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(2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Glutathione synthesis and substrate binding","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"86f4ef7d-7758-59f3-bcf3-2b4b75070a2c","evidence_kind":"source_excerpt","locator":"Lines 840-851","start_line":840,"end_line":851,"excerpt":"### sulforaphane-gcl-first-step\nGlutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step.\nCondition category: normal\nnutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The induced machinery still needs its amino-acid building blocks.\norganism: Human GSS\ntissue_or_cell_type: Glutathione synthesis and substrate binding\nexperimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics\nlimitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.\nexposure: S-loop variants; established biosynthetic reactions described in the introduction\nevidence_span: {\"source_cache\": \"artifacts/sulforaphane-research/30581542.fulltext.txt\", \"locator\": \"Primary full-text span; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1\", \"start_char\": 762, \"end_char\": 1092, \"text_sha256\": \"927fa13b085700c20b578ecabc7c8c17a66ea4600b90809e3061d12bcaea3849\"}\n[sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. 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