Partial characterization of the gene encoding myoadenylate deaminase from the teleost fish Platichthys flesus
Fish Physiology and Biochemistry, ISSN: 0920-1742, Vol: 36, Issue: 4, Page: 819-825
2010
- 6Citations
- 9Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations6
- Citation Indexes6
- CrossRef3
- Captures9
- Readers9
Article Description
AMP-deaminase (AMPD, EC 3. 5. 4. 6), which catalyzes the irreversible hydrolytic deamination of AMP to IMP and ammonia, is an important energy-related enzyme. The partial genomic sequence of the gene encoding myoadenylate deaminase (AMPD1) from the teleost fish Platichthys flesus was determined. The amino acid sequence of P. flesus AMPD1 shows 82% homology with that of the teleost fish Danio rerio. Comparison of genomic sequences of P. flesus and Rattus norvegicus reveals a high degree of conservation of both sequence and structural organization. A phylogenetic analysis of AMPD sequences shows that bony fish and mammalian AMPD1s arise by duplication of a common primordial gene. © 2009 Springer Science+Business Media B.V.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=78149500893&origin=inward; http://dx.doi.org/10.1007/s10695-009-9358-y; http://www.ncbi.nlm.nih.gov/pubmed/19821138; http://link.springer.com/10.1007/s10695-009-9358-y; http://www.springerlink.com/index/10.1007/s10695-009-9358-y; http://www.springerlink.com/index/pdf/10.1007/s10695-009-9358-y
Springer Science and Business Media LLC
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