Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites - Wikidata - wikimedia - TriplyDB

Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites

Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites

http://www.wikidata.org/entity/Q34518030

about

DLC-1: a Rho GTPase-activating protein and tumour suppressor The tumor suppressor Mst1 promotes changes in the cellular redox state by phosphorylation and inactivation of peroxiredoxin-1 protein Large-scale proteomics and phosphoproteomics of urinary exosomes Regulation of renal urea transport by vasopressin Large-scale phosphoproteomic analysis of membrane proteins in renal proximal and distal tubule Methods and approaches for the comprehensive characterization and quantification of cellular proteomes using mass spectrometry The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular Diseases A Minireview on Vasopressin-regulated Aquaporin-2 in Kidney Collecting Duct Cells A novel therapeutic effect of statins on nephrogenic diabetes insipidus Regulation of nephron water and electrolyte transport by adenylyl cyclases Cherry Valley Ducks Mitochondrial Antiviral-Signaling Protein-Mediated Signaling Pathway and Antiviral Activity Research Structure and permeation mechanism of a mammalian urea transporter.Mass spectrometry of membrane proteins: a focus on aquaporins.Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating Dynactin's pointed-end complex is a cargo-targeting module Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry A fluorimetry-based ssYFP secretion assay to monitor vasopressin-induced exocytosis in LLC-PK1 cells expressing aquaporin-2.An Efficient Dynamic Programming Algorithm for Phosphorylation Site Assignment of Large-Scale Mass Spectrometry Data.Exploiting Thread-Level and Instruction-Level Parallelism to Cluster Mass Spectrometry Data using Multicore Architectures.MS-REDUCE: an ultrafast technique for reduction of big mass spectrometry data for high-throughput processing.PhosphoScore: an open-source phosphorylation site assignment tool for MSn data.Proteomics in renal research.Integrated platform for manual and high-throughput statistical validation of tandem mass spectra.Phosphorylation of aquaporin-2 regulates its endocytosis and protein-protein interactions.Strategies for quantitation of phosphoproteomic data.Signal integration and gene induction by a functionally distinct STAT3 phosphoform.Phosphoproteomics for the masses Novel Ser/Thr protein phosphatase 5 (PP5) regulated targets during DNA damage identified by proteomics analysis.Proteomic profiling of nuclei from native renal inner medullary collecting duct cells using LC-MS/MS Phosphoproteomic profiling reveals vasopressin-regulated phosphorylation sites in collecting duct Expression of transporters involved in urine concentration recovers differently after cessation of lithium treatment.Quantitative phosphoproteomic analysis reveals vasopressin V2-receptor-dependent signaling pathways in renal collecting duct cells.Quantitative analysis of aquaporin-2 phosphorylation.Phosphorylation of UT-A1 on serine 486 correlates with membrane accumulation and urea transport activity in both rat IMCDs and cultured cells Phosphoproteomic analysis reveals regulatory mechanisms at the kidney filtration barrier Use of LC-MS/MS and Bayes' theorem to identify protein kinases that phosphorylate aquaporin-2 at Ser256.Sensing, signaling and sorting events in kidney epithelial cell physiology.Monitoring single-channel water permeability in polarized cells.Dynamics of the G protein-coupled vasopressin V2 receptor signaling network revealed by quantitative phosphoproteomics.

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P2860

Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites

http://www.wikidata.org/entity/Q34518030

description

2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006 թվականի ապրիլին հրատարակված գիտական հոդված

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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name

Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

@ast

Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

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Quantitative phosphoproteomics ...... 2 phosphorylation at two sites

@en

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Guanghui Wang

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Jason D Hoffert

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Mark A Knepper

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Rong-Fong Shen

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P2860

Large-scale characterization of HeLa cell nuclear phosphoproteins

Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein

Phospho.ELM: a database of experimentally verified phosphorylation sites in eukaryotic proteins

Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase

Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases

Development of human protein reference database as an initial platform for approaching systems biology in humans

Identification and characterization of phosphorylated proteins in the human pituitary

Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)

Cellular localization of type 5 and type 6 ACs in collecting duct and regulation of cAMP synthesis

Identification of a multiprotein "motor" complex binding to water channel aquaporin-2

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Trairak Pisitkun

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phosphorylation

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1459033

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