Detection of the key enzyme of alginate biosynthesis in Vibrio sp. QY102
World Journal of Microbiology and Biotechnology, ISSN: 0959-3993, Vol: 24, Issue: 8, Page: 1613-1615
2008
- 3Citations
- 6Captures
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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.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Article Description
Alginate is an important component of biofilms of many pathogens, but its presence in Vibrio has not been reported. The GDP-mannose dehydrogenase gene (algD), which is the kinetic control point in alginate biosynthesis, was cloned for the first time from Vibrio species using degenerated PCR and inverse PCR. Sequence analysis showed that algD was also localized in an alginate biosynthesis cluster, as it is in Pseudomonas aeruginosa. In addition, the existence of mannuronic acid, a component of alginate, was supported by the NMR spectrum of Vibrio sp. QY102 exopolysaccharide. © 2007 Springer Science+Business Media B.V.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=45849148126&origin=inward; http://dx.doi.org/10.1007/s11274-007-9632-z; http://link.springer.com/10.1007/s11274-007-9632-z; http://link.springer.com/content/pdf/10.1007/s11274-007-9632-z; http://link.springer.com/content/pdf/10.1007/s11274-007-9632-z.pdf; http://link.springer.com/article/10.1007/s11274-007-9632-z/fulltext.html; https://dx.doi.org/10.1007/s11274-007-9632-z; https://link.springer.com/article/10.1007/s11274-007-9632-z; http://www.springerlink.com/index/10.1007/s11274-007-9632-z; http://www.springerlink.com/index/pdf/10.1007/s11274-007-9632-z
Springer Science and Business Media LLC
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