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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2010-2-18
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pubmed:abstractText |
Two enzymes, alpha glycerophosphate dehydrogenase (GPDH-1) in the cytoplasm and alpha glycerophosphate oxidase (GPO-1) in the mitochondrion cooperate in Drosophila flight muscles to generate the ATP needed for muscle contraction. Null mutants for either enzyme cannot fly. Here, we characterize 15 ethyl methane sulfonate (EMS)-induced mutants in GPDH-1 at the molecular level and assess their effects on structural and evolutionarily conserved domains of this enzyme. In addition, we molecularly characterize 3 EMS-induced GPO-1 mutants and excisions of a P element insertion in the GPO-1 gene. The latter represent the best candidate for null or amorphic mutants in this gene.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-10471707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-10731132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-12756285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-16204217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-17249099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-18493052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-1851957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-2530131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-3135237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-3147213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-4154945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-4202771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-4624777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-6058005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-6414883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-6414884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19995806-9307964
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1465-7333
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
218-24
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pubmed:dateRevised |
2011-7-25
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pubmed:meshHeading |
pubmed-meshheading:19995806-Amino Acid Sequence,
pubmed-meshheading:19995806-Animals,
pubmed-meshheading:19995806-Animals, Genetically Modified,
pubmed-meshheading:19995806-DNA Mutational Analysis,
pubmed-meshheading:19995806-Drosophila melanogaster,
pubmed-meshheading:19995806-Enzyme Activation,
pubmed-meshheading:19995806-Flight, Animal,
pubmed-meshheading:19995806-Glycerolphosphate Dehydrogenase,
pubmed-meshheading:19995806-Glycerophosphates,
pubmed-meshheading:19995806-Molecular Sequence Data,
pubmed-meshheading:19995806-Mutant Proteins,
pubmed-meshheading:19995806-Mutation,
pubmed-meshheading:19995806-Protein Structure, Tertiary
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pubmed:articleTitle |
The alpha glycerophosphate cycle in Drosophila melanogaster V. molecular analysis of alpha glycerophosphate dehydrogenase and alpha glycerophosphate oxidase mutants.
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pubmed:affiliation |
Department of Molecular Biology and Genetics, 407 Biotechnology Building, Cornell University, Ithaca, NY 14853, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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