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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F04%3A00012918%21RIV%2F2005%2FGA0%2F223305%2FN
rdf:type
skos:Concept n17:Vysledek
dcterms:description
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 Studium modifikací tyrosinu pomocí MALDI-TOF MS
dcterms:title
Tyrosine Residues Modifications Studied by MALDI-TOF MS Studium modifikací tyrosinu pomocí MALDI-TOF MS Tyrosine Residues Modifications Studied by MALDI-TOF MS
skos:prefLabel
Studium modifikací tyrosinu pomocí MALDI-TOF MS Tyrosine Residues Modifications Studied by MALDI-TOF MS Tyrosine Residues Modifications Studied by MALDI-TOF MS
skos:notation
RIV/60461373:22330/04:00012918!RIV/2005/GA0/223305/N
n4:strany
50
n4:aktivita
n9:P n9:Z
n4:aktivity
P(GA203/02/0922), Z(MSM 223300006)
n4:dodaniDat
n14:2005
n4:domaciTvurceVysledku
n5:6936903 n5:1120530 n5:9046976 n5:9724486 n5:7333129
n4:druhVysledku
n11:D
n4:duvernostUdaju
n19:S
n4:entitaPredkladatele
n10:predkladatel
n4:idSjednocenehoVysledku
591123
n4:idVysledku
RIV/60461373:22330/04:00012918
n4:jazykVysledku
n13:eng
n4:klicovaSlova
tyrosine phosphorylation
n4:klicoveSlovo
n20:tyrosine%20phosphorylation
n4:kontrolniKodProRIV
[FFA7FF23E83C]
n4:mistoKonaniAkce
Santa Fe - New Mexico - USA
n4:mistoVydani
Santa Fe - New Mexico - USA
n4:nazevZdroje
Mass Spectrometry in Systems Biology
n4:obor
n18:CE
n4:pocetDomacichTvurcuVysledku
5
n4:pocetTvurcuVysledku
5
n4:projekt
n12:GA203%2F02%2F0922
n4:rokUplatneniVysledku
n14:2004
n4:tvurceVysledku
Novotná, Zuzana Kadlčík, Vojtěch Kodíček, Milan Hynek, Radovan Šantrůček, Jiří
n4:typAkce
n16:WRD
n4:zahajeniAkce
2004-02-14+01:00
n4:zamer
n21:MSM%20223300006
s:numberOfPages
1
n7:hasPublisher
Neuveden
n15:organizacniJednotka
22330