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| Description
| - Biologické systémy jsou kontrolovány proteinovými komplexy, které vytvářejí dynamickou interakční síť. Popisujeme strategii, která je schopná analyzovat proteinové komplexy pomocí propojení kvantitavivní hmotnostní spektrometrie bez použití izotopických značek a počítačové analýzy. Porovnáním intensity peptidových profilů mezi vzorky s postupným ředěním, tzv. MasterMap systém je schopen identifikovat specificky interagující proteiny, zaznamenat změny ve složení proteinových komplexů a odhalit variace ve stavu fosforylace jednotlivých komponent. Použili jsme komplex obsahující lidský transkripční faktor FoxO3A, abychom doložili spolehlivost a použitelnost této technologie. Identifikovali jsme známé i neznámé interakce FoxO3A s 14-3-3 proteiny, navíc jsme identifikovali fosforylační místa FoxO3A a detekovali navízanou redukovanou formu 14-3-3 po inhibici fosfoinositide-3 kinázou. MasterMap systém posouvá několik limitujících faktorů současných přístupů analýzy proteinových komplexů pomocí lepší specific (cs)
- Biological systems are controlled by protein complexes that associate into dynamic protein interaction networks. We describe a strategy that analyzes protein complexes through the integration of label-free, quantitative mass spectrometry and computational analysis. By evaluating peptide intensity profiles throughout the sequential dilution of samples, the MasterMap system identifies specific interaction partners, detects changes in the composition of protein complexes and reveals variations in the phosphorylation states of components of protein complexes. We use the complexes containing the human forkhead transcription factor FoxO3A to demonstrate the validity and performance of this technology. Our analysis identifies previously known and unknown interactions of FoxO3A with 14-3-3 proteins, in addition to identifying FoxO3A phosphorylation sites and detecting reduced 14-3-3 binding following inhibition of phosphoinositide-3 kinase. By improving specificity and sensitivity of interaction networks, ass
- Biological systems are controlled by protein complexes that associate into dynamic protein interaction networks. We describe a strategy that analyzes protein complexes through the integration of label-free, quantitative mass spectrometry and computational analysis. By evaluating peptide intensity profiles throughout the sequential dilution of samples, the MasterMap system identifies specific interaction partners, detects changes in the composition of protein complexes and reveals variations in the phosphorylation states of components of protein complexes. We use the complexes containing the human forkhead transcription factor FoxO3A to demonstrate the validity and performance of this technology. Our analysis identifies previously known and unknown interactions of FoxO3A with 14-3-3 proteins, in addition to identifying FoxO3A phosphorylation sites and detecting reduced 14-3-3 binding following inhibition of phosphoinositide-3 kinase. By improving specificity and sensitivity of interaction networks, ass (en)
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| Title
| - Integrovaný přístup kombinující hmotnostní spektrometrii a výpočty pro analýzu proteinových interakčních sítí (cs)
- An integrated mass spectrometric and computational framework for the analysis of protein interaction networks
- An integrated mass spectrometric and computational framework for the analysis of protein interaction networks (en)
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| skos:prefLabel
| - Integrovaný přístup kombinující hmotnostní spektrometrii a výpočty pro analýzu proteinových interakčních sítí (cs)
- An integrated mass spectrometric and computational framework for the analysis of protein interaction networks
- An integrated mass spectrometric and computational framework for the analysis of protein interaction networks (en)
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| skos:notation
| - RIV/60162694:G44__/07:00001756!RIV08-MO0-G44_____
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/60162694:G44__/07:00001756
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - 14-3-3 Proteins; Algorithms; Chromatography, Liquid; Forkhead Transcription Factors; Internet; Mass Spectrometry; Phosphorylation; Protein Interaction Mapping; Protein Processing, Post-Translational; Proteome; Proteomics; Sensitivity and Specificity (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
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| http://linked.open...in/vavai/riv/obor
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| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
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| http://linked.open...vavai/riv/projekt
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| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Hubálek, Martin
- Aebersold, Ruedi
- Gstaiger, Matthias
- Muller, Marcus
- Müller, Lucas N.
- Rinner, Oliver
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| issn
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| number of pages
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| http://localhost/t...ganizacniJednotka
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