About: Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
Description
  • Mycobacterium tuberculosis is a pathogen that is resistant to most common antibiotics and chemotherapeutic agents. This resistance is related to an unusual and well-organized structure of the mycobacterial cell wall that shows an abnormally low degree of the hydrophilic permeability. Outer cell wall contains the biochemically unique structures of sugar residues, constituents of various branched and complex polysaccharides and glycolipids . There is very little knowledge about the biosynthesis pathways of these glycoconjugates and about the enzymes, especially glycosyltransferases (GT), involved. The genome of M. tuberculosis contains 3,951 protein-coding sequences. Putative function annotation of some of them was predicted using a combination of sequence alignment and motif comparison . Using this approach, only a small number of putative GTs was identified. Recent crystal structure determination of GTs demonstrated that they adopt only a limited number of topology . We focused on 3D-topology identifi
  • Mycobacterium tuberculosis is a pathogen that is resistant to most common antibiotics and chemotherapeutic agents. This resistance is related to an unusual and well-organized structure of the mycobacterial cell wall that shows an abnormally low degree of the hydrophilic permeability. Outer cell wall contains the biochemically unique structures of sugar residues, constituents of various branched and complex polysaccharides and glycolipids . There is very little knowledge about the biosynthesis pathways of these glycoconjugates and about the enzymes, especially glycosyltransferases (GT), involved. The genome of M. tuberculosis contains 3,951 protein-coding sequences. Putative function annotation of some of them was predicted using a combination of sequence alignment and motif comparison . Using this approach, only a small number of putative GTs was identified. Recent crystal structure determination of GTs demonstrated that they adopt only a limited number of topology . We focused on 3D-topology identifi (en)
  • Mycobacterium tuberculosis is a pathogen that is resistant to most common antibiotics and chemotherapeutic agents. This resistance is related to an unusual and well-organized structure of the mycobacterial cell wall that shows an abnormally low degree of the hydrophilic permeability. Outer cell wall contains the biochemically unique structures of sugar residues, constituents of various branched and complex polysaccharides and glycolipids . There is very little knowledge about the biosynthesis pathways of these glycoconjugates and about the enzymes, especially glycosyltransferases (GT), involved. The genome of M. tuberculosis contains 3,951 protein-coding sequences. Putative function annotation of some of them was predicted using a combination of sequence alignment and motif comparison . Using this approach, only a small number of putative GTs was identified. Recent crystal structure determination of GTs demonstrated that they adopt only a limited number of topology . We focused on 3D-topology identifi (cs)
Title
  • Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome
  • Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome (en)
  • Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome (cs)
skos:prefLabel
  • Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome
  • Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome (en)
  • Mycobacterial glycosyltransferases: fold recognition analysis of the Mycobacterium tuberculosis genome (cs)
skos:notation
  • RIV/00216224:14310/02:00007110!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany
  • 65
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LN00A016)
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
  • 654716
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/02:00007110
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • threading; glycosyltransferase; mycobacterium tuberculosis (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [842B0666E0DB]
http://linked.open...v/mistoKonaniAkce
  • May 20 - 24, Albe, France
http://linked.open...i/riv/mistoVydani
  • France
http://linked.open...i/riv/nazevZdroje
  • XIXčmes Journées de Chimie et Biochimie des Glucides
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Imberty, Anne
  • Wimmerová, Michaela
  • Bettler, Emmanuel
http://linked.open...vavai/riv/typAkce
http://linked.open.../riv/zahajeniAkce
number of pages
http://purl.org/ne...btex#hasPublisher
  • Societe francaise de Chimie
http://localhost/t...ganizacniJednotka
  • 14310
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 58 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software