The tumor suppressor gene H-Rev107 functions as a novel Ca2+-independent cytosolic phospholipase A1/2 of the thiol hydrolase type

Journal of Lipid Research

Volumn 50, Issue 4, 2009, Pages 685-693

  Uyama, Toru ^a   Morishita, Jun ^a   Jin, Xing Hua ^a,b   Okamoto, Yasuo ^a,c   Tsuboi, Kazuhito ^a   Ueda, Natsuo ^a  

^a KAGAWA UNIVERSITY   (Japan)

^b QIQIHAR MEDICAL UNIVERSITY   (China)

^c KANAZAWA UNIVERSITY GRADUATE SCHOOL OF MEDICAL SCIENCE   (Japan)

Author keywords

Glycerophospholipid; Lecithin retinol acyltransferase; N acyltransferase

Indexed keywords

COMPLEMENTARY DNA; CYSTEINE; DITHIOTHREITOL; HISTIDINE; IODOACETIC ACID; PALMITIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHOLIPASE A1; PHOSPHOLIPASE A2; PROLINE; PROTEIN H REV107; RECOMBINANT PROTEIN; THIOL ESTER HYDROLASE; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; CALCIUM; CYTOSOLIC PHOSPHOLIPASE A2; HRASLS3 PROTEIN, HUMAN; HRASLS3 PROTEIN, MOUSE; HRASLS3 PROTEIN, RAT; PRIMER DNA; PROTEIN; SIGNAL PEPTIDE;

ACYLATION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL PROLIFERATION; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVITY; GENE FUNCTION; GENE LOCATION; HUMAN; HUMAN TISSUE; HYDROPHOBICITY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; RAT; REGULATORY MECHANISM; SITE DIRECTED MUTAGENESIS; TUMOR SUPPRESSOR GENE; ANIMAL; CHEMISTRY; GENE DELETION; GENETICS; MALE; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; TISSUE DISTRIBUTION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CALCIUM; CLONING, MOLECULAR; DNA PRIMERS; DNA, COMPLEMENTARY; GENES, TUMOR SUPPRESSOR; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MALE; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHOLIPASES A1; PHOSPHOLIPASES A2, CYTOSOLIC; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RATS; RECOMBINANT PROTEINS; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; TISSUE DISTRIBUTION; TUMOR SUPPRESSOR PROTEINS;

EID: 67449116736     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M800453-JLR200     Document Type: Article

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