BIOMAT Database Logo BIOMAT Database Logo

Engineering and expression in Drosophila melanogaster of a xanthine dehydrogenase (rosy) variant. 1996

W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
School of Biological Sciences and Chemistry, University of Sussex, Brighton, U.K.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D004331 Drosophila melanogaster A species of fruit fly frequently used in genetics because of the large size of its chromosomes. D. melanogaster,Drosophila melanogasters,melanogaster, Drosophila
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D014644 Genetic Variation Genotypic differences observed among individuals in a population. Genetic Diversity,Variation, Genetic,Diversity, Genetic,Diversities, Genetic,Genetic Diversities,Genetic Variations,Variations, Genetic
D014968 Xanthine Dehydrogenase An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes. Purine Hydroxylase I,Xanthine Oxidoreductase,Dehydrogenase, Xanthine,Oxidoreductase, Xanthine
D015202 Protein Engineering Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes. Genetic Engineering of Proteins,Genetic Engineering, Protein,Proteins, Genetic Engineering,Engineering, Protein,Engineering, Protein Genetic,Protein Genetic Engineering
D016133 Polymerase Chain Reaction In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships. Anchored PCR,Inverse PCR,Nested PCR,PCR,Anchored Polymerase Chain Reaction,Inverse Polymerase Chain Reaction,Nested Polymerase Chain Reaction,PCR, Anchored,PCR, Inverse,PCR, Nested,Polymerase Chain Reactions,Reaction, Polymerase Chain,Reactions, Polymerase Chain
D016297 Mutagenesis, Site-Directed Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion. Mutagenesis, Oligonucleotide-Directed,Mutagenesis, Site-Specific,Oligonucleotide-Directed Mutagenesis,Site-Directed Mutagenesis,Site-Specific Mutagenesis,Mutageneses, Oligonucleotide-Directed,Mutageneses, Site-Directed,Mutageneses, Site-Specific,Mutagenesis, Oligonucleotide Directed,Mutagenesis, Site Directed,Mutagenesis, Site Specific,Oligonucleotide Directed Mutagenesis,Oligonucleotide-Directed Mutageneses,Site Directed Mutagenesis,Site Specific Mutagenesis,Site-Directed Mutageneses,Site-Specific Mutageneses

Related Publications

W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
The rosy locus and xanthine dehydrogenase in Drosophila melanogaster.
January 1990, Progress in clinical and biological research,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
The rosy locus in Drosophila melanogaster: xanthine dehydrogenase and eye pigments.
December 1991, Genetics,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster.
May 1987, Genetics,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
An analysis of xanthine dehydrogenase negative mutants of the rosy locus in Drosophila melanogaster.
September 1979, Canadian journal of genetics and cytology. Journal canadien de genetique et de cytologie,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
Genetic limits of the xanthine dehydrogenase structural element within the rosy locus in Drosophila melanogaster.
November 1974, Genetics,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
Role and oxidation state of the pterin molybdenum cofactor of molybdenum enzymes: studies of a Drosophila melanogaster xanthine dehydrogenase (rosy) variant, G1011E.
February 1996, Biochemical Society transactions,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
PURIFICATION OF XANTHINE DEHYDROGENASE FROM DROSOPHILA MELANOGASTER.
December 1964, Biochimica et biophysica acta,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
Expression of xanthine dehydrogenase activity during embryonic development of Drosophila melanogaster.
July 1973, Developmental biology,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
Genetic regulation of xanthine dehydrogenase in Drosophila melanogaster.
January 1965, Federation proceedings,
W A Doyle, and J F Burke, and A Chovnick, and F L Dutton, and C Russell, and J R Whittle, and R C Bray
Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster.
November 1965, Genetics,
Copied contents to your clipboard!