{"id":"24b1ec8a-507a-511f-82e1-99185684ee76","stable_key":"44eaeae5-557a-552b-8998-884f30462e2a:sulforaphane-urease-inactivation","predicate":"inactivates","statement":"Sulforaphane caused time-dependent urease inactivation with spectroscopic evidence of cysteine-thiol adduct formation.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"08b7ba5f-a24b-5fda-87ba-b0310fe4819b","mechanism_event_label":"The compound can chemically inhibit a bacterial enzyme.","subject":{"id":"67e70215-70c4-546a-84b4-0819fac0b326","slug":"sulforaphane","display_name":"Sulforaphane / SFN, stereochemistry specified per study","entity_type_key":"small_molecule"},"object":{"id":"40e0758b-f676-5ba0-b980-4827a5d356c0","slug":"h-pylori-urease","display_name":"Helicobacter pylori urease complex","entity_type_key":"protein_complex"},"evidence_count":1,"mechanism_event":{"id":"08b7ba5f-a24b-5fda-87ba-b0310fe4819b","stable_key":"44eaeae5-557a-552b-8998-884f30462e2a:sulforaphane-urease-inactivation-event","event_type":"biochemical_relationship","label":"The compound can chemically inhibit a bacterial enzyme.","description":"Sulforaphane caused time-dependent urease inactivation with spectroscopic evidence of cysteine-thiol adduct formation.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"67e70215-70c4-546a-84b4-0819fac0b326","slug":"sulforaphane","display_name":"Sulforaphane / SFN, stereochemistry specified per study","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"40e0758b-f676-5ba0-b980-4827a5d356c0","slug":"h-pylori-urease","display_name":"Helicobacter pylori urease complex","entity_type_key":"protein_complex"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""}]},"contexts":[{"dimension":"evidence_span","value_text":"{\"source_cache\": \"artifacts/sulforaphane-research/23583386.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577\", \"start_char\": 0, \"end_char\": 1843, \"text_sha256\": \"4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577\"}","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Purified urease assays and bacterial comparisons","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Sulforaphane and related isothiocyanates","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Urease inactivation was not obligatory for bacterial killing; do not portray one target as the entire antibacterial mechanism.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Sulforaphane research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"sulforaphane","display_name":"Sulforaphane / SFN, stereochemistry specified per study","entity_type_key":"small_molecule"}},{"dimension":"organism","value_text":"H. pylori and jack-bean urease experiments","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"The compound can chemically inhibit a bacterial enzyme.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[sulforaphane-p23583386] Urease from Helicobacter pylori is inactivated by sulforaphane and other isothiocyanates. (2013). https://pubmed.ncbi.nlm.nih.gov/23583386/ DOI: 10.1016/j.bbrc.2013.03.126","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Urease modification and bacterial killing","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"8cec9326-9d51-542c-8fa9-69d801f79494","evidence_kind":"source_excerpt","locator":"Lines 1282-1293","start_line":1282,"end_line":1293,"excerpt":"### sulforaphane-urease-inactivation\nSulforaphane caused time-dependent urease inactivation with spectroscopic evidence of cysteine-thiol adduct formation.\nCondition category: normal\nnutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The compound can chemically inhibit a bacterial enzyme.\norganism: H. pylori and jack-bean urease experiments\ntissue_or_cell_type: Urease modification and bacterial killing\nexperimental_model: Purified urease assays and bacterial comparisons\nlimitations: Urease inactivation was not obligatory for bacterial killing; do not portray one target as the entire antibacterial mechanism.\nexposure: Sulforaphane and related isothiocyanates\nevidence_span: {\"source_cache\": \"artifacts/sulforaphane-research/23583386.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577\", \"start_char\": 0, \"end_char\": 1843, \"text_sha256\": \"4542d001efffa337d1aae4de7767a914ed8cd951bc5e56ded5183046abe10577\"}\n[sulforaphane-p23583386] Urease from Helicobacter pylori is inactivated by sulforaphane and other isothiocyanates. 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