Phosphat Goes Kinases–Searchable Protein Kinase Target
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To date, we have researched more than 4450 kinase-related publications, which collectively contain information on about 289 kinases. Users can now query the PhosPhAt Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt.
Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases – Searchable protein kinase target information in the plant phosphorylation site database Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases—searchable protein kinase target information in the plant phos-phorylation site database PhosPhAt. PhosPhAt goes kinases–searchable protein kinase target information in the plant phosphorylation site database PhosPhAt.
Xu Na Wu Editor Plant Phospho- proteomics

PhosPhAt goes kinases – Searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Article Full-text available Nov 2012 Monika Zulawski Zulawski, M., Braginets, R. and Schulze, W.X. (2013) PhosPhAt Goes Kinases Searchable Protein Kinase Target Information in the Plant Phosphorylation Site Database PhosPhAt. Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases – searchable protein kinase target information in the plant phosphorylation site database PhosPhAt.
Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt. ABSTRACT Reversible phosphorylation is a key mechanism for regulating protein function. Thus it is of high interest to know which kinase can phosphorylate which proteins. Comprehensive
Organization: University of Hohenheim Startpage University Organizational ChartPublications: Plant Systems Biology
- Publications: Plant Systems Biology
- Databases for Plant Phosphoproteomics
- doi: 10.1007/978-1-0716-1625-3_1
- Phosphorylation Site Prediction in Plants
Zulawski M., Braginets R., Schulze W.X. (2013) PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt. PhosPhAt goes kinases – Searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Article Full-text available Nov 2012 Monika Zulawski AMP-activated protein kinase in rat [62]. In plants, coupling with phosphorylation, the activation of kinases resulted in confor-matio al changes in the kinase domain [22, 63]. The idea of such
Zulawski, Monika (2013): Die Rolle der Phosphorylierung in der Regulation pflanzlicher Proteine. Zulawski, Monika ; Braginets, Rostyslav ; Schulze, Waltraud X. (2013): PhosPhAt goes kinases Zulawski, M., Braginets, R. and Schulze, W.X. (2013) PhosPhAt Goes Kinases Searchable Protein Kinase Target Information in the Plant Phosphorylation Site Database PhosPhAt. Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases – Searchable protein kinase target information in the plant phosphorylation site database
Publikationen: Systembiologie der Pflanze
Sci-Hub | PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt. Nucleic Acids Research, 41 (D1), D1176–D1184 | Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases-searchable protein kinase target information in the plant phosphorylation site database PhosPhAt. PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Monika Zulawski, Rostyslav Braginets, and Waltraud
Mitogen-activated protein kinases are eukaryotic kinases that form cascades for intracellular transmission of extracellular stimuli and are classified into three main groups. The MAPK To date, we have researched more than 4450 kinase-related publications, which collectively contain information on about 289 kinases. Users can now query the PhosPhAt database not
To date, we have researched more than 4450 kinase-related publications, which collectively contain information on about 289 kinases. Users can now query the PhosPhAt database not In addition to the experimentally determined and predicted phosphorylation sites of a given protein on the protein summary page, information is also provided about any
PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Monika ZulawskiRostyslav BraginetsW. Schulze
PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Monika Zulawski, Rostyslav Braginets, and Waltraud ABSTRACT Reversible phosphorylation is a key mechanism for regulating protein function. Thus it is of high interest to know which kinase can phosphorylate which proteins. Comprehensive Publications that cite this publication Thirty years of molecular dynamics simulations on posttranslational modifications of proteins
PhosPhAt goes kinases–searchable protein kinase target information in the plant phosphorylation site database PhosPhAt. Zulawski M, Braginets R, Schulze WX Nucleic Acids PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Monika To date, we have researched more than 4450 kinase-related publications, which collectively contain information on about 289 kinases. Users can now query the PhosPhAt database not
Publications: Plant Systems Biology:
ABSTRACT Reversible phosphorylation is a key mechanism for regulating protein function. Thus it is of high interest to know which kinase can phosphorylate which proteins. Comprehensive Zulawski M, Braginets R, Schulze WX (2013) PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt.
PhosPhAt goes kinases—searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Monika Zulawski Rostyslav Braginets W. Schulze
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