Identifying protein kinase target preferences using mass spectrometry.
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Letter to the editor: "Systems biology versus reductionism in cell physiology"The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular DiseasesGlobal analysis of the effects of the V2 receptor antagonist satavaptan on protein phosphorylation in collecting ductVasopressin-2 receptor signaling and autosomal dominant polycystic kidney disease: from bench to bedside and back again.Use of LC-MS/MS and Bayes' theorem to identify protein kinases that phosphorylate aquaporin-2 at Ser256.A knowledge base of vasopressin actions in the kidney.Using bacteria to determine protein kinase specificity and predict target substratesRapid Identification of Protein Kinase Phosphorylation Site Motifs Using Combinatorial Peptide LibrariesA Systems Level Analysis of Vasopressin-mediated Signaling Networks in Kidney Distal Convoluted Tubule Cells.A machine learning strategy for predicting localization of post-translational modification sites in protein-protein interacting regionsQuantitative phosphoproteomics in nuclei of vasopressin-sensitive renal collecting duct cellsExploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomicsSystems biology in physiology: the vasopressin signaling network in kidney.Vasopressin and the regulation of aquaporin-2Proteome-wide measurement of protein half-lives and translation rates in vasopressin-sensitive collecting duct cellsCaMKII Phosphorylation of Na(V)1.5: Novel in Vitro Sites Identified by Mass Spectrometry and Reduced S516 Phosphorylation in Human Heart Failure.The DAP-kinase interactome.Regulation of renal Na-(K)-Cl cotransporters by vasopressin.Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners.Systems-level identification of PKA-dependent signaling in epithelial cells.Combined 15N-Labeling and TandemMOAC Quantifies Phosphorylation of MAP Kinase Substrates Downstream of MKK7 in Arabidopsis.
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Identifying protein kinase target preferences using mass spectrometry.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 20 June 2012
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Identifying protein kinase target preferences using mass spectrometry.
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Identifying protein kinase target preferences using mass spectrometry.
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type
label
Identifying protein kinase target preferences using mass spectrometry.
@en
Identifying protein kinase target preferences using mass spectrometry.
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prefLabel
Identifying protein kinase target preferences using mass spectrometry.
@en
Identifying protein kinase target preferences using mass spectrometry.
@nl
P2093
P2860
P1476
Identifying protein kinase target preferences using mass spectrometry.
@en
P2093
Davis Bradford
Fahad Saeed
Jacqueline Douglass
Jason D Hoffert
Mark A Knepper
Peter J Steinbach
Ruwan Gunaratne
Trairak Pisitkun
P2860
P304
P356
10.1152/AJPCELL.00166.2012
P577
2012-06-20T00:00:00Z