Analysis of bacterial glycoproteins

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F11%3A00002453" target="_blank" >RIV/60162694:G44__/11:00002453 - isvavai.cz</a>
Result on the web
<a href="http://www.wiley-vch.de/publish/en/books/newTitles201109/3-527-32780-0/?sID=1ii6ulo4deirvu13ilgcs6nmi7" target="_blank" >http://www.wiley-vch.de/publish/en/books/newTitles201109/3-527-32780-0/?sID=1ii6ulo4deirvu13ilgcs6nmi7</a>
DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Analysis of bacterial glycoproteins
Original language description
Glycosylation, together with phosphorylation, represent the most common post-translational modifications of proteins. Over 50% of today's known proteins, as well as 80% of membrane proteins, are estimated to be modified with glycans. The commonly-accepted theory limited the ability of organisms to glycosylate their proteins to eukaryotes. This false conclusion originated from the fact that the most frequently studied prokaryotes, such as Escherichia coli, Bacillus subtilis, and Salmonella species were identified as nonglycosylated]. However, advances in analytical technologies and genome sequencing enabled the discovery of glycosylation in prokaryotes, such as bacteria. To date, a noticeable number of membrane-associated, surface-associated, exoenzymes, and even secreted glycoproteins from diverse bacterial species have been characterized.
Czech name
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Czech description
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Project
<a href="/en/project/ME08105" target="_blank" >ME08105: Differential proteome analysis of bacterial Francisella tularensis glyco- and phospho- proteins</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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