This HTML5 document contains 53 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

Namespace Prefixes

PrefixIRI
dctermshttp://purl.org/dc/terms/
n16http://linked.opendata.cz/resource/domain/vavai/vysledek/RIV%2F00216224%3A14310%2F10%3A00057175%21RIV13-GA0-14310___/
n10http://localhost/temp/predkladatel/
n9http://linked.opendata.cz/resource/domain/vavai/riv/tvurce/
n7http://linked.opendata.cz/resource/domain/vavai/projekt/
n17http://linked.opendata.cz/ontology/domain/vavai/
n13http://linked.opendata.cz/resource/domain/vavai/zamer/
shttp://schema.org/
skoshttp://www.w3.org/2004/02/skos/core#
n3http://linked.opendata.cz/ontology/domain/vavai/riv/
n12http://bibframe.org/vocab/
n2http://linked.opendata.cz/resource/domain/vavai/vysledek/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
n4http://linked.opendata.cz/ontology/domain/vavai/riv/klicoveSlovo/
n20http://linked.opendata.cz/ontology/domain/vavai/riv/duvernostUdaju/
xsdhhttp://www.w3.org/2001/XMLSchema#
n15http://linked.opendata.cz/ontology/domain/vavai/riv/aktivita/
n14http://linked.opendata.cz/ontology/domain/vavai/riv/jazykVysledku/
n19http://linked.opendata.cz/ontology/domain/vavai/riv/obor/
n18http://linked.opendata.cz/ontology/domain/vavai/riv/druhVysledku/
n8http://reference.data.gov.uk/id/gregorian-year/

Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F10%3A00057175%21RIV13-GA0-14310___
rdf:type
skos:Concept n17:Vysledek
dcterms:description
The opportunistic pathogen Burkholderia cenocepacia expresses several soluble lectins, among them BC2L-C. This lectin exhibits two domains: a C-terminal domain with high sequence similarity to the recently described calcium-dependent mannose-binding lectin BC2L-A, and an N-terminal domain of 156 amino acids without similarity to any known protein. The recombinant N-terminal BC2L-C domain is a new lectin with specificity for fucosylated human histo-blood group epitopes H-type 1, Lewis b, and Lewis Y, as determined by glycan array and isothermal titration calorimetry. Methylselenofucoside was used as ligand to solve the crystal structure of the N-terminal BC2L-C domain. Additional molecular modeling studies rationalized the preference for Lewis epitopes. The structure reveals a trimeric jellyroll arrangement with striking similarity to TNF-like proteins, and to BclA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs. The opportunistic pathogen Burkholderia cenocepacia expresses several soluble lectins, among them BC2L-C. This lectin exhibits two domains: a C-terminal domain with high sequence similarity to the recently described calcium-dependent mannose-binding lectin BC2L-A, and an N-terminal domain of 156 amino acids without similarity to any known protein. The recombinant N-terminal BC2L-C domain is a new lectin with specificity for fucosylated human histo-blood group epitopes H-type 1, Lewis b, and Lewis Y, as determined by glycan array and isothermal titration calorimetry. Methylselenofucoside was used as ligand to solve the crystal structure of the N-terminal BC2L-C domain. Additional molecular modeling studies rationalized the preference for Lewis epitopes. The structure reveals a trimeric jellyroll arrangement with striking similarity to TNF-like proteins, and to BclA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs.
dcterms:title
A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens
skos:prefLabel
A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens
skos:notation
RIV/00216224:14310/10:00057175!RIV13-GA0-14310___
n3:aktivita
n15:S n15:P n15:Z
n3:aktivity
P(GA303/09/1168), P(GD301/09/H004), P(LC06030), S, Z(MSM0021622413)
n3:cisloPeriodika
1
n3:dodaniDat
n8:2013
n3:domaciTvurceVysledku
n9:5522064 Delia, Monia n9:9907327
n3:druhVysledku
n18:J
n3:duvernostUdaju
n20:S
n3:entitaPredkladatele
n16:predkladatel
n3:idSjednocenehoVysledku
245037
n3:idVysledku
RIV/00216224:14310/10:00057175
n3:jazykVysledku
n14:eng
n3:klicovaSlova
lectin; Burkholderia cenocepacia; pathogen; TNF
n3:klicoveSlovo
n4:lectin n4:pathogen n4:Burkholderia%20cenocepacia n4:TNF
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[9EB39E2574DA]
n3:nazevZdroje
Structure
n3:obor
n19:CD
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
7
n3:projekt
n7:GD301%2F09%2FH004 n7:LC06030 n7:GA303%2F09%2F1168
n3:rokUplatneniVysledku
n8:2010
n3:svazekPeriodika
18
n3:tvurceVysledku
Šulák, Ondřej Delia, Monia Wimmerová, Michaela Cioci, Gianluca Lahmann, Martina Imberty, Anne Varrot, Annabelle
n3:wos
000273859700010
n3:zamer
n13:MSM0021622413
s:issn
0969-2126
s:numberOfPages
14
n12:doi
10.1016/j.str.2009.10.021
n10:organizacniJednotka
14310