{"id":"9507c70c-2cd5-506d-9f1b-0eab5c23656c","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-glrx-gapdh-tagging","predicate":"enhances_in_assay","statement":"Recombinant human glutaredoxin enhanced GAPDH S-glutathionylation under the tested GSSG conditions.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"6ce738ad-6e7b-5d9d-8579-40668749054d","mechanism_event_label":"Reaction conditions can change the direction of a redox enzyme’s effect.","subject":{"id":"9693fa26-7353-5e19-8cb0-c03c4564afea","slug":"glrx","display_name":"Human glutaredoxin 1 / GLRX","entity_type_key":"protein"},"object":{"id":"baa06723-69b9-55d7-b20a-83ca97ac898c","slug":"gapdh-s-glutathionylation","display_name":"S-Glutathionylation of purified human GAPDH","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"6ce738ad-6e7b-5d9d-8579-40668749054d","stable_key":"db0fc92e-b5ef-5667-a4c5-3ef257edbc9b:glutathione-glrx-gapdh-tagging-event","event_type":"biochemical_relationship","label":"Reaction conditions can change the direction of a redox enzyme’s effect.","description":"Recombinant human glutaredoxin enhanced GAPDH S-glutathionylation under the tested GSSG conditions.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"1d9b9d7b-3fdf-57af-b9dd-00194fa1de9e","slug":"oxidized-glutathione","display_name":"GSSG","entity_type_key":"small_molecule"},"role":"disulfide_source","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"9693fa26-7353-5e19-8cb0-c03c4564afea","slug":"glrx","display_name":"Human glutaredoxin 1 / GLRX","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"baa06723-69b9-55d7-b20a-83ca97ac898c","slug":"gapdh-s-glutathionylation","display_name":"S-Glutathionylation of purified human GAPDH","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/glutathione-research/9642155.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72\", \"start_char\": 0, \"end_char\": 1538, \"text_sha256\": \"701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified GAPDH oxidation and radiolabeled disulfide assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Hydrogen peroxide versus GSSG and glutaredoxin","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Glutathione research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"Human GAPDH; human or bacterial glutaredoxin","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Reaction conditions can change the direction of a redox enzyme’s effect.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Cell-free enzyme system","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"44ba7909-f316-527e-9502-2774576a5827","evidence_kind":"source_excerpt","locator":"Lines 866-877","start_line":866,"end_line":877,"excerpt":"### glutathione-glrx-gapdh-tagging\nRecombinant human glutaredoxin enhanced GAPDH S-glutathionylation under the tested GSSG conditions.\nCondition category: normal\nnutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Reaction conditions can change the direction of a redox enzyme’s effect.\norganism: Human GAPDH; human or bacterial glutaredoxin\ntissue_or_cell_type: Cell-free enzyme system\nexperimental_model: Purified GAPDH oxidation and radiolabeled disulfide assays\nlimitations: This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins.\nexposure: Hydrogen peroxide versus GSSG and glutaredoxin\nevidence_span: {\"source_cache\": \"artifacts/glutathione-research/9642155.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72\", \"start_char\": 0, \"end_char\": 1538, \"text_sha256\": \"701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72\"}\n[glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695","model_system":"Purified GAPDH oxidation and radiolabeled disulfide assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"9b7417fd-059d-5683-b452-71d1e3cf82d0","stable_key":"import-db0fc92e-b5ef-5667-a4c5-3ef257edbc9b","title":"Glutathione: metabolism, signaling and nutrient connections (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. 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