AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs

Nature Chemical Biology

Volumn 12, Issue 5, 2016, Pages 367-372

  Parsons, William H ^a   Kolar, Matthew J ^b   Kamat, Siddhesh S ^a   Cognetta, Armand B ^a   Hulce, Jonathan J ^a   Saez, Enrique ^a   Kahn, Barbara B ^c   Saghatelian, Alan ^b   Cravatt, Benjamin F ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FATTY ACID ESTER; HYDROLASE; HYDROLASE INHIBITOR; HYDROXY FATTY ACID; MEMBRANE ENZYME; PROTEIN ADTRP; PROTEIN AIG1; PROTEOME; UNCLASSIFIED DRUG; ADTRP PROTEIN, HUMAN; AIG1 PROTEIN, HUMAN; ESTER; FATTY ACID; HYDROXYACID; MEMBRANE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; FATTY ACID METABOLISM; GENETIC CONSERVATION; HUMAN; HUMAN CELL; HYDROLYSIS; LIPID METABOLISM; MAMMAL CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; WESTERN BLOTTING; GENE EXPRESSION REGULATION; GENETICS; HEK293 CELL LINE; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHYSIOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; CLONING, MOLECULAR; ESTERS; FATTY ACIDS; GENE EXPRESSION REGULATION; HEK293 CELLS; HUMANS; HYDROLASES; HYDROXY ACIDS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED;

EID: 84961743022     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2051     Document Type: Article

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