Mouse retinal dehydrogenase 4 (RALDH4), molecular cloning, cellular expression, and activity in 9-cis-retinoic acid biosynthesis in intact cells

Journal of Biological Chemistry

Volumn 278, Issue 11, 2003, Pages 9856-9861

  Lin, Min ^a   Zhang, Min ^a   Abraham, Michael ^a   Smith, Susan M ^b   Napoli, Joseph L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; DNA; PROTEINS;

MOLECULAR CLONING;

CLONING;

ALDEHYDE DEHYDROGENASE; ALITRETINOIN; AMINO ACID; COMPLEMENTARY DNA; MESSENGER RNA; OXIDOREDUCTASE; PROTEIN CRAD1; PROTEIN CRAD3; PROTEIN RDH1; RETINAL; RETINAL DEHYDROGENASE 1; RETINAL DEHYDROGENASE 2; RETINAL DEHYDROGENASE 3; RETINAL DEHYDROGENASE 4; UNCLASSIFIED DRUG; ALCOHOL DEHYDROGENASE; CIS RETINOL ANDROGEN DEHYDROGENASE; CIS-RETINOL - ANDROGEN DEHYDROGENASE; HYDROXYSTEROID DEHYDROGENASE; RDH1 PROTEIN, MOUSE; RETINAL DEHYDROGENASE; RETINOIC ACID;

ADOLESCENT; ANIMAL CELL; ARTICLE; BIOSYNTHESIS; EMBRYO; ENZYME ACTIVITY; FETUS; GENETIC TRANSFECTION; GLOMERULUS; IMMUNOHISTOCHEMISTRY; KIDNEY CORTEX; KIDNEY DISTAL TUBULE; KIDNEY MEDULLA; KIDNEY PROXIMAL TUBULE; LIVER; MALE; MOLECULAR CLONING; MOUSE; NONHUMAN; NORTHERN BLOTTING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CHO CELL; DOSE RESPONSE; ENZYMOLOGY; GENETICS; HAMSTER; IN SITU HYBRIDIZATION; KIDNEY; METABOLISM; MOLECULAR GENETICS; RAT; SEQUENCE HOMOLOGY; WESTERN BLOTTING;

ANIMALIA; GLOMERULUS;

ALCOHOL OXIDOREDUCTASES; ALDEHYDE OXIDOREDUCTASES; AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BLOTTING, NORTHERN; BLOTTING, WESTERN; CHO CELLS; CLONING, MOLECULAR; CRICETINAE; DNA, COMPLEMENTARY; DOSE-RESPONSE RELATIONSHIP, DRUG; HYDROXYSTEROID DEHYDROGENASES; IMMUNOHISTOCHEMISTRY; IN SITU HYBRIDIZATION; KIDNEY; LIVER; MICE; MOLECULAR SEQUENCE DATA; RATS; RETINAL DEHYDROGENASE; RNA, MESSENGER; SEQUENCE HOMOLOGY, AMINO ACID; TRETINOIN;

EID: 0037646508     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M211417200     Document Type: Article

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