Structure-guided inhibitor design for human FAAH by interspecies active site conversion (Q27651822)

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Douglas S Johnson

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Zhigang Wang

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Daniel S Everdeen

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Brandon Pabst

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Keshab Bhattacharya

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Richard A Nugent

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Satwik Kamtekar

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Kay Ahn

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Raymond C Stevens

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

2 September 2008

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published in

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volume

105

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issue

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page(s)

12820-4

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cites work

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The endogenous cannabinoid system protects against colonic inflammation

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Discovering potent and selective reversible inhibitors of enzymes in complex proteomes

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Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamide

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Mice lacking fatty acid amide hydrolase exhibit a cannabinoid receptor-mediated phenotypic hypoalgesia

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Evaluation of fatty acid amide hydrolase inhibition in murine models of emotionality

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Reduced anxiety-like behaviour induced by genetic and pharmacological inhibition of the endocannabinoid-degrading enzyme fatty acid amide hydrolase (FAAH) is mediated by CB1 receptors

21 January 2018

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Characterization of the sleep-wake patterns in mice lacking fatty acid amide hydrolase

21 January 2018

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Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization

27 November 2018

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C-H...pi-interactions in proteins

27 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/18753625

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Study of the amidase signature group

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/18753625

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.0806121105

1 reference

ADS bibcode

2008PNAS..10512820M

0 references

1 reference

1 reference

PubMed publication ID

18753625

1 reference