Title |
Specific use of start codons and cellular localization of splice variants of human phosphodiesterase 9A gene
|
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Published in |
BMC Molecular and Cell Biology, November 2006
|
DOI | 10.1186/1471-2199-7-39 |
Pubmed ID | |
Authors |
Carles Rentero, Pere Puigdomènech |
Abstract |
Phosphodiesterases are an important protein family that catalyse the hydrolysis of cyclic nucleotide monophosphates (cAMP and cGMP), second intracellular messengers responsible for transducing a variety of extra-cellular signals. A number of different splice variants have been observed for the human phosphodiesterase 9A gene, a cGMP-specific high-affinity PDE. These mRNAs differ in the use of specific combinations of exons located at the 5' end of the gene while the 3' half, that codes for the catalytic domain of the protein, always has the same combination of exons. It was observed that to deduce the protein sequence with the catalytic domain from all the variants, at least two ATG start codons have to be used. Alternatively some variants code for shorter non-functional polypeptides. |
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Demographic breakdown
Readers by professional status | Count | As % |
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