{"gene":"PF3D7_0919300","run_date":"2026-09-08T19:44:17","timeline":{"discoveries":[{"year":2023,"finding":"In situ cryo-electron tomography and subvolume averaging of P. falciparum sporozoites revealed that TrxL1 is a component of an interrupted luminal helix (ILH) within subpellicular microtubules (SPMTs) of mosquito-stage (ookinete and sporozoite) parasites, where it structurally reinforces the 13-protofilament microtubule architecture. TrxL1 was absent from the lumens of merozoite and gametocyte microtubules, demonstrating stage-specific assembly of the ILH.","method":"In situ cryo-electron tomography and subvolume averaging with pseudoatomic model fitting (PDB 7MIZ); comparative structural analysis of TrxL1 N-terminal helix between Plasmodium and T. gondii","journal":"Nature Communications","confidence":"High","confidence_rationale":"Tier 1 / Moderate — cryo-ET structural determination with subvolume averaging and model fitting in a single rigorous study; multiple orthogonal structural methods","pmids":["36869034"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"Single gene deletion of TrxL1 in a rodent malaria parasite showed that TrxL1, as a MIP associated with subpellicular microtubules, is dispensable for transmission from the vertebrate host to the mosquito and back, indicating functional redundancy among SPMT-associated MIPs at transmissive stages.","method":"Single gene deletion (knockout) followed by transmission assays in rodent malaria model","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — clean genetic knockout with defined transmission phenotype (negative result: dispensable), single lab, single method","pmids":["39908102"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2017,"finding":"TrxL1 was identified as a poor substrate for thioredoxin reductase in P. falciparum; however, it can be reduced by the glutathione system (glutaredoxin/GSH pathway), demonstrating cross-talk between the glutathione and thioredoxin antioxidant systems that can compensate for TrxL1's inaccessibility to thioredoxin reductase.","method":"In vitro biochemical reduction assay comparing thioredoxin reductase activity versus glutathione system activity on TrxL1","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro enzymatic assay, single lab, single method, no mutagenesis","pmids":["28479253"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"ChIP-seq analysis showed that the transcription factor PfAP2-EXP2 directly binds to the TrxL1 gene locus in P. falciparum, and conditional knockdown of PfAP2-EXP2 reduced TrxL1 expression, placing TrxL1 as a direct transcriptional target of PfAP2-EXP2 at the schizont stage.","method":"ChIP-seq (chromatin immunoprecipitation followed by sequencing) and conditional knockdown of PfAP2-EXP2 with transcriptome profiling (RNA-seq/RPKM quantification)","journal":"Frontiers in cell and developmental biology","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — ChIP-seq with transcriptome validation, two orthogonal methods, single lab","pmids":["35083215"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]}],"current_model":"TrxL1 (PF3D7_0919300) is a microtubule inner protein (MIP) that localizes to the lumen of subpellicular microtubules specifically in mosquito-stage P. falciparum (ookinetes and sporozoites), where cryo-ET structures show it forms part of an interrupted luminal helix that reinforces the 13-protofilament microtubule architecture; biochemically, TrxL1 is a poor substrate for thioredoxin reductase but can be reduced by the glutathione system; its transcription is directly activated by the ApiAP2 factor PfAP2-EXP2; and single-gene deletion in P. berghei demonstrates it is individually dispensable for parasite transmission, suggesting functional redundancy with other SPMT-associated MIPs."},"narrative":{"mechanistic_narrative":"TrxL1 (PF3D7_0919300) is a microtubule inner protein (MIP) that reinforces the subpellicular microtubule (SPMT) cytoskeleton of mosquito-stage Plasmodium parasites [PMID:36869034]. In situ cryo-electron tomography of P. falciparum sporozoites places TrxL1 within an interrupted luminal helix (ILH) inside the lumen of 13-protofilament SPMTs, where it structurally braces the microtubule wall; assembly of this ILH is stage-specific, with TrxL1 present in ookinete and sporozoite microtubules but absent from merozoite and gametocyte microtubule lumens [PMID:36869034]. Despite its annotation as a thioredoxin-like protein, TrxL1 is a poor substrate for thioredoxin reductase and is instead reduced by the glutathione/glutaredoxin system, indicating cross-talk between the two antioxidant systems on this protein [PMID:28479253]. Transcriptionally, TrxL1 is a direct target of the ApiAP2 factor PfAP2-EXP2, which binds its locus and is required for its expression at the schizont stage [PMID:35083215]. In the rodent parasite P. berghei, single-gene deletion of TrxL1 leaves transmission between vertebrate host and mosquito intact, implying functional redundancy among SPMT-associated MIPs at transmissive stages [PMID:39908102]. Beyond these findings, the functional consequence of TrxL1's thioredoxin-like fold and its redox activity within the microtubule lumen have not been characterized in the available corpus.","teleology":[{"year":2017,"claim":"It was unknown how the thioredoxin-like TrxL1 fits into the parasite's redox networks; the biochemical assay established that TrxL1 is poorly served by thioredoxin reductase but accessible to the glutathione system, revealing redundancy between antioxidant pathways acting on it.","evidence":"In vitro biochemical reduction assays comparing thioredoxin reductase versus glutathione-system activity on TrxL1 in P. falciparum","pmids":["28479253"],"confidence":"Medium","gaps":["No mutagenesis of catalytic residues to confirm a functional redox center","No demonstration of a physiological substrate or in vivo redox role","Does not connect the redox chemistry to any cellular function"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"claim":"The transcriptional control of TrxL1 was undefined; ChIP-seq plus conditional knockdown showed it is a direct target of PfAP2-EXP2, placing its expression under a defined ApiAP2 regulatory program at the schizont stage.","evidence":"ChIP-seq and conditional knockdown of PfAP2-EXP2 with transcriptome profiling in P. falciparum 3D7","pmids":["35083215"],"confidence":"Medium","gaps":["Does not identify the cis-element within the TrxL1 locus bound by PfAP2-EXP2","Does not establish whether this regulation drives the stage-specific luminal assembly of TrxL1","Single lab, two orthogonal methods only"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2023,"claim":"The cellular role of TrxL1 was unresolved; in situ cryo-ET localized it to the lumen of subpellicular microtubules as part of an interrupted luminal helix, redefining it as a stage-specific microtubule inner protein that reinforces 13-protofilament architecture.","evidence":"In situ cryo-electron tomography and subvolume averaging with pseudoatomic model fitting (PDB 7MIZ) in P. falciparum sporozoites","pmids":["36869034"],"confidence":"High","gaps":["Does not test whether TrxL1 loss alters microtubule stability or morphology","Mechanism directing stage-specific ILH assembly (present in ookinetes/sporozoites, absent in merozoites/gametocytes) is not established","Does not resolve whether the thioredoxin-like fold has a redox function within the lumen"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether TrxL1 is required for its microtubule-associated role was unknown; targeted deletion in P. berghei showed it is dispensable for full-cycle transmission, arguing that SPMT-associated MIPs function with redundancy at transmissive stages.","evidence":"Single-gene knockout followed by transmission assays in the P. berghei rodent malaria model","pmids":["39908102"],"confidence":"Medium","gaps":["Negative phenotype does not identify which MIPs provide the redundant function","Does not assay microtubule integrity or subtle fitness defects beyond transmission","Shown in P. berghei; not directly tested in P. falciparum"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"It remains unknown whether the thioredoxin-like fold of TrxL1 exerts any redox function inside the microtubule lumen, and which factors direct its stage-specific luminal assembly.","evidence":"","pmids":[],"confidence":"Low","gaps":["No link established between TrxL1 redox chemistry and its structural microtubule role","Partner MIPs and assembly determinants of the interrupted luminal helix are uncharacterized in this corpus","No structural or functional data for TrxL1 outside mosquito stages"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Interrupted luminal helix (ILH) within subpellicular microtubules of mosquito-stage parasites [#0]"],"partners":["PFAP2-EXP2 (TRANSCRIPTIONAL ACTIVATOR BINDING THE TRXL1 LOCUS) [#3]","GLUTATHIONE/GLUTAREDOXIN SYSTEM (REDUCES TRXL1) [#2]"],"other_free_text":["TrxL1 is a microtubule inner protein reinforcing 13-protofilament subpellicular microtubules, assembled stage-specifically in ookinetes and sporozoites but absent from merozoite and gametocyte microtubules [#0].","TrxL1 is a poor substrate for thioredoxin reductase but is reducible via the glutathione system [#2].","Deletion of TrxL1 in P. berghei is dispensable for transmission, indicating redundancy among SPMT-associated MIPs [#1]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"28479253","id":"PMC_28479253","title":"Glutathione and thioredoxin systems of the malaria parasite Plasmodium falciparum: Partners in crime?","date":"2017","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/28479253","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["thioredoxin-like protein 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"39908102","id":"PMC_39908102","title":"Microtubule inner proteins of Plasmodium are essential for transmission of malaria parasites.","date":"2025","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/39908102","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["TrxL1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"41626803","id":"","title":"Microtubule inner proteins in apicomplexan parasites.","date":"2026","source":"Biochemical Society transactions","url":"https://pubmed.ncbi.nlm.nih.gov/41626803","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["TrxL1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36869034","id":"","title":"Variable microtubule architecture in the malaria parasite.","date":"2023","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/36869034","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["TrxL1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"41117539","id":"","title":"Plasmodium berghei IMC1j interacts with δ-tubulin to orchestrate subpellicular microtubule organization in ookinetes.","date":"2025","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/41117539","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["TrxL1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35083215","id":"","title":"PfAP2-EXP2, an Essential Transcription Factor for the Intraerythrocytic Development of Plasmodium falciparum.","date":"2022","source":"Frontiers in cell and developmental biology","url":"https://pubmed.ncbi.nlm.nih.gov/35083215","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["TrxL1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36625655","id":"","title":"A Microtubule-Associated Protein Is Essential for Malaria Parasite Transmission.","date":"2023","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/36625655","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["TrxL1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33879496","id":"","title":"Dual RNA Sequencing Meta-analysis in Plasmodium Infection Identifies Host-Parasite Interactions.","date":"2021","source":"mSystems","url":"https://pubmed.ncbi.nlm.nih.gov/33879496","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["TrxL1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":10499,"output_tokens":1357,"usd":0.025926,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6219,"output_tokens":2767,"usd":0.050135,"stage2_stop_reason":"end_turn"},"total_usd":0.076061,"stage1_batch_id":"msgbatch_01SRp5hyRc82zNjddxyCCXGk","stage2_batch_id":"msgbatch_01K3BTmBazRo3pRrMvyaPMTY","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2023,\n      \"finding\": \"In situ cryo-electron tomography and subvolume averaging of P. falciparum sporozoites revealed that TrxL1 is a component of an interrupted luminal helix (ILH) within subpellicular microtubules (SPMTs) of mosquito-stage (ookinete and sporozoite) parasites, where it structurally reinforces the 13-protofilament microtubule architecture. TrxL1 was absent from the lumens of merozoite and gametocyte microtubules, demonstrating stage-specific assembly of the ILH.\",\n      \"method\": \"In situ cryo-electron tomography and subvolume averaging with pseudoatomic model fitting (PDB 7MIZ); comparative structural analysis of TrxL1 N-terminal helix between Plasmodium and T. gondii\",\n      \"journal\": \"Nature Communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — cryo-ET structural determination with subvolume averaging and model fitting in a single rigorous study; multiple orthogonal structural methods\",\n      \"pmids\": [\"36869034\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Single gene deletion of TrxL1 in a rodent malaria parasite showed that TrxL1, as a MIP associated with subpellicular microtubules, is dispensable for transmission from the vertebrate host to the mosquito and back, indicating functional redundancy among SPMT-associated MIPs at transmissive stages.\",\n      \"method\": \"Single gene deletion (knockout) followed by transmission assays in rodent malaria model\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean genetic knockout with defined transmission phenotype (negative result: dispensable), single lab, single method\",\n      \"pmids\": [\"39908102\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"TrxL1 was identified as a poor substrate for thioredoxin reductase in P. falciparum; however, it can be reduced by the glutathione system (glutaredoxin/GSH pathway), demonstrating cross-talk between the glutathione and thioredoxin antioxidant systems that can compensate for TrxL1's inaccessibility to thioredoxin reductase.\",\n      \"method\": \"In vitro biochemical reduction assay comparing thioredoxin reductase activity versus glutathione system activity on TrxL1\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro enzymatic assay, single lab, single method, no mutagenesis\",\n      \"pmids\": [\"28479253\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"ChIP-seq analysis showed that the transcription factor PfAP2-EXP2 directly binds to the TrxL1 gene locus in P. falciparum, and conditional knockdown of PfAP2-EXP2 reduced TrxL1 expression, placing TrxL1 as a direct transcriptional target of PfAP2-EXP2 at the schizont stage.\",\n      \"method\": \"ChIP-seq (chromatin immunoprecipitation followed by sequencing) and conditional knockdown of PfAP2-EXP2 with transcriptome profiling (RNA-seq/RPKM quantification)\",\n      \"journal\": \"Frontiers in cell and developmental biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — ChIP-seq with transcriptome validation, two orthogonal methods, single lab\",\n      \"pmids\": [\"35083215\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    }\n  ],\n  \"current_model\": \"TrxL1 (PF3D7_0919300) is a microtubule inner protein (MIP) that localizes to the lumen of subpellicular microtubules specifically in mosquito-stage P. falciparum (ookinetes and sporozoites), where cryo-ET structures show it forms part of an interrupted luminal helix that reinforces the 13-protofilament microtubule architecture; biochemically, TrxL1 is a poor substrate for thioredoxin reductase but can be reduced by the glutathione system; its transcription is directly activated by the ApiAP2 factor PfAP2-EXP2; and single-gene deletion in P. berghei demonstrates it is individually dispensable for parasite transmission, suggesting functional redundancy with other SPMT-associated MIPs.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TrxL1 (PF3D7_0919300) is a microtubule inner protein (MIP) that reinforces the subpellicular microtubule (SPMT) cytoskeleton of mosquito-stage Plasmodium parasites [#0]. In situ cryo-electron tomography of P. falciparum sporozoites places TrxL1 within an interrupted luminal helix (ILH) inside the lumen of 13-protofilament SPMTs, where it structurally braces the microtubule wall; assembly of this ILH is stage-specific, with TrxL1 present in ookinete and sporozoite microtubules but absent from merozoite and gametocyte microtubule lumens [#0]. Despite its annotation as a thioredoxin-like protein, TrxL1 is a poor substrate for thioredoxin reductase and is instead reduced by the glutathione/glutaredoxin system, indicating cross-talk between the two antioxidant systems on this protein [#2]. Transcriptionally, TrxL1 is a direct target of the ApiAP2 factor PfAP2-EXP2, which binds its locus and is required for its expression at the schizont stage [#3]. In the rodent parasite P. berghei, single-gene deletion of TrxL1 leaves transmission between vertebrate host and mosquito intact, implying functional redundancy among SPMT-associated MIPs at transmissive stages [#1]. Beyond these findings, the functional consequence of TrxL1's thioredoxin-like fold and its redox activity within the microtubule lumen have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2017,\n      \"claim\": \"It was unknown how the thioredoxin-like TrxL1 fits into the parasite's redox networks; the biochemical assay established that TrxL1 is poorly served by thioredoxin reductase but accessible to the glutathione system, revealing redundancy between antioxidant pathways acting on it.\",\n      \"evidence\": \"In vitro biochemical reduction assays comparing thioredoxin reductase versus glutathione-system activity on TrxL1 in P. falciparum\",\n      \"pmids\": [\"28479253\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"No mutagenesis of catalytic residues to confirm a functional redox center\",\n        \"No demonstration of a physiological substrate or in vivo redox role\",\n        \"Does not connect the redox chemistry to any cellular function\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"The transcriptional control of TrxL1 was undefined; ChIP-seq plus conditional knockdown showed it is a direct target of PfAP2-EXP2, placing its expression under a defined ApiAP2 regulatory program at the schizont stage.\",\n      \"evidence\": \"ChIP-seq and conditional knockdown of PfAP2-EXP2 with transcriptome profiling in P. falciparum 3D7\",\n      \"pmids\": [\"35083215\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Does not identify the cis-element within the TrxL1 locus bound by PfAP2-EXP2\",\n        \"Does not establish whether this regulation drives the stage-specific luminal assembly of TrxL1\",\n        \"Single lab, two orthogonal methods only\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"The cellular role of TrxL1 was unresolved; in situ cryo-ET localized it to the lumen of subpellicular microtubules as part of an interrupted luminal helix, redefining it as a stage-specific microtubule inner protein that reinforces 13-protofilament architecture.\",\n      \"evidence\": \"In situ cryo-electron tomography and subvolume averaging with pseudoatomic model fitting (PDB 7MIZ) in P. falciparum sporozoites\",\n      \"pmids\": [\"36869034\"],\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Does not test whether TrxL1 loss alters microtubule stability or morphology\",\n        \"Mechanism directing stage-specific ILH assembly (present in ookinetes/sporozoites, absent in merozoites/gametocytes) is not established\",\n        \"Does not resolve whether the thioredoxin-like fold has a redox function within the lumen\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether TrxL1 is required for its microtubule-associated role was unknown; targeted deletion in P. berghei showed it is dispensable for full-cycle transmission, arguing that SPMT-associated MIPs function with redundancy at transmissive stages.\",\n      \"evidence\": \"Single-gene knockout followed by transmission assays in the P. berghei rodent malaria model\",\n      \"pmids\": [\"39908102\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Negative phenotype does not identify which MIPs provide the redundant function\",\n        \"Does not assay microtubule integrity or subtle fitness defects beyond transmission\",\n        \"Shown in P. berghei; not directly tested in P. falciparum\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown whether the thioredoxin-like fold of TrxL1 exerts any redox function inside the microtubule lumen, and which factors direct its stage-specific luminal assembly.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"No link established between TrxL1 redox chemistry and its structural microtubule role\",\n        \"Partner MIPs and assembly determinants of the interrupted luminal helix are uncharacterized in this corpus\",\n        \"No structural or functional data for TrxL1 outside mosquito stages\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008017\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0015036\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005874\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:1904115\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0007017\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0006355\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [\n      \"Interrupted luminal helix (ILH) within subpellicular microtubules of mosquito-stage parasites [#0]\"\n    ],\n    \"partners\": [\n      \"PfAP2-EXP2 (transcriptional activator binding the TrxL1 locus) [#3]\",\n      \"Glutathione/glutaredoxin system (reduces TrxL1) [#2]\"\n    ],\n    \"other_free_text\": [\n      \"TrxL1 is a microtubule inner protein reinforcing 13-protofilament subpellicular microtubules, assembled stage-specifically in ookinetes and sporozoites but absent from merozoite and gametocyte microtubules [#0].\",\n      \"TrxL1 is a poor substrate for thioredoxin reductase but is reducible via the glutathione system [#2].\",\n      \"Deletion of TrxL1 in P. berghei is dispensable for transmission, indicating redundancy among SPMT-associated MIPs [#1].\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0919300","name":null,"product":"thioredoxin-like protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0820200","name":null,"product":"thioredoxin-like protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0717300","name":null,"product":"thioredoxin-like protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"TrxL1","evaluation":null}