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#bioinfo #publication #research #self
Question
we discover that FAAH inhibitors may bind to the [place and protien?] and several other BAs, and thus disrupt their cellular functions
Answer
dimerization interface of NMDA receptor (NMDAR)

Tags
#bioinfo #publication #research #self
Question
we discover that FAAH inhibitors may bind to the [place and protien?] and several other BAs, and thus disrupt their cellular functions
Answer
?

Tags
#bioinfo #publication #research #self
Question
we discover that FAAH inhibitors may bind to the [place and protien?] and several other BAs, and thus disrupt their cellular functions
Answer
dimerization interface of NMDA receptor (NMDAR)
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we discover that FAAH inhibitors may bind to the dimerization interface of NMDA receptor (NMDAR) and several other BAs, and thus disrupt their cellular functions

Original toplevel document

Molecular mechanisms involved in the side effects of fatty acid amide hydrolase inhibitors: a structural phenomics approach to proteome-wide cellular off-target deconvolution and disease association : npj Systems Biology and Applications
inding profile in the cellular context and on a structural proteome scale, and investigate the roles of these off-targets in impacting human physiology and pathology using text mining-based phenomics analysis. Using this integrative approach, <span>we discover that FAAH inhibitors may bind to the dimerization interface of NMDA receptor (NMDAR) and several other BAs, and thus disrupt their cellular functions. Specifically, the malfunction of the NMDAR is associated with a wide spectrum of brain disorders that are directly related to the observed side effects of FAAH inhibitors. This finding

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