The minimal domain of adipose triglyceride lipase (ATGL) ranges until leucine 254 and can be activated and inhibited by CGI-58 and G0S2, respectively

PLoS ONE

Volumn 6, Issue 10, 2011, Pages

  Cornaciu, Irina ^a   Boeszoermenyi, Andras ^a   Lindermuth, Hanna ^a   Nagy, Harald M ^a   Cerk, Ines K ^a   Ebner, Catharina ^a   Salzburger, Barbara ^a   Gruber, Astrid ^a   Schweiger, Martina ^a   Zechner, Rudolf ^a   Lass, Achim ^a   Zimmermann, Robert ^a   Oberer, Monika ^a  

^a UNIVERSITY OF GRAZ   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ADIPOSE TRIACYLGLYCEROL LIPASE; COMPARATIVE GENE IDENTIFICATION 58 PROTEIN; G0 G1 SWITCH GENE 2 PROTEIN; LEUCINE; PATATIN LIKE PHOSPHOLIPASE DOMAIN CONTAINING 1; PATATIN LIKE PHOSPHOLIPASE DOMAIN CONTAINING 2; PATATIN LIKE PHOSPHOLIPASE DOMAIN CONTAINING 3; PATATIN LIKE PHOSPHOLIPASE DOMAIN CONTAINING 5; PHOSPHOLIPASE; REGULATOR PROTEIN; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; 1 ACYLGLYCEROPHOSPHATE ACYLTRANSFERASE; ABHD5 PROTEIN, MOUSE; CELL CYCLE PROTEIN; DESNUTRIN PROTEIN, MOUSE; G0S2 PROTEIN, MOUSE; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME INHIBITION; ENZYME REGULATION; IN VITRO STUDY; LIPOLYSIS; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; GENETICS; HYDROLYSIS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY;

MAMMALIA;

1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE; AMINO ACID SEQUENCE; ANIMALS; CELL CYCLE PROTEINS; CLONING, MOLECULAR; ENZYME ACTIVATION; HYDROLYSIS; LEUCINE; LIPASE; LIPOLYSIS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TRIGLYCERIDES;

EID: 80054778472     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026349     Document Type: Article

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