{"gene":"PF3D7_0306300","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2001,"finding":"PF3D7_0306300 (GRX1/PfGrx-1) encodes a 12.4 kDa classical glutaredoxin with the active-site motif CPYC that displays glutathione-dependent glutaredoxin activity in the β-hydroxyethyl disulfide (HEDS) assay and reduces Trypanosoma brucei ribonucleotide reductase in vitro. Glutathione:HEDS transhydrogenase activity was detected in trophozoite extracts from multiple P. falciparum strains.","method":"In vitro HEDS transhydrogenase assay, recombinant protein overexpression in E. coli, insulin reduction assay","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — in vitro enzymatic assay with recombinant protein plus activity confirmed in parasite extracts across multiple strains; single lab but multiple orthogonal assays","pmids":["11479312"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"finding":"PF3D7_0306300 (GRX1) efficiently catalyzes protein deglutathionylation in P. falciparum, as demonstrated by enzymatic deglutathionylation assays; it is itself a target of S-glutathionylation and participates in the regulation of the parasite's glutathionylome.","method":"Enzymatic deglutathionylation assay, affinity purification of biotin-maleimide-tagged proteins, proteomics","journal":"Antioxidants & redox signaling","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — enzymatic activity demonstrated in vitro and by affinity-based proteomics; single lab, two orthogonal methods","pmids":["21595565"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2009,"finding":"PF3D7_0306300 (GRX1/PfGrx) undergoes reversible two-state unfolding (native ↔ unfolded) under guanidine hydrochloride and thermal denaturation; it is conformationally stable across pH 3.0–11.0 with maximum thermostability at pH 8.0 (Tm = 76.2 °C, ΔHm = 119 kcal/mol) and a small free energy of unfolding (1.56 kcal/mol at 25 °C).","method":"Isothermal guanidine hydrochloride-induced denaturation, pH-dependent thermal denaturation, protein stability curve analysis","journal":"Biochimie","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — rigorous biophysical characterization of the purified recombinant protein, single lab, no functional mutagenesis","pmids":["20006670"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"finding":"The atomic-resolution crystal structure of PF3D7_0306300 (GRX1/PfGrx1) was determined by sulfur single-wavelength anomalous diffraction (S-SAD). The structure reveals a conserved GSH-binding site with motifs CXXC, TVP, CDD, Lys26, and Gln/Arg63; the active-site Cys29 shows an alternate conformation due to radiation damage. PfGrx1 possesses several polar/charged substitutions that provide additional hydrogen bonds and salt bridges absent in other glutaredoxins.","method":"X-ray crystallography (S-SAD phasing), structural comparison with other glutaredoxins","journal":"Acta crystallographica. Section D, Biological crystallography","confidence":"High","confidence_rationale":"Tier 1 / Moderate — atomic-resolution crystal structure with active-site residue identification and structural annotation; single lab but rigorous structural determination","pmids":["24419382"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_0306300 (GRX1/PfGrx1) is a classical 12.4 kDa dithiol glutaredoxin with a CPYC active site that catalyzes glutathione-dependent thiol–disulfide exchange (including deglutathionylation of target proteins and reduction of ribonucleotide reductase) in P. falciparum; its atomic-resolution crystal structure confirms a conserved GSH-binding site, and biophysical studies show it is conformationally stable across a wide pH and temperature range."},"narrative":{"mechanistic_narrative":"PF3D7_0306300 (GRX1) is a classical 12.4 kDa dithiol glutaredoxin of Plasmodium falciparum that carries out glutathione-dependent thiol–disulfide exchange through its CPYC active-site motif [PMID:11479312]. It displays glutathione:HEDS transhydrogenase activity detectable in trophozoite extracts across multiple parasite strains and reduces heterologous (Trypanosoma brucei) ribonucleotide reductase in vitro, establishing it as an enzymatically active, GSH-dependent oxidoreductase [PMID:11479312]. GRX1 efficiently catalyzes protein deglutathionylation and is itself a substrate of S-glutathionylation, placing it within the regulation of the parasite glutathionylome [PMID:21595565]. Its atomic-resolution crystal structure confirms a conserved GSH-binding site built from the CXXC, TVP and CDD motifs together with Lys26 and Gln/Arg63, and reveals polar/charged substitutions that add hydrogen bonds and salt bridges not present in other glutaredoxins [PMID:24419382]; biophysically, the protein folds via reversible two-state unfolding and is conformationally stable across pH 3.0–11.0 with peak thermostability at pH 8.0 [PMID:20006670]. Beyond these in vitro biochemical, structural and biophysical characterizations, the in vivo physiological substrates and cellular role of GRX1 in the parasite have not been characterized in the available corpus.","teleology":[{"year":2001,"claim":"Establishing whether the P. falciparum genome encodes a functional classical glutaredoxin resolved whether the parasite possesses a dedicated glutathione-dependent thiol-disulfide oxidoreductase; the CPYC-motif protein was shown to be catalytically active.","evidence":"In vitro HEDS transhydrogenase and insulin reduction assays with recombinant protein, plus transhydrogenase activity in trophozoite extracts from multiple strains","pmids":["11479312"],"confidence":"High","gaps":["Ribonucleotide reductase substrate was heterologous (T. brucei), not the P. falciparum enzyme","No demonstration of endogenous physiological substrates in the parasite","No loss-of-function or essentiality data"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2009,"claim":"Determining the folding and stability behavior of GRX1 addressed how robust the enzyme is as a protein scaffold, showing reversible two-state unfolding and broad pH/thermal stability.","evidence":"Guanidine hydrochloride and pH-dependent thermal denaturation of purified recombinant protein with stability curve analysis","pmids":["20006670"],"confidence":"Medium","gaps":["No functional mutagenesis linking stability to catalysis","Biophysical study of isolated protein, not in a cellular context"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"claim":"Defining the catalytic repertoire of GRX1 beyond simple transhydrogenase activity showed it catalyzes protein deglutathionylation and is itself glutathionylated, embedding it in glutathionylome regulation.","evidence":"Enzymatic deglutathionylation assays and affinity purification of biotin-maleimide-tagged glutathionylated proteins with proteomics","pmids":["21595565"],"confidence":"Medium","gaps":["Specific in vivo deglutathionylation targets in the parasite not individually validated","Functional consequence of GRX1 self-glutathionylation unresolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"claim":"Solving the crystal structure answered how GRX1 recognizes glutathione at atomic resolution, identifying the conserved GSH-binding site and Plasmodium-specific polar/charged substitutions.","evidence":"X-ray crystallography with S-SAD phasing and structural comparison to other glutaredoxins","pmids":["24419382"],"confidence":"High","gaps":["Active-site Cys29 captured in an alternate conformation due to radiation damage","No structure of substrate- or GSH-bound complex","Functional significance of the parasite-specific substitutions not tested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The endogenous physiological substrates, cellular localization, essentiality, and in vivo redox role of GRX1 in the parasite life cycle remain undefined.","evidence":"","pmids":[],"confidence":"Low","gaps":["No genetic knockout/knockdown to establish essentiality","No identified native P. falciparum protein substrates in vivo","No subcellular localization data in the corpus"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["CPYC/CXXC active-site motif with GSH-binding residues (TVP, CDD, Lys26, Gln/Arg63) identified by crystallography [#3]","Reduces heterologous Trypanosoma brucei ribonucleotide reductase in vitro [#0]","Catalyzes protein deglutathionylation and is itself a target of S-glutathionylation [#1]","Reversible two-state folding, stable across pH 3.0–11.0 with Tm = 76.2 °C at pH 8.0 [#2]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"21595565","id":"PMC_21595565","title":"Protein S-glutathionylation in malaria parasites.","date":"2011","source":"Antioxidants & redox signaling","url":"https://pubmed.ncbi.nlm.nih.gov/21595565","citation_count":87,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"11479312","id":"PMC_11479312","title":"Plasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domain.","date":"2001","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/11479312","citation_count":83,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfGRX1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"24348249","id":"PMC_24348249","title":"Real-time imaging of the intracellular glutathione redox potential in the malaria parasite Plasmodium falciparum.","date":"2013","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/24348249","citation_count":49,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28062360","id":"PMC_28062360","title":"Determination of glutathione redox potential and pH value in subcellular compartments of malaria parasites.","date":"2017","source":"Free radical biology & medicine","url":"https://pubmed.ncbi.nlm.nih.gov/28062360","citation_count":29,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30129748","id":"PMC_30129748","title":"Stable Integration and Comparison of hGrx1-roGFP2 and sfroGFP2 Redox Probes in the Malaria Parasite Plasmodium falciparum.","date":"2018","source":"ACS infectious diseases","url":"https://pubmed.ncbi.nlm.nih.gov/30129748","citation_count":19,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26593282","id":"PMC_26593282","title":"Comparison of methods probing the intracellular redox milieu in Plasmodium falciparum.","date":"2015","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/26593282","citation_count":17,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"20006670","id":"PMC_20006670","title":"Conformational stability and energetics of Plasmodium falciparum glutaredoxin.","date":"2009","source":"Biochimie","url":"https://pubmed.ncbi.nlm.nih.gov/20006670","citation_count":12,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"24419382","id":"PMC_24419382","title":"Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.","date":"2013","source":"Acta crystallographica. Section D, Biological crystallography","url":"https://pubmed.ncbi.nlm.nih.gov/24419382","citation_count":11,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1","PfGRX1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35072524","id":"PMC_35072524","title":"Structure and Function of Redox-Sensitive Superfolder Green Fluorescent Protein Variant.","date":"2022","source":"Antioxidants & redox signaling","url":"https://pubmed.ncbi.nlm.nih.gov/35072524","citation_count":11,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40480411","id":"PMC_40480411","title":"Rational synthesis, activity and mechanism insights of a new aminoquinoline salt against malaria parasites: in vitro and in vivo approaches.","date":"2025","source":"Chemico-biological interactions","url":"https://pubmed.ncbi.nlm.nih.gov/40480411","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["glutaredoxin 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36558863","id":"PMC_36558863","title":"Rational-Based Discovery of Novel β-Carboline Derivatives as Potential Antimalarials: From In Silico Identification of Novel Targets to Inhibition of Experimental Cerebral Malaria.","date":"2022","source":"Pathogens (Basel, Switzerland)","url":"https://pubmed.ncbi.nlm.nih.gov/36558863","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfGRX1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":8935,"output_tokens":1348,"usd":0.023512,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6208,"output_tokens":2300,"usd":0.04427,"stage2_stop_reason":"end_turn"},"total_usd":0.067782,"stage1_batch_id":"msgbatch_01DbiymDmubkPpYvdbAu5a7V","stage2_batch_id":"msgbatch_012TbrWvMRH129T7PQ4SmvrJ","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2001,\n      \"finding\": \"PF3D7_0306300 (GRX1/PfGrx-1) encodes a 12.4 kDa classical glutaredoxin with the active-site motif CPYC that displays glutathione-dependent glutaredoxin activity in the β-hydroxyethyl disulfide (HEDS) assay and reduces Trypanosoma brucei ribonucleotide reductase in vitro. Glutathione:HEDS transhydrogenase activity was detected in trophozoite extracts from multiple P. falciparum strains.\",\n      \"method\": \"In vitro HEDS transhydrogenase assay, recombinant protein overexpression in E. coli, insulin reduction assay\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in vitro enzymatic assay with recombinant protein plus activity confirmed in parasite extracts across multiple strains; single lab but multiple orthogonal assays\",\n      \"pmids\": [\"11479312\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"PF3D7_0306300 (GRX1) efficiently catalyzes protein deglutathionylation in P. falciparum, as demonstrated by enzymatic deglutathionylation assays; it is itself a target of S-glutathionylation and participates in the regulation of the parasite's glutathionylome.\",\n      \"method\": \"Enzymatic deglutathionylation assay, affinity purification of biotin-maleimide-tagged proteins, proteomics\",\n      \"journal\": \"Antioxidants & redox signaling\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — enzymatic activity demonstrated in vitro and by affinity-based proteomics; single lab, two orthogonal methods\",\n      \"pmids\": [\"21595565\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"PF3D7_0306300 (GRX1/PfGrx) undergoes reversible two-state unfolding (native ↔ unfolded) under guanidine hydrochloride and thermal denaturation; it is conformationally stable across pH 3.0–11.0 with maximum thermostability at pH 8.0 (Tm = 76.2 °C, ΔHm = 119 kcal/mol) and a small free energy of unfolding (1.56 kcal/mol at 25 °C).\",\n      \"method\": \"Isothermal guanidine hydrochloride-induced denaturation, pH-dependent thermal denaturation, protein stability curve analysis\",\n      \"journal\": \"Biochimie\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — rigorous biophysical characterization of the purified recombinant protein, single lab, no functional mutagenesis\",\n      \"pmids\": [\"20006670\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"The atomic-resolution crystal structure of PF3D7_0306300 (GRX1/PfGrx1) was determined by sulfur single-wavelength anomalous diffraction (S-SAD). The structure reveals a conserved GSH-binding site with motifs CXXC, TVP, CDD, Lys26, and Gln/Arg63; the active-site Cys29 shows an alternate conformation due to radiation damage. PfGrx1 possesses several polar/charged substitutions that provide additional hydrogen bonds and salt bridges absent in other glutaredoxins.\",\n      \"method\": \"X-ray crystallography (S-SAD phasing), structural comparison with other glutaredoxins\",\n      \"journal\": \"Acta crystallographica. Section D, Biological crystallography\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — atomic-resolution crystal structure with active-site residue identification and structural annotation; single lab but rigorous structural determination\",\n      \"pmids\": [\"24419382\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_0306300 (GRX1/PfGrx1) is a classical 12.4 kDa dithiol glutaredoxin with a CPYC active site that catalyzes glutathione-dependent thiol–disulfide exchange (including deglutathionylation of target proteins and reduction of ribonucleotide reductase) in P. falciparum; its atomic-resolution crystal structure confirms a conserved GSH-binding site, and biophysical studies show it is conformationally stable across a wide pH and temperature range.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0306300 (GRX1) is a classical 12.4 kDa dithiol glutaredoxin of Plasmodium falciparum that carries out glutathione-dependent thiol\\u2013disulfide exchange through its CPYC active-site motif [#0]. It displays glutathione:HEDS transhydrogenase activity detectable in trophozoite extracts across multiple parasite strains and reduces heterologous (Trypanosoma brucei) ribonucleotide reductase in vitro, establishing it as an enzymatically active, GSH-dependent oxidoreductase [#0]. GRX1 efficiently catalyzes protein deglutathionylation and is itself a substrate of S-glutathionylation, placing it within the regulation of the parasite glutathionylome [#1]. Its atomic-resolution crystal structure confirms a conserved GSH-binding site built from the CXXC, TVP and CDD motifs together with Lys26 and Gln/Arg63, and reveals polar/charged substitutions that add hydrogen bonds and salt bridges not present in other glutaredoxins [#3]; biophysically, the protein folds via reversible two-state unfolding and is conformationally stable across pH 3.0\\u201311.0 with peak thermostability at pH 8.0 [#2]. Beyond these in vitro biochemical, structural and biophysical characterizations, the in vivo physiological substrates and cellular role of GRX1 in the parasite have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Establishing whether the P. falciparum genome encodes a functional classical glutaredoxin resolved whether the parasite possesses a dedicated glutathione-dependent thiol-disulfide oxidoreductase; the CPYC-motif protein was shown to be catalytically active.\",\n      \"evidence\": \"In vitro HEDS transhydrogenase and insulin reduction assays with recombinant protein, plus transhydrogenase activity in trophozoite extracts from multiple strains\",\n      \"pmids\": [\"11479312\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Ribonucleotide reductase substrate was heterologous (T. brucei), not the P. falciparum enzyme\",\n        \"No demonstration of endogenous physiological substrates in the parasite\",\n        \"No loss-of-function or essentiality data\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Determining the folding and stability behavior of GRX1 addressed how robust the enzyme is as a protein scaffold, showing reversible two-state unfolding and broad pH/thermal stability.\",\n      \"evidence\": \"Guanidine hydrochloride and pH-dependent thermal denaturation of purified recombinant protein with stability curve analysis\",\n      \"pmids\": [\"20006670\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No functional mutagenesis linking stability to catalysis\",\n        \"Biophysical study of isolated protein, not in a cellular context\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Defining the catalytic repertoire of GRX1 beyond simple transhydrogenase activity showed it catalyzes protein deglutathionylation and is itself glutathionylated, embedding it in glutathionylome regulation.\",\n      \"evidence\": \"Enzymatic deglutathionylation assays and affinity purification of biotin-maleimide-tagged glutathionylated proteins with proteomics\",\n      \"pmids\": [\"21595565\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Specific in vivo deglutathionylation targets in the parasite not individually validated\",\n        \"Functional consequence of GRX1 self-glutathionylation unresolved\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Solving the crystal structure answered how GRX1 recognizes glutathione at atomic resolution, identifying the conserved GSH-binding site and Plasmodium-specific polar/charged substitutions.\",\n      \"evidence\": \"X-ray crystallography with S-SAD phasing and structural comparison to other glutaredoxins\",\n      \"pmids\": [\"24419382\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Active-site Cys29 captured in an alternate conformation due to radiation damage\",\n        \"No structure of substrate- or GSH-bound complex\",\n        \"Functional significance of the parasite-specific substitutions not tested\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The endogenous physiological substrates, cellular localization, essentiality, and in vivo redox role of GRX1 in the parasite life cycle remain undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No genetic knockout/knockdown to establish essentiality\",\n        \"No identified native P. falciparum protein substrates in vivo\",\n        \"No subcellular localization data in the corpus\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0009055\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0015038\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0045454\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006749\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"CPYC/CXXC active-site motif with GSH-binding residues (TVP, CDD, Lys26, Gln/Arg63) identified by crystallography [#3]\",\n      \"Reduces heterologous Trypanosoma brucei ribonucleotide reductase in vitro [#0]\",\n      \"Catalyzes protein deglutathionylation and is itself a target of S-glutathionylation [#1]\",\n      \"Reversible two-state folding, stable across pH 3.0\\u201311.0 with Tm = 76.2 \\u00b0C at pH 8.0 [#2]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0306300","name":null,"product":"glutaredoxin 1","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0404700","name":null,"product":"glutaredoxin 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0836400","name":null,"product":"glutaredoxin 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"GRX1","evaluation":null}