About: PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria     Goto   Sponge   NotDistinct   Permalink

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  • Enormous potential of sugar structures gives them a crucial importance in recognition and signalling events. Carbohydrate-mediated recognition plays an important role in the ability of parasitic organisms to adhere to the surface of the host cell in the first step of their invasion and infectivity. For example, Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1,2]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. This characteristics is correlated to the remarkable presence of two calcium ions in the binding site of the protein [3]. Database searching in newly sequenced bacterial genomes revealed the presence of PA-IIL like proteins within a limited number of other opportunistic pathogens. All of them are soil inhabitants, are phylogenetically related and in past
  • Enormous potential of sugar structures gives them a crucial importance in recognition and signalling events. Carbohydrate-mediated recognition plays an important role in the ability of parasitic organisms to adhere to the surface of the host cell in the first step of their invasion and infectivity. For example, Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1,2]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. This characteristics is correlated to the remarkable presence of two calcium ions in the binding site of the protein [3]. Database searching in newly sequenced bacterial genomes revealed the presence of PA-IIL like proteins within a limited number of other opportunistic pathogens. All of them are soil inhabitants, are phylogenetically related and in past (en)
  • Enormous potential of sugar structures gives them a crucial importance in recognition and signalling events. Carbohydrate-mediated recognition plays an important role in the ability of parasitic organisms to adhere to the surface of the host cell in the first step of their invasion and infectivity. For example, Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients [1,2]. Moreover, the PA-IIL lectin displays an affinity for fucose in micromolar range, unusually high for monosaccharide binding. This characteristics is correlated to the remarkable presence of two calcium ions in the binding site of the protein [3]. Database searching in newly sequenced bacterial genomes revealed the presence of PA-IIL like proteins within a limited number of other opportunistic pathogens. All of them are soil inhabitants, are phylogenetically related and in past (cs)
Title
  • PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria
  • PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria (en)
  • PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria (cs)
skos:prefLabel
  • PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria
  • PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria (en)
  • PA-IIL like lectins: a common feature of high adaptability of some opportunistic bacteria (cs)
skos:notation
  • RIV/00216224:14310/04:00021355!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany
  • 72-73
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM 143100005)
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 578736
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/04:00021355
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • lectin; pathogen; saccharide (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [F38BE484EF9D]
http://linked.open...v/mistoKonaniAkce
  • Olomouc
http://linked.open...i/riv/mistoVydani
  • Olomouc
http://linked.open...i/riv/nazevZdroje
  • Chemica 43S
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Cioci, Gianluca
  • Imberty, Anne
  • Kostlánová, Nikola
  • Pokorná, Martina
  • Wimmerová, Michaela
  • Gilboa-Garber, Nechama
  • Mitchell, Edward P.
  • Sabin, Charles
  • Perret, Stephanie
http://linked.open...vavai/riv/typAkce
http://linked.open.../riv/zahajeniAkce
http://linked.open...n/vavai/riv/zamer
number of pages
http://purl.org/ne...btex#hasPublisher
  • Ceska spolecnost pro biochemii a molekularni biologii
https://schema.org/isbn
  • 80-244-0882-1
http://localhost/t...ganizacniJednotka
  • 14310
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