Acyl chain specificity of ceramide synthases is determined within a region of 150 residues in the tram-lag-CLN8 (TLC) domain

Journal of Biological Chemistry

Volumn 287, Issue 5, 2012, Pages 3197-3206

  Tidhar, Rotem ^a   Ben Dor, Shifra ^a   Wang, Elaine ^b   Kelly, Samuel ^b   Merrill, Alfred H ^b   Futerman, Anthony H ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOSYNTHESIS; CELL MEMBRANES; CERAMIDES; CHAINS;

ACYL CHAIN; ACYL-COA; C-TERMINUS; CERAMIDE SYNTHASE; CHAINS LENGTH; ENDOPLASMIC RETICULUM; MOLECULAR FEATURE; SYNTHESISED; TRANS-MEMBRANE PROTEINS; TRANSMEMBRANE PROTEINS;

PROTEINS;

CERAMIDE SYNTHASE; SYNTHETASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL STRAIN HEK293; CHIMERA; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

MAMMALIA;

EID: 84856305649     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.280271     Document Type: Article

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