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  • Tyrosine residue is often a target of biologically interesting posttranslational modifications. Among them, phosphorylation, which plays pivotal roles in regulation of protein activity and thus also in signal transduction pathways, and nitration, which is associated with oxidative stress, are believed to be the most important ones.In the first part of this study we used chemical modification of tyrosine residues of model proteins by tetranitomethane to verify the possibility to detect localization of aromatic groups on the surface of protein globule. The modified tyrosine residues were localized by tryptic cleavage and MALDI-TOF MS. The method for determination of surface tyrosine residues which represent potential targets for posttranslational modifications was developed. Secondly we localized natural occuring posttranslational phosphorylation of plant phospholipase D from Brasica oleracea var capitata. This was performed by comparison of MALDI-TOF MS spectra of tryptic digests of phosphorylated form
  • Tyrosine residue is often a target of biologically interesting posttranslational modifications. Among them, phosphorylation, which plays pivotal roles in regulation of protein activity and thus also in signal transduction pathways, and nitration, which is associated with oxidative stress, are believed to be the most important ones.In the first part of this study we used chemical modification of tyrosine residues of model proteins by tetranitomethane to verify the possibility to detect localization of aromatic groups on the surface of protein globule. The modified tyrosine residues were localized by tryptic cleavage and MALDI-TOF MS. The method for determination of surface tyrosine residues which represent potential targets for posttranslational modifications was developed. Secondly we localized natural occuring posttranslational phosphorylation of plant phospholipase D from Brasica oleracea var capitata. This was performed by comparison of MALDI-TOF MS spectra of tryptic digests of phosphorylated form (en)
  • Studium modifikací tyrosinu pomocí MALDI-TOF MS (cs)
Title
  • Tyrosine Residues Modifications Studied by MALDI-TOF MS
  • Tyrosine Residues Modifications Studied by MALDI-TOF MS (en)
  • Studium modifikací tyrosinu pomocí MALDI-TOF MS (cs)
skos:prefLabel
  • Tyrosine Residues Modifications Studied by MALDI-TOF MS
  • Tyrosine Residues Modifications Studied by MALDI-TOF MS (en)
  • Studium modifikací tyrosinu pomocí MALDI-TOF MS (cs)
skos:notation
  • RIV/60461373:22330/04:00012918!RIV/2005/GA0/223305/N
http://linked.open.../vavai/riv/strany
  • 50
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA203/02/0922), Z(MSM 223300006)
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
  • 591123
http://linked.open...ai/riv/idVysledku
  • RIV/60461373:22330/04:00012918
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • tyrosine phosphorylation (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [FFA7FF23E83C]
http://linked.open...v/mistoKonaniAkce
  • Santa Fe - New Mexico - USA
http://linked.open...i/riv/mistoVydani
  • Santa Fe - New Mexico - USA
http://linked.open...i/riv/nazevZdroje
  • Mass Spectrometry in Systems Biology
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
  • Hynek, Radovan
  • Kodíček, Milan
  • Šantrůček, Jiří
  • Novotná, Zuzana
  • Kadlčík, Vojtěch
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
  • Neuveden
http://localhost/t...ganizacniJednotka
  • 22330
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