{"gene":"PF3D7_1032800","run_date":"2026-09-08T12:51:28","timeline":{"discoveries":[{"year":2006,"finding":"LRR1 (PfLRR1) physically interacts with PfPP1 (protein phosphatase type 1) as shown by GST pull-down assay, and the LRR1–PfPP1 complex is detectable in parasite extracts; LRR1 inhibits PfPP1 phosphatase activity in vitro.","method":"GST pull-down assay; detection of complex in parasite extracts; in vitro phosphatase activity assay","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal pulldown plus in vitro activity assay in a single lab; single study but two orthogonal methods","pmids":["16629662"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2006,"finding":"In Xenopus oocyte functional assays, LRR1 (PfLRR1) interacted with endogenous Xenopus PP1 and promoted progression through the G2/M cell cycle checkpoint, inducing germinal vesicle breakdown (GVBD), phenocopying anti-PP1 antibody treatment or okadaic acid, indicating LRR1 regulates cell cycle by binding to and modulating PP1 activity.","method":"Xenopus oocyte microinjection/functional cell cycle assay; comparison with okadaic acid and anti-PP1 antibody controls","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional heterologous system with multiple controls, single lab","pmids":["16629662"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"PbLRR1 (P. berghei orthologue of LRR1) forms a complex with PbPP1 in both asexual and sexual stages of P. berghei and inhibits PbPP1 phosphatase activity; depletion of PbLRR1 adversely affects oocyst development in mosquitoes.","method":"Co-immunoprecipitation (complex detection in asexual and sexual stages); in vitro phosphatase activity assay; genetic depletion (knock-down/knock-out) with phenotypic readout (oocyst development)","journal":"Open biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal complex detection across life stages, in vitro enzymatic assay, and genetic loss-of-function with specific developmental phenotype, multiple orthogonal methods","pmids":["35920043"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2022,"finding":"Interactome and phospho-proteomics analysis of PbLRR1-depleted P. berghei parasites revealed that Inhibitor 3 (I3), a direct PP1 interactor, is drastically hypophosphorylated upon PbLRR1 depletion, and I3 was detected in the LRR1–PP1 complex, suggesting the LRR1–PP1 complex controls the phosphorylation status of I3 and thereby contributes to oocyst development.","method":"Interactome mass spectrometry; phospho-proteomics in PbLRR1-depleted parasites","journal":"Open biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — mass spectrometry-based interactome and phosphoproteomics in a single lab, mechanistically novel but not yet reconstituted in vitro","pmids":["35920043"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2007,"finding":"LRR1 (PfLRR1) is one of 14 LRR-containing proteins encoded in the P. falciparum genome; molecular cloning and cDNA sequencing confirmed it contains 4–10 LRR motifs, and real-time quantitative PCR showed its transcript is highly expressed in late intraerythrocytic stages (late trophozoites and schizonts).","method":"Genome analysis; molecular cloning and cDNA sequencing; real-time quantitative PCR","journal":"Molecular and biochemical parasitology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — transcriptional expression profiling and gene characterization without functional mechanistic follow-up for this specific gene","pmids":["17689674"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"LRR1 (PF3D7_1032800) is a leucine-rich repeat protein that physically interacts with and inhibits Protein Phosphatase type 1 (PP1) activity in Plasmodium falciparum and P. berghei; this LRR1–PP1 complex is present in both asexual and sexual parasite stages, modulates the phosphorylation state of PP1 regulator Inhibitor 3, promotes cell cycle progression through the G2/M checkpoint, and is required for efficient oocyst development in the mosquito."},"narrative":{"mechanistic_narrative":"LRR1 (PF3D7_1032800) is a leucine-rich repeat protein of Plasmodium that functions as a regulator of Protein Phosphatase type 1 (PP1), coupling phosphatase control to cell cycle progression and parasite development [PMID:16629662, PMID:35920043]. In P. falciparum, LRR1 physically binds PfPP1 and inhibits its phosphatase activity in vitro, and in a heterologous Xenopus oocyte system LRR1 engages endogenous PP1 to drive progression through the G2/M checkpoint, inducing germinal vesicle breakdown in a manner phenocopying PP1 inhibition [PMID:16629662]. In P. berghei, the orthologue forms a PP1 complex across both asexual and sexual stages and inhibits PP1 activity, and its depletion impairs oocyst development in the mosquito [PMID:35920043]. Within this complex, LRR1 controls the phosphorylation status of the PP1 regulator Inhibitor 3, which becomes drastically hypophosphorylated upon LRR1 depletion, linking LRR1–PP1 activity to transmission-stage development [PMID:35920043].","teleology":[{"year":2006,"claim":"It was unknown what regulated PfPP1 in the parasite; identifying LRR1 as a direct binding partner and inhibitor established a specific molecular mechanism for controlling phosphatase activity.","evidence":"GST pull-down, complex detection in parasite extracts, and in vitro phosphatase assay in P. falciparum","pmids":["16629662"],"confidence":"Medium","gaps":["Single lab, single study","Binding site and stoichiometry on PP1 not defined","In vivo consequence in the parasite not tested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2006,"claim":"Whether LRR1's PP1 inhibition had functional consequences for cell cycle control was untested; a Xenopus oocyte assay showed LRR1 drives G2/M progression, tying PP1 modulation to checkpoint control.","evidence":"Xenopus oocyte microinjection functional assay with okadaic acid and anti-PP1 antibody controls","pmids":["16629662"],"confidence":"Medium","gaps":["Heterologous system, not native parasite cell cycle","Direct demonstration in Plasmodium G2/M lacking","Downstream substrates unidentified"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2007,"claim":"The genomic context and expression timing of LRR1 were undefined; cloning and qPCR placed it among 14 parasite LRR proteins and showed peak transcription in late intraerythrocytic stages consistent with a cell-cycle role.","evidence":"Genome analysis, cDNA cloning/sequencing, and real-time qPCR in P. falciparum","pmids":["17689674"],"confidence":"Low","gaps":["Transcript-level only, no protein or functional follow-up","Number of LRR motifs given as a range (4–10)","Does not address mechanism"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"claim":"It was unknown whether the LRR1–PP1 interaction was conserved and physiologically required in vivo; genetic loss-of-function in P. berghei showed the complex forms across life stages and is needed for oocyst development.","evidence":"Co-immunoprecipitation across asexual and sexual stages, in vitro phosphatase assay, and genetic depletion with oocyst phenotype in P. berghei","pmids":["35920043"],"confidence":"High","gaps":["Mechanism linking PP1 inhibition to oocyst development not fully resolved","Asexual essentiality not clarified by the phenotype","Single lab"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2022,"claim":"The downstream targets of the LRR1–PP1 complex were unknown; interactome and phosphoproteomics identified Inhibitor 3 as a complex member whose phosphorylation depends on LRR1, connecting the complex to a defined regulatory node.","evidence":"Interactome mass spectrometry and phospho-proteomics in PbLRR1-depleted P. berghei","pmids":["35920043"],"confidence":"Medium","gaps":["Not reconstituted in vitro","Kinase acting on I3 not identified","Causal chain from I3 phosphorylation to phenotype not established"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"How LRR1 inhibition of PP1 is regulated during the parasite life cycle and which native substrates translate this into cell cycle and developmental outcomes remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the LRR1–PP1 interface","Native parasite substrates of the complex undefined","Regulation of LRR1 activity across stages unknown"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["LRR1–PP1 complex","LRR1–PP1–Inhibitor 3 complex"],"partners":["PFPP1 (PROTEIN PHOSPHATASE TYPE 1)","PBPP1","INHIBITOR 3 (I3)"],"other_free_text":["Contains leucine-rich repeat (LRR) motifs; one of 14 LRR proteins in P. falciparum [#4]","Transcript peaks in late intraerythrocytic stages (late trophozoites and schizonts) [#4]","Depletion of the P. berghei orthologue impairs mosquito-stage oocyst development [#2]","Complex present in both asexual and sexual stages of P. berghei [#2]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"16629662","id":"PMC_16629662","title":"Regulation of protein phosphatase type 1 and cell cycle progression by PfLRR1, a novel leucine-rich repeat protein of the human malaria parasite Plasmodium falciparum.","date":"2006","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/16629662","citation_count":34,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["leucine-rich repeat protein","PfLRR1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"22607144","id":"PMC_22607144","title":"Inhibition of protein-protein interactions in Plasmodium falciparum: future drug targets.","date":"2012","source":"Current pharmaceutical design","url":"https://pubmed.ncbi.nlm.nih.gov/22607144","citation_count":10,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfLRR1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"17689674","id":"PMC_17689674","title":"Census, molecular characterization and developmental expression of Leucine-Rich-Repeat proteins in Plasmodium falciparum.","date":"2007","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/17689674","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfLRR1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35920043","id":"PMC_35920043","title":"Plasmodium berghei leucine-rich repeat protein 1 downregulates protein phosphatase 1 activity and is required for efficient oocyst development.","date":"2022","source":"Open biology","url":"https://pubmed.ncbi.nlm.nih.gov/35920043","citation_count":5,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LRR1","PbLRR1","leucine-rich repeat protein","leucine-rich repeat protein 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4755,"output_tokens":1490,"usd":0.018308,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6441,"output_tokens":2433,"usd":0.046515,"stage2_stop_reason":"end_turn"},"total_usd":0.064823,"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\": 2006,\n      \"finding\": \"LRR1 (PfLRR1) physically interacts with PfPP1 (protein phosphatase type 1) as shown by GST pull-down assay, and the LRR1–PfPP1 complex is detectable in parasite extracts; LRR1 inhibits PfPP1 phosphatase activity in vitro.\",\n      \"method\": \"GST pull-down assay; detection of complex in parasite extracts; in vitro phosphatase activity assay\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal pulldown plus in vitro activity assay in a single lab; single study but two orthogonal methods\",\n      \"pmids\": [\"16629662\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"In Xenopus oocyte functional assays, LRR1 (PfLRR1) interacted with endogenous Xenopus PP1 and promoted progression through the G2/M cell cycle checkpoint, inducing germinal vesicle breakdown (GVBD), phenocopying anti-PP1 antibody treatment or okadaic acid, indicating LRR1 regulates cell cycle by binding to and modulating PP1 activity.\",\n      \"method\": \"Xenopus oocyte microinjection/functional cell cycle assay; comparison with okadaic acid and anti-PP1 antibody controls\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional heterologous system with multiple controls, single lab\",\n      \"pmids\": [\"16629662\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"PbLRR1 (P. berghei orthologue of LRR1) forms a complex with PbPP1 in both asexual and sexual stages of P. berghei and inhibits PbPP1 phosphatase activity; depletion of PbLRR1 adversely affects oocyst development in mosquitoes.\",\n      \"method\": \"Co-immunoprecipitation (complex detection in asexual and sexual stages); in vitro phosphatase activity assay; genetic depletion (knock-down/knock-out) with phenotypic readout (oocyst development)\",\n      \"journal\": \"Open biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal complex detection across life stages, in vitro enzymatic assay, and genetic loss-of-function with specific developmental phenotype, multiple orthogonal methods\",\n      \"pmids\": [\"35920043\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Interactome and phospho-proteomics analysis of PbLRR1-depleted P. berghei parasites revealed that Inhibitor 3 (I3), a direct PP1 interactor, is drastically hypophosphorylated upon PbLRR1 depletion, and I3 was detected in the LRR1–PP1 complex, suggesting the LRR1–PP1 complex controls the phosphorylation status of I3 and thereby contributes to oocyst development.\",\n      \"method\": \"Interactome mass spectrometry; phospho-proteomics in PbLRR1-depleted parasites\",\n      \"journal\": \"Open biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — mass spectrometry-based interactome and phosphoproteomics in a single lab, mechanistically novel but not yet reconstituted in vitro\",\n      \"pmids\": [\"35920043\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2007,\n      \"finding\": \"LRR1 (PfLRR1) is one of 14 LRR-containing proteins encoded in the P. falciparum genome; molecular cloning and cDNA sequencing confirmed it contains 4–10 LRR motifs, and real-time quantitative PCR showed its transcript is highly expressed in late intraerythrocytic stages (late trophozoites and schizonts).\",\n      \"method\": \"Genome analysis; molecular cloning and cDNA sequencing; real-time quantitative PCR\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — transcriptional expression profiling and gene characterization without functional mechanistic follow-up for this specific gene\",\n      \"pmids\": [\"17689674\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"LRR1 (PF3D7_1032800) is a leucine-rich repeat protein that physically interacts with and inhibits Protein Phosphatase type 1 (PP1) activity in Plasmodium falciparum and P. berghei; this LRR1–PP1 complex is present in both asexual and sexual parasite stages, modulates the phosphorylation state of PP1 regulator Inhibitor 3, promotes cell cycle progression through the G2/M checkpoint, and is required for efficient oocyst development in the mosquito.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"LRR1 (PF3D7_1032800) is a leucine-rich repeat protein of Plasmodium that functions as a regulator of Protein Phosphatase type 1 (PP1), coupling phosphatase control to cell cycle progression and parasite development [#0, #2]. In P. falciparum, LRR1 physically binds PfPP1 and inhibits its phosphatase activity in vitro, and in a heterologous Xenopus oocyte system LRR1 engages endogenous PP1 to drive progression through the G2/M checkpoint, inducing germinal vesicle breakdown in a manner phenocopying PP1 inhibition [#0, #1]. In P. berghei, the orthologue forms a PP1 complex across both asexual and sexual stages and inhibits PP1 activity, and its depletion impairs oocyst development in the mosquito [#2]. Within this complex, LRR1 controls the phosphorylation status of the PP1 regulator Inhibitor 3, which becomes drastically hypophosphorylated upon LRR1 depletion, linking LRR1\\u2013PP1 activity to transmission-stage development [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"It was unknown what regulated PfPP1 in the parasite; identifying LRR1 as a direct binding partner and inhibitor established a specific molecular mechanism for controlling phosphatase activity.\",\n      \"evidence\": \"GST pull-down, complex detection in parasite extracts, and in vitro phosphatase assay in P. falciparum\",\n      \"pmids\": [\"16629662\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab, single study\", \"Binding site and stoichiometry on PP1 not defined\", \"In vivo consequence in the parasite not tested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"Whether LRR1's PP1 inhibition had functional consequences for cell cycle control was untested; a Xenopus oocyte assay showed LRR1 drives G2/M progression, tying PP1 modulation to checkpoint control.\",\n      \"evidence\": \"Xenopus oocyte microinjection functional assay with okadaic acid and anti-PP1 antibody controls\",\n      \"pmids\": [\"16629662\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Heterologous system, not native parasite cell cycle\", \"Direct demonstration in Plasmodium G2/M lacking\", \"Downstream substrates unidentified\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2007,\n      \"claim\": \"The genomic context and expression timing of LRR1 were undefined; cloning and qPCR placed it among 14 parasite LRR proteins and showed peak transcription in late intraerythrocytic stages consistent with a cell-cycle role.\",\n      \"evidence\": \"Genome analysis, cDNA cloning/sequencing, and real-time qPCR in P. falciparum\",\n      \"pmids\": [\"17689674\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Transcript-level only, no protein or functional follow-up\", \"Number of LRR motifs given as a range (4\\u201310)\", \"Does not address mechanism\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"It was unknown whether the LRR1\\u2013PP1 interaction was conserved and physiologically required in vivo; genetic loss-of-function in P. berghei showed the complex forms across life stages and is needed for oocyst development.\",\n      \"evidence\": \"Co-immunoprecipitation across asexual and sexual stages, in vitro phosphatase assay, and genetic depletion with oocyst phenotype in P. berghei\",\n      \"pmids\": [\"35920043\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanism linking PP1 inhibition to oocyst development not fully resolved\", \"Asexual essentiality not clarified by the phenotype\", \"Single lab\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"The downstream targets of the LRR1\\u2013PP1 complex were unknown; interactome and phosphoproteomics identified Inhibitor 3 as a complex member whose phosphorylation depends on LRR1, connecting the complex to a defined regulatory node.\",\n      \"evidence\": \"Interactome mass spectrometry and phospho-proteomics in PbLRR1-depleted P. berghei\",\n      \"pmids\": [\"35920043\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Not reconstituted in vitro\", \"Kinase acting on I3 not identified\", \"Causal chain from I3 phosphorylation to phenotype not established\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How LRR1 inhibition of PP1 is regulated during the parasite life cycle and which native substrates translate this into cell cycle and developmental outcomes remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structural model of the LRR1\\u2013PP1 interface\", \"Native parasite substrates of the complex undefined\", \"Regulation of LRR1 activity across stages unknown\"],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008157\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0019888\", \"supporting_discovery_ids\": [0, 2, 3]},\n      {\"term_id\": \"GO:0004864\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0000086\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0035825\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"complexes\": [\"LRR1\\u2013PP1 complex\", \"LRR1\\u2013PP1\\u2013Inhibitor 3 complex\"],\n    \"partners\": [\"PfPP1 (protein phosphatase type 1)\", \"PbPP1\", \"Inhibitor 3 (I3)\"],\n    \"other_free_text\": [\n      \"Contains leucine-rich repeat (LRR) motifs; one of 14 LRR proteins in P. falciparum [#4]\",\n      \"Transcript peaks in late intraerythrocytic stages (late trophozoites and schizonts) [#4]\",\n      \"Depletion of the P. berghei orthologue impairs mosquito-stage oocyst development [#2]\",\n      \"Complex present in both asexual and sexual stages of P. berghei [#2]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1032800","name":null,"product":"leucine-rich repeat protein 1","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0516600","name":null,"product":"leucine-rich repeat protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0617600","name":null,"product":"leucine-rich repeat protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"LRR1","evaluation":null}