Analysis of bacterial glycoproteins

Kód výsledku v 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>

Výsledek na webu

<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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Jazyk výsledku

angličtina

Název v původním jazyce

Analysis of bacterial glycoproteins

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Analysis of bacterial glycoproteins

Popis výsledku anglicky

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.

Druh

C - Kapitola v odborné knize

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/ME08105" target="_blank" >ME08105: Diferenciální proteomová analýza glyko- a fosfo- proteinů bakterie Francisella tularensis</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název knihy nebo sborníku

BSL3 and BSL4 agents

ISBN

978-3-527-32780-5

Počet stran výsledku

12

Strana od-do

67-78

Počet stran knihy

236

Název nakladatele

Wiley (Weinheim)

Místo vydání

Weinheim

Kód UT WoS kapitoly

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