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(2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Phosphatidylserine-bearing surfaces and receptors","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"4db37bf6-c399-59a5-a375-64d4f9d710cc","evidence_kind":"source_excerpt","locator":"Lines 591-602","start_line":591,"end_line":602,"excerpt":"### k2-gas6-axl\nFunctional AXL activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement.\nCondition category: normal\nnutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: A modified signaling protein needs the right membrane surface to activate its receptor.\norganism: Recombinant human GAS6 and TAM reporter systems\ntissue_or_cell_type: Phosphatidylserine-bearing surfaces and receptors\nexperimental_model: TAM reporter cells and GAS6 domain/point mutagenesis\nlimitations: Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested.\nexposure: Warfarin, Gla/EGF mutations and PS-positive cells or vesicles\nevidence_span: {\"source_cache\": \"artifacts/k2-research/29176978.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7\", \"start_char\": 0, \"end_char\": 1704, \"text_sha256\": \"14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7\"}\n[k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. 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