"pmid":"42174606","id":"PMC_42174606","title":"hUCMSC-exosomes attenuate acute lung injury by inhibiting ferroptosis in pulmonary microvascular endothelial cells through ribosomal protein RPS11 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\"finding\": \"RPS11 (bacterial S11) physically interacts with ribosomal protein S7 at the E site of the 30S subunit, connecting the head to the platform and forming the mRNA exit channel; disruption of this interaction by site-directed mutagenesis increases frameshifting, readthrough of nonsense codons, codon misreading, and enhanced mRNA binding to 30S subunits, demonstrating a functional role in translational fidelity and ribosome dynamics.\",\n      \"method\": \"Site-directed mutagenesis, in vivo translational fidelity assays (frameshifting, readthrough, misreading), toeprinting assays, filter-binding assays\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — multiple orthogonal methods (mutagenesis + in vivo fidelity assays + toeprinting + filter-binding) in a single focused study on this specific protein interaction\",\n      \"pmids\": [\"12937172\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1988,\n      \"finding\": \"RPS11 (eukaryotic S11) interacts with the 690-720 and 790 loop regions of 16S rRNA in a cooperative manner with proteins S6 and S18, as shown by chemical probing of rRNA reactivities upon protein assembly into the 30S subunit; these proteins interact with residues near P-site nucleotides in 16S rRNA.\",\n      \"method\": \"Chemical probing of 16S rRNA with chemical probes during ribosome assembly\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct RNA chemical probing with assembly-dependent controls, single lab but well-defined methodology\",\n      \"pmids\": [\"2459389\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1987,\n      \"finding\": \"E. coli ribosomal protein S11 is cross-linked to 16S rRNA within an oligonucleotide encompassing positions 693-697, placing it in the central domain of the 30S subunit platform.\",\n      \"method\": \"RNA-protein cross-linking with bis-(2-chloroethyl)-methylamine followed by partial nuclease digestion and RNA/protein analysis\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Strong — replicated by two independent cross-linking studies (PMID 2437528 and 2437527) using different chemical cross-linkers, both mapping S11 to the same 693-705 region of 16S rRNA\",\n      \"pmids\": [\"2437528\", \"2437527\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1978,\n      \"finding\": \"E. coli ribosomal proteins S1, S11, and S21 are directly required for tRNA binding to the 30S ribosome; reconstitution experiments showed that unmodified S11 restores phe-tRNA binding activity to tetranitromethane-inactivated 30S ribosomes.\",\n      \"method\": \"Ribosome reconstitution with tetranitromethane-inactivated 30S subunits and individual purified proteins, phe-tRNA binding assay\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — reconstitution assay establishing direct functional role, but single lab, single method\",\n      \"pmids\": [\"25421\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1984,\n      \"finding\": \"Eukaryotic ribosomal protein S11 is cross-linked to mRNA within the 48S pre-initiation complex, identifying it as part of the mRNA-binding domain of the small ribosomal subunit during translation initiation.\",\n      \"method\": \"Chemical cross-linking with diepoxybutane of native 48S pre-initiation complexes formed with 125I-labeled globin mRNA, followed by isolation and identification of covalent mRNA-protein complexes\",\n      \"journal\": \"Nucleic acids research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct biochemical cross-linking in a functional complex, single lab, single method\",\n      \"pmids\": [\"6514574\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1977,\n      \"finding\": \"E. coli ribosomal protein S11 has a unique N-terminal isopeptide bond between N-alpha-monomethylalanine and the epsilon-amino group of the N-terminal lysine residue, creating a branching point — a post-translational modification not previously observed in ribosomal proteins.\",\n      \"method\": \"Direct protein N-terminal sequence analysis and chemical characterization of the isopeptide bond\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — direct chemical characterization of PTM, single lab, single study\",\n      \"pmids\": [\"337304\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1999,\n      \"finding\": \"E. coli ribosomal protein S11 accumulates near-stoichiometric levels of isoaspartate (estimated 0.5 mol per mol S11) during logarithmic growth, representing a post-translational modification that may be functionally important; expression of rat PIMT in E. coli reduced isoaspartate levels in cellular proteins.\",\n      \"method\": \"Isoaspartate quantification in E. coli protein fractions, identification of isoaspartate-containing protein by mass analysis, plasmid-based expression of rat PIMT\",\n      \"journal\": \"Journal of bacteriology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct biochemical identification of isoaspartate modification in S11 with quantification, single lab\",\n      \"pmids\": [\"10217780\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1997,\n      \"finding\": \"In E. coli 70S ribosomes, the D loop (nucleotide U20) of P-site bound tRNA(Phe) is directly cross-linked to ribosomal protein S11, mapping the D loop to the platform of the 30S subunit.\",\n      \"method\": \"Photoaffinity cross-linking with 4-thiouridine-substituted tRNA(Phe) at the ribosomal P site, irradiation at 300 nm, identification of cross-linked proteins\",\n      \"journal\": \"RNA (New York, N.Y.)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — direct photoaffinity cross-linking establishing spatial contact between S11 and P-site tRNA, single lab, single method\",\n      \"pmids\": [\"9292501\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Loss of human RPS11 via CRISPR knockout confers resistance to topoisomerase II poisons (etoposide and doxorubicin) in glioma cells and impairs induction of the proapoptotic gene APAF1 following treatment, establishing RPS11 as a factor required for the DNA damage-induced apoptotic response to TOP2 poisons.\",\n      \"method\": \"Genome-scale CRISPR knockout screen with etoposide, validation by individual RPS11 knockout, measurement of APAF1 expression by immunoblot/qPCR, cell viability assays\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CRISPR screen plus targeted validation with defined molecular readout (APAF1 induction), single lab but two orthogonal approaches\",\n      \"pmids\": [\"32528131\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Plant 30S ribosomal protein S11 (NbRPS11) physically interacts with the CMV 2b protein (LS2b); knockdown of NbRPS11 by TRV-based gene silencing reduced CMV viral RNA replication, decreased CMV infection levels, and reduced the RNA silencing suppressor activity of CMV 2b protein in Nicotiana benthamiana.\",\n      \"method\": \"Yeast two-hybrid, bimolecular fluorescence complementation (BiFC) by confocal microscopy, GST pull-down assay, TRV-based gene silencing knockdown, immunoblot analysis of viral RNA and protein levels\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal interaction methods (Y2H, BiFC, GST pull-down) plus functional knockdown with defined readouts, single lab\",\n      \"pmids\": [\"28806733\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Enterococcus faecalis ribosomal protein RPS11 induces trained immunity in innate immune cells through TLR4-TET2 signaling-mediated ribosomal biogenesis inhibition, resulting in enhanced MHC molecule expression on antigen-presenting cells; RPS11 conjugated to superparamagnetic iron oxide nanoparticles boosted influenza vaccine efficacy.\",\n      \"method\": \"Bioactivity-guided fractionation, Galleria mellonella larval phenotypic model, mechanistic pathway analysis (TLR4-TET2 signaling), MHC expression measurement, in vivo vaccine efficacy testing\",\n      \"journal\": \"International journal of biological macromolecules\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, mechanistic pathway identification by fractionation and signaling analysis, but abstract lacks detail on direct reconstitution or mutagenesis confirming TLR4-TET2 pathway\",\n      \"pmids\": [\"40381785\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"RPS11 knockdown in human pulmonary microvascular endothelial cells (HPMECs) blocked the ability of hUCMSC-derived exosomes to suppress ferroptosis and restore mitochondrial function; mechanistically, hUCMSC-Exos upregulate RPS11 to promote mitochondria-encoded protein translation.\",\n      \"method\": \"Proteomic sequencing of mitochondria from treated HPMECs, RPS11 knockdown, assessment of ferroptosis markers and mitochondrial function, multi-omics analysis\",\n      \"journal\": \"Journal of nanobiotechnology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, knockdown with functional readout but mechanistic link to mitochondrial translation is inferred from proteomics without direct reconstitution\",\n      \"pmids\": [\"42174606\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1999,\n      \"finding\": \"Human RPS11 and RPL13A genes are tandemly located in the genome separated by only 4.6 kb, with four snoRNA genes (U32, U33, U34 in RPL13A introns; U35 in both RPL13A intron 6 and RPS11 intron 3) encoded within their introns, a conserved organization also found in mouse.\",\n      \"method\": \"Genomic sequencing and gene structure analysis of human and mouse RPS11/RPL13A loci\",\n      \"journal\": \"Gene\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — genomic structural characterization without direct functional experiment on RPS11 protein mechanism\",\n      \"pmids\": [\"10580157\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"RPS11 is a conserved 40S small ribosomal subunit protein that binds to the platform region of the ribosome (contacting 16S/18S rRNA at positions 693-705), directly participates in mRNA and tRNA binding at the ribosomal P site, and functionally interacts with ribosomal protein S7 to maintain the mRNA exit channel and translational fidelity (suppressing frameshifting, readthrough, and misreading); in human cells, RPS11 is additionally required for the proapoptotic response to topoisomerase II poisons through APAF1 induction, and has been implicated in mitochondrial protein translation and ferroptosis suppression, while carrying unusual post-translational modifications (N-terminal isopeptide bond and isoaspartate) whose functional significance remains incompletely understood.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"RPS11 is a conserved small ribosomal subunit protein that localizes to the platform/central domain of the small subunit, where it directly contacts rRNA, mRNA, and tRNA to support translation [#0, #1, #2]. Cross-linking and chemical-probing studies place RPS11 in contact with the 693-705 and 690-720/790 loop regions of small-subunit rRNA near P-site nucleotides, assembling cooperatively with neighboring proteins S6 and S18 [#1, #2], and reconstitution assays establish it as directly required for tRNA binding to the small subunit [#3], with photoaffinity mapping confirming contact between the D loop of P-site tRNA and RPS11 [#7]. RPS11 also participates directly in mRNA binding, being cross-linked to mRNA within the 48S pre-initiation complex [#4], and its physical interaction with protein S7 forms the mRNA exit channel; disrupting this interaction increases frameshifting, nonsense readthrough, and codon misreading, defining a role in translational fidelity and ribosome dynamics [#0]. RPS11 carries unusual post-translational modifications including an N-terminal isopeptide bond and near-stoichiometric isoaspartate [#5, #6]. Beyond the ribosome, human RPS11 is required for the proapoptotic response to topoisomerase II poisons, with its loss conferring resistance to etoposide and doxorubicin and impairing induction of APAF1 [#8].\",\n  \"teleology\": [\n    {\n      \"year\": 1977,\n      \"claim\": \"Initial characterization revealed that RPS11 carries an unusual covalent modification, raising the question of what post-translational chemistry distinguishes this ribosomal protein.\",\n      \"evidence\": \"N-terminal protein sequencing and chemical characterization of an isopeptide bond in E. coli S11\",\n      \"pmids\": [\"337304\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional consequence of the N-terminal isopeptide bond is unresolved\", \"Conservation of the modification in eukaryotic RPS11 not established\"]\n    },\n    {\n      \"year\": 1978,\n      \"claim\": \"Reconstitution experiments addressed whether RPS11 is functionally required for ribosome activity, showing it is directly needed for tRNA binding to the small subunit.\",\n      \"evidence\": \"Reconstitution of tetranitromethane-inactivated 30S subunits with purified S11 and phe-tRNA binding assay\",\n      \"pmids\": [\"25421\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single method/single lab\", \"Does not localize the binding contact at nucleotide resolution\"]\n    },\n    {\n      \"year\": 1984,\n      \"claim\": \"Cross-linking in the initiation complex established that RPS11 contacts mRNA, placing it within the mRNA-binding domain of the small subunit during translation initiation.\",\n      \"evidence\": \"Diepoxybutane cross-linking of native 48S pre-initiation complexes formed with labeled globin mRNA\",\n      \"pmids\": [\"6514574\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Does not define mRNA channel residues\", \"Single cross-linking method\"]\n    },\n    {\n      \"year\": 1987,\n      \"claim\": \"RNA-protein cross-linking localized RPS11 to a specific rRNA region, anchoring it to the central platform domain of the small subunit.\",\n      \"evidence\": \"Chemical cross-linking to 16S rRNA positions 693-697, replicated across two independent cross-linkers\",\n      \"pmids\": [\"2437528\", \"2437527\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Static contact map only\", \"Does not address dynamics during translation\"]\n    },\n    {\n      \"year\": 1988,\n      \"claim\": \"Assembly-dependent rRNA probing showed RPS11 binds rRNA cooperatively with S6 and S18 near P-site nucleotides, integrating it into the platform assembly pathway.\",\n      \"evidence\": \"Chemical probing of 16S rRNA reactivities during 30S subunit assembly\",\n      \"pmids\": [\"2459389\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Cooperativity inferred from probing, not structural data\", \"Order of assembly events not fully resolved\"]\n    },\n    {\n      \"year\": 1997,\n      \"claim\": \"Photoaffinity cross-linking resolved a direct spatial contact between P-site tRNA and RPS11, linking its platform position to tRNA accommodation.\",\n      \"evidence\": \"4-thiouridine photoaffinity cross-linking of P-site tRNA(Phe) D loop to S11 in 70S ribosomes\",\n      \"pmids\": [\"9292501\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Snapshot of one functional state\", \"Does not quantify contribution to tRNA selection\"]\n    },\n    {\n      \"year\": 1999,\n      \"claim\": \"Quantification of isoaspartate identified a second abundant modification of RPS11, extending the question of how modification chemistry affects this protein.\",\n      \"evidence\": \"Isoaspartate quantification and PIMT expression in E. coli protein fractions\",\n      \"pmids\": [\"10217780\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional significance of isoaspartate unknown\", \"Whether modification is regulated or stochastic damage unclear\"]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"Mutagenesis of the RPS11-S7 interface tied a specific physical contact to translational accuracy, defining RPS11's role in suppressing frameshifting, readthrough, and misreading via the mRNA exit channel.\",\n      \"evidence\": \"Site-directed mutagenesis with in vivo fidelity assays, toeprinting, and filter-binding\",\n      \"pmids\": [\"12937172\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of how the contact constrains the mRNA path not resolved\", \"Eukaryotic conservation of the fidelity role not directly tested\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"A plant study extended RPS11 beyond core translation, showing it physically binds a viral suppressor protein and supports viral replication, implying extra-ribosomal interactions.\",\n      \"evidence\": \"Y2H, BiFC, GST pull-down and TRV gene silencing of NbRPS11 with CMV 2b in Nicotiana benthamiana\",\n      \"pmids\": [\"28806733\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism of how RPS11 supports 2b silencing-suppressor activity unclear\", \"Relevance to human RPS11 not established\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"A CRISPR screen revealed an unexpected requirement for human RPS11 in DNA-damage-induced apoptosis, linking it to APAF1 induction after topoisomerase II poisoning.\",\n      \"evidence\": \"Genome-scale CRISPR knockout screen with etoposide plus validation knockout and APAF1 readout in glioma cells\",\n      \"pmids\": [\"32528131\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether the effect is via canonical translation or an extra-ribosomal function unresolved\", \"Molecular mechanism connecting RPS11 to APAF1 transcription unknown\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"A bacterial RPS11 was reported to induce trained immunity via TLR4-TET2 signaling, raising the possibility of immunomodulatory activity distinct from translation.\",\n      \"evidence\": \"Bioactivity-guided fractionation, Galleria model, pathway analysis, and vaccine adjuvant testing\",\n      \"pmids\": [\"40381785\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No reconstitution or mutagenesis confirming the TLR4-TET2 pathway\", \"Single lab, abstract-level mechanism only\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"RPS11 was implicated in mitochondrial protein translation and ferroptosis suppression downstream of MSC exosomes, but the mechanism is inferred rather than directly demonstrated.\",\n      \"evidence\": \"Mitochondrial proteomics and RPS11 knockdown with ferroptosis/mitochondrial readouts in HPMECs\",\n      \"pmids\": [\"42174606\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Link to mitochondrial translation inferred from proteomics without reconstitution\", \"Direct role of cytoplasmic RPS11 in mitochondrial translation not established\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unresolved whether the human extra-ribosomal roles of RPS11 (APAF1-dependent apoptosis, mitochondrial translation, ferroptosis) reflect a moonlighting function or secondary consequences of altered ribosome biogenesis, and the functional purpose of its conserved post-translational modifications is unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No mechanism connecting ribosomal RPS11 to APAF1 transcription\", \"Functional role of N-terminal isopeptide and isoaspartate modifications undefined\", \"No human structural model of the RPS11-S7 exit channel in the timeline\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [1, 2, 4]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005840\", \"supporting_discovery_ids\": [0, 1, 2, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-72766\", \"supporting_discovery_ids\": [0, 4]}\n    ],\n    \"complexes\": [\"40S small ribosomal subunit\"],\n    \"partners\": [\"RPS7\", \"RPS6\", \"RPS18\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}