{"gene":"PF3D7_1134100","run_date":"2026-09-08T12:51:28","timeline":{"discoveries":[{"year":2006,"finding":"PF3D7_1134100 (PDI-11) was identified as one of nine PDI-like molecules in Plasmodium falciparum; it was named PfPDI-11 based on its chromosomal location and characterized for sequence, phylogenetic relationships, protein structure, and thioredoxin-domain composition. Its membership in the P. falciparum PDI family was established by gene isolation and sequence analysis.","method":"Gene isolation, sequence analysis, phylogenetic comparison, protein structure and thioredoxin-domain analysis","journal":"International journal for parasitology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single paper, sequence/bioinformatic characterization only; no direct biochemical assay reported for PDI-11 itself (biochemical work was done on the sibling PfPDI-8, not PDI-11)","pmids":["16806221"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2005,"finding":"Overproduction of P. falciparum protein disulfide isomerase (PfPDI, corresponding to PF3D7_1134100/PDI-11 as the sole PfPDI described in this study) in Pichia pastoris increased the proportion of the correctly folded Pfs25(A) isoform relative to Pfs25(B), and altered the O-linked glycosylation pattern of Pfs25(A) compared to expression without PfPDI overproduction, demonstrating that PDI-11 can influence disulfide-dependent folding and post-translational modification of a heterologous substrate in a yeast expression system.","method":"Heterologous overexpression in Pichia pastoris, biochemical characterization (mass spectrometry, isoform ratio analysis) of co-expressed vaccine candidate Pfs25","journal":"Journal of biotechnology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single expression-system experiment; the identity of 'PfPDI' as PF3D7_1134100 vs. another family member is not unambiguously established in this abstract, and the experiment is performed in yeast, not in Plasmodium","pmids":["16274825"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2003,"finding":"P. falciparum protein disulfide isomerase (the PDI identified in this study by FP-agarose pulldown) was found to bind ferriprotoporphyrin IX (heme/FP) immobilized on agarose, identifying it as an FP-interacting protein in P. falciparum lysates. Note: the abstract does not specify which PDI family member was recovered; attribution to PDI-11 specifically cannot be confirmed.","method":"Affinity pulldown with FP-agarose followed by mass spectrometry identification","journal":"The Journal of biological chemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single pulldown experiment; the specific PDI family member (PDI-11 vs. others) is not identified at the gene level in the abstract, making attribution uncertain","pmids":["12748176"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"A cell-permeable divinyl sulfone (DVSF) crosslinking strategy was developed to trap and identify substrates of thioredoxin (Trx)-domain-containing proteins (including PDI family members) in P. falciparum via mixed disulfide intermediate capture followed by immunoprecipitation-mass spectrometry. This method is described as applicable to PDI-11/PDI family members but no PDI-11-specific substrate is reported in the abstract.","method":"Activity-based crosslinking with divinyl sulfone (DVSF) followed by immunoprecipitation and mass spectrometry","journal":"Bio-protocol","confidence":"Low","confidence_rationale":"Tier 3 / Weak — methodological paper; no PDI-11-specific substrate or result is identified in the abstract","pmids":["35340291"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1134100 (PDI-11) is a member of the P. falciparum protein disulfide isomerase family, identified by chromosomal location and sequence/thioredoxin-domain analysis; beyond its family membership and the demonstration that overexpression of a PfPDI (possibly PDI-11) in yeast shifts folding of a heterologous disulfide-rich substrate, no direct biochemical mechanism, substrate, or localization has been experimentally established specifically for PDI-11 in available literature."},"narrative":{"mechanistic_narrative":"PF3D7_1134100 (PDI-11) is one of nine protein disulfide isomerase-like molecules encoded by Plasmodium falciparum, assigned to the PfPDI family by chromosomal location, sequence, phylogeny, and thioredoxin-domain composition [PMID:16806221]. Direct biochemical characterization specific to PDI-11 is limited: in a Pichia pastoris heterologous system, overproduction of a P. falciparum PDI increased the fraction of the correctly folded Pfs25(A) isoform and altered its O-linked glycosylation, indicating that a PfPDI can influence disulfide-dependent folding and post-translational modification of a heterologous substrate [PMID:16274825], but this study did not unambiguously resolve whether the enzyme assayed was PDI-11 or another family member. Beyond family membership [PMID:16806221] and this yeast folding activity attributed to a PfPDI [PMID:16274825], no PDI-11-specific substrate, catalytic mechanism, native localization, or in-parasite function has been experimentally established in the available corpus.","teleology":[{"year":2003,"claim":"Whether a P. falciparum PDI physically engages the heme byproduct of hemoglobin digestion was addressed to place thiol-oxidoreductases in the parasite's heme-handling environment, but the recovered PDI was not resolved to the gene level.","evidence":"Ferriprotoporphyrin IX (FP)-agarose affinity pulldown from parasite lysate with mass spectrometry identification","pmids":["12748176"],"confidence":"Low","gaps":["The specific PDI family member recovered was not identified at the gene level, so attribution to PDI-11 cannot be confirmed","No functional consequence of FP binding was established","Single pulldown without reciprocal or genetic validation"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2005,"claim":"The question of whether a PfPDI possesses functional disulfide-folding activity was tested by asking if it could improve folding of a disulfide-rich malaria antigen in a heterologous host.","evidence":"Heterologous overexpression of PfPDI in Pichia pastoris co-expressing Pfs25, with mass spectrometry and isoform-ratio analysis of the folded product","pmids":["16274825"],"confidence":"Low","gaps":["The identity of the assayed 'PfPDI' as PF3D7_1134100 versus another family member is not unambiguously established","Activity was measured in yeast, not in Plasmodium","No native substrate or in-parasite folding role was demonstrated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2006,"claim":"To define the enzyme's identity, PDI-11 was formally delineated as a distinct member of the P. falciparum PDI family, establishing its sequence, thioredoxin-domain architecture, and phylogenetic placement.","evidence":"Gene isolation, sequence and phylogenetic analysis, and thioredoxin-domain characterization of nine PfPDI-like molecules","pmids":["16806221"],"confidence":"Low","gaps":["Bioinformatic/sequence characterization only; no direct biochemical assay was performed on PDI-11 itself","Native localization within the parasite was not determined","Catalytic activity and substrates specific to PDI-11 remain unassigned"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"claim":"A means to capture the endogenous substrates of Trx-domain oxidoreductases, including PDI family members, was developed to move beyond bioinformatic assignment toward direct substrate mapping.","evidence":"Cell-permeable divinyl sulfone (DVSF) activity-based crosslinking trapping mixed-disulfide intermediates, followed by immunoprecipitation-mass spectrometry (methodological/protocol paper)","pmids":["35340291"],"confidence":"Low","gaps":["Methodological paper; no PDI-11-specific substrate is reported","Applicability is stated for PDI family members generally, not demonstrated for PDI-11","No validation of trapped complexes for this gene"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"It remains unknown whether PDI-11 catalyzes disulfide isomerization on defined native Plasmodium substrates, where it localizes in the parasite, and what its role is in the parasite life cycle, as no experiment in the corpus assigns a biochemical activity or substrate unambiguously to PF3D7_1134100.","evidence":"","pmids":[],"confidence":"Low","gaps":["No native substrate identified specifically for PDI-11","No in-parasite localization or genetic essentiality data","The activity attributed to 'PfPDI' in yeast has not been genetically tied to PF3D7_1134100"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["Member of the nine-gene P. falciparum protein disulfide isomerase family, assigned by chromosomal location and thioredoxin-domain composition [#0]","A PfPDI improved folding and altered O-linked glycosylation of the Pfs25 antigen when overexpressed in Pichia pastoris, though the assayed enzyme was not unambiguously resolved as PDI-11 [#1]","A P. falciparum PDI binds ferriprotoporphyrin IX in lysate pulldowns, but the recovered family member was not identified at the gene level [#2]","A DVSF activity-based crosslinking method exists for capturing Trx/PDI-family substrates but reports no PDI-11-specific substrate [#3]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"16274825","id":"PMC_16274825","title":"Overproduction of Pichia pastoris or Plasmodium falciparum protein disulfide isomerase affects expression, folding and O-linked glycosylation of a malaria vaccine candidate expressed in P. pastoris.","date":"2005","source":"Journal of biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/16274825","citation_count":71,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"12748176","id":"PMC_12748176","title":"Identification and characterization of heme-interacting proteins in the malaria parasite, Plasmodium falciparum.","date":"2003","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/12748176","citation_count":58,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"16806221","id":"PMC_16806221","title":"Protein disulfide isomerase assisted protein folding in malaria parasites.","date":"2006","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/16806221","citation_count":39,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"17166645","id":"PMC_17166645","title":"Biochemical properties and cellular localization of Plasmodium falciparum protein disulfide isomerase.","date":"2006","source":"Biochimie","url":"https://pubmed.ncbi.nlm.nih.gov/17166645","citation_count":29,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"11078887","id":"PMC_11078887","title":"Cloning of Plasmodium falciparum protein disulfide isomerase homologue by affinity purification using the antiplasmodial inhibitor 1,4-bis[3-[N-(cyclohexyl methyl)amino]propyl]piperazine.","date":"2000","source":"FEBS letters","url":"https://pubmed.ncbi.nlm.nih.gov/11078887","citation_count":25,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"22658767","id":"PMC_22658767","title":"Plasmodium yoelii blood-stage antigens newly identified by immunoaffinity using purified IgG antibodies from malaria-resistant mice.","date":"2012","source":"Immunobiology","url":"https://pubmed.ncbi.nlm.nih.gov/22658767","citation_count":10,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32523082","id":"PMC_32523082","title":"Plasmodium falciparum immunodominant IgG epitopes in subclinical malaria.","date":"2020","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/32523082","citation_count":8,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19615402","id":"PMC_19615402","title":"Gene sequencing, modelling and immunolocalization of the protein disulfide isomerase from Plasmodium chabaudi.","date":"2009","source":"International journal of biological macromolecules","url":"https://pubmed.ncbi.nlm.nih.gov/19615402","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37302957","id":"PMC_37302957","title":"Protein disulfide isomerases - a way to tackle malaria.","date":"2023","source":"Trends in parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/37302957","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35340291","id":"PMC_35340291","title":"Activity-based Crosslinking to Identify Substrates of Thioredoxin-domain Proteinsin Malaria Parasites.","date":"2022","source":"Bio-protocol","url":"https://pubmed.ncbi.nlm.nih.gov/35340291","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["protein disulfide-isomerase"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7474,"output_tokens":1366,"usd":0.021456,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6245,"output_tokens":2353,"usd":0.045025,"stage2_stop_reason":"end_turn"},"total_usd":0.066481,"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\": \"PF3D7_1134100 (PDI-11) was identified as one of nine PDI-like molecules in Plasmodium falciparum; it was named PfPDI-11 based on its chromosomal location and characterized for sequence, phylogenetic relationships, protein structure, and thioredoxin-domain composition. Its membership in the P. falciparum PDI family was established by gene isolation and sequence analysis.\",\n      \"method\": \"Gene isolation, sequence analysis, phylogenetic comparison, protein structure and thioredoxin-domain analysis\",\n      \"journal\": \"International journal for parasitology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single paper, sequence/bioinformatic characterization only; no direct biochemical assay reported for PDI-11 itself (biochemical work was done on the sibling PfPDI-8, not PDI-11)\",\n      \"pmids\": [\"16806221\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2005,\n      \"finding\": \"Overproduction of P. falciparum protein disulfide isomerase (PfPDI, corresponding to PF3D7_1134100/PDI-11 as the sole PfPDI described in this study) in Pichia pastoris increased the proportion of the correctly folded Pfs25(A) isoform relative to Pfs25(B), and altered the O-linked glycosylation pattern of Pfs25(A) compared to expression without PfPDI overproduction, demonstrating that PDI-11 can influence disulfide-dependent folding and post-translational modification of a heterologous substrate in a yeast expression system.\",\n      \"method\": \"Heterologous overexpression in Pichia pastoris, biochemical characterization (mass spectrometry, isoform ratio analysis) of co-expressed vaccine candidate Pfs25\",\n      \"journal\": \"Journal of biotechnology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single expression-system experiment; the identity of 'PfPDI' as PF3D7_1134100 vs. another family member is not unambiguously established in this abstract, and the experiment is performed in yeast, not in Plasmodium\",\n      \"pmids\": [\"16274825\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"P. falciparum protein disulfide isomerase (the PDI identified in this study by FP-agarose pulldown) was found to bind ferriprotoporphyrin IX (heme/FP) immobilized on agarose, identifying it as an FP-interacting protein in P. falciparum lysates. Note: the abstract does not specify which PDI family member was recovered; attribution to PDI-11 specifically cannot be confirmed.\",\n      \"method\": \"Affinity pulldown with FP-agarose followed by mass spectrometry identification\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single pulldown experiment; the specific PDI family member (PDI-11 vs. others) is not identified at the gene level in the abstract, making attribution uncertain\",\n      \"pmids\": [\"12748176\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"A cell-permeable divinyl sulfone (DVSF) crosslinking strategy was developed to trap and identify substrates of thioredoxin (Trx)-domain-containing proteins (including PDI family members) in P. falciparum via mixed disulfide intermediate capture followed by immunoprecipitation-mass spectrometry. This method is described as applicable to PDI-11/PDI family members but no PDI-11-specific substrate is reported in the abstract.\",\n      \"method\": \"Activity-based crosslinking with divinyl sulfone (DVSF) followed by immunoprecipitation and mass spectrometry\",\n      \"journal\": \"Bio-protocol\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — methodological paper; no PDI-11-specific substrate or result is identified in the abstract\",\n      \"pmids\": [\"35340291\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"PF3D7_1134100 (PDI-11) is a member of the P. falciparum protein disulfide isomerase family, identified by chromosomal location and sequence/thioredoxin-domain analysis; beyond its family membership and the demonstration that overexpression of a PfPDI (possibly PDI-11) in yeast shifts folding of a heterologous disulfide-rich substrate, no direct biochemical mechanism, substrate, or localization has been experimentally established specifically for PDI-11 in available literature.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1134100 (PDI-11) is one of nine protein disulfide isomerase-like molecules encoded by Plasmodium falciparum, assigned to the PfPDI family by chromosomal location, sequence, phylogeny, and thioredoxin-domain composition [#0]. Direct biochemical characterization specific to PDI-11 is limited: in a Pichia pastoris heterologous system, overproduction of a P. falciparum PDI increased the fraction of the correctly folded Pfs25(A) isoform and altered its O-linked glycosylation, indicating that a PfPDI can influence disulfide-dependent folding and post-translational modification of a heterologous substrate [#1], but this study did not unambiguously resolve whether the enzyme assayed was PDI-11 or another family member. Beyond family membership [#0] and this yeast folding activity attributed to a PfPDI [#1], no PDI-11-specific substrate, catalytic mechanism, native localization, or in-parasite function has been experimentally established in the available corpus.\"\n  ,\n  \"teleology\": [\n    {\n      \"year\": 2003,\n      \"claim\": \"Whether a P. falciparum PDI physically engages the heme byproduct of hemoglobin digestion was addressed to place thiol-oxidoreductases in the parasite's heme-handling environment, but the recovered PDI was not resolved to the gene level.\",\n      \"evidence\": \"Ferriprotoporphyrin IX (FP)-agarose affinity pulldown from parasite lysate with mass spectrometry identification\",\n      \"pmids\": [\"12748176\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"The specific PDI family member recovered was not identified at the gene level, so attribution to PDI-11 cannot be confirmed\",\n        \"No functional consequence of FP binding was established\",\n        \"Single pulldown without reciprocal or genetic validation\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"The question of whether a PfPDI possesses functional disulfide-folding activity was tested by asking if it could improve folding of a disulfide-rich malaria antigen in a heterologous host.\",\n      \"evidence\": \"Heterologous overexpression of PfPDI in Pichia pastoris co-expressing Pfs25, with mass spectrometry and isoform-ratio analysis of the folded product\",\n      \"pmids\": [\"16274825\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"The identity of the assayed 'PfPDI' as PF3D7_1134100 versus another family member is not unambiguously established\",\n        \"Activity was measured in yeast, not in Plasmodium\",\n        \"No native substrate or in-parasite folding role was demonstrated\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"To define the enzyme's identity, PDI-11 was formally delineated as a distinct member of the P. falciparum PDI family, establishing its sequence, thioredoxin-domain architecture, and phylogenetic placement.\",\n      \"evidence\": \"Gene isolation, sequence and phylogenetic analysis, and thioredoxin-domain characterization of nine PfPDI-like molecules\",\n      \"pmids\": [\"16806221\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Bioinformatic/sequence characterization only; no direct biochemical assay was performed on PDI-11 itself\",\n        \"Native localization within the parasite was not determined\",\n        \"Catalytic activity and substrates specific to PDI-11 remain unassigned\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"A means to capture the endogenous substrates of Trx-domain oxidoreductases, including PDI family members, was developed to move beyond bioinformatic assignment toward direct substrate mapping.\",\n      \"evidence\": \"Cell-permeable divinyl sulfone (DVSF) activity-based crosslinking trapping mixed-disulfide intermediates, followed by immunoprecipitation-mass spectrometry (methodological/protocol paper)\",\n      \"pmids\": [\"35340291\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Methodological paper; no PDI-11-specific substrate is reported\",\n        \"Applicability is stated for PDI family members generally, not demonstrated for PDI-11\",\n        \"No validation of trapped complexes for this gene\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown whether PDI-11 catalyzes disulfide isomerization on defined native Plasmodium substrates, where it localizes in the parasite, and what its role is in the parasite life cycle, as no experiment in the corpus assigns a biochemical activity or substrate unambiguously to PF3D7_1134100.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No native substrate identified specifically for PDI-11\",\n        \"No in-parasite localization or genetic essentiality data\",\n        \"The activity attributed to 'PfPDI' in yeast has not been genetically tied to PF3D7_1134100\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003756\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0020037\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006457\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"Member of the nine-gene P. falciparum protein disulfide isomerase family, assigned by chromosomal location and thioredoxin-domain composition [#0]\",\n      \"A PfPDI improved folding and altered O-linked glycosylation of the Pfs25 antigen when overexpressed in Pichia pastoris, though the assayed enzyme was not unambiguously resolved as PDI-11 [#1]\",\n      \"A P. falciparum PDI binds ferriprotoporphyrin IX in lysate pulldowns, but the recovered family member was not identified at the gene level [#2]\",\n      \"A DVSF activity-based crosslinking method exists for capturing Trx/PDI-family substrates but reports no PDI-11-specific substrate [#3]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1134100","name":null,"product":"protein disulfide-isomerase, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0914300","name":null,"product":"protein disulfide-isomerase, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0932300","name":null,"product":"protein disulfide-isomerase, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"PDI-11","evaluation":null}