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Details on Person In vitro studies using purified NLRP1 and caspase-1 suggest ...
| Class:Id | Summation:844441 |
|---|---|
| _displayName | In vitro studies using purified NLRP1 and caspase-1 suggest ... |
| _timestamp | 2010-06-14 16:02:43 |
| created | [InstanceEdit:844451] Jupe, S, 2010-05-28 |
| modified | [InstanceEdit:844509] Jupe, S, 2010-05-28 [InstanceEdit:877366] Jupe, S, 2010-06-14 |
| text | In vitro studies using purified NLRP1 and caspase-1 suggest that MDP induces a conformational change in NLRP1 that allows it to bind nucleotides and oligomerize, creating a binding platform for caspase-1 (Faustin et al. 2008). There is no direct evidence that NLRP1 binds MDP so the mechanism that stimulates NLRP1 is unclear. |
| (summation) | [BlackBoxEvent:844447] NLRP1 senses MDP [Homo sapiens] [BlackBoxEvent:9988918] NLRP1 senses bacterial MDP (to replace 844447) [Homo sapiens] |
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No pathways have been reviewed or authored by In vitro studies using purified NLRP1 and caspase-1 suggest ... (844441)
