A protein from the cabbage looper, Trichoplusia ni, regulated by a bacterial infection is homologous to 3-dehydroecdysone 3β-reductase

Insect Biochemistry and Molecular Biology

Volumn 32, Issue 8, 2002, Pages 829-837

  Lundstrom A ^a   Kang, D ^a   Liu, G ^a   Fernandez, C ^b   Warren, J T ^c   Gilbert, L I ^c   Steiner, H ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b STOCKHOLM UNIVERSITY   (Sweden)

^c UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

Aldo keto reductase; Ecdysone; Immune response; Molting

Indexed keywords

3 DEHYDROECDYSONE 3BETA REDUCTASE; 3 HYDROXYSTEROID DEHYDROGENASES; 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; 3-DEHYDROECDYSONE 3BETA-REDUCTASE; ANTISERUM; COMPLEMENTARY DNA; ECDYSONE; INSECT PROTEIN; MAKISTERONE; OXIDOREDUCTASE; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; DRUG DERIVATIVE;

AMINO ACID SEQUENCE; ANIMAL; ARMYWORM; ARTICLE; BACTERIAL INFECTION; BACULOVIRUS EXPRESSION SYSTEM; CABBAGE; CHEMICAL STRUCTURE; CHEMISTRY; CONTROLLED STUDY; ENZYME LOCALIZATION; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYMOLOGY; FAT BODY; GENE; GENE CONTROL; GENE EXPRESSION; GENE INDUCTION; GENETICS; HEMOLYMPH; IMMUNOHISTOCHEMISTRY; INSECT; INTEGUMENT; INTRON; METABOLISM; MICROBIOLOGY; MOLECULAR CLONING; MOLECULAR GENETICS; MOTH; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; WESTERN BLOTTING;

BACTERIA (MICROORGANISMS); BRASSICA OLERACEA VAR. CAPITATA; INSECTA; SPODOPTERA LITTORALIS; TRICHOPLUSIA NI; UNIDENTIFIED BACULOVIRUS;

3-HYDROXYSTEROID DEHYDROGENASES; AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ECDYSONE; FAT BODY; GENE EXPRESSION; GENES, INSECT; INSECT PROTEINS; INTRONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOTHS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPODOPTERA; SUBSTRATE SPECIFICITY;

EID: 0035983284     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(01)00145-X     Document Type: Article

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