Quantitative protein and mRNA profiling shows selective post-transcriptional control of protein expression by vasopressin in kidney cells. - Wikidata - wikimedia - TriplyDB

Quantitative protein and mRNA profiling shows selective post-transcriptional control of protein expression by vasopressin in kidney cells.

Quantitative protein and mRNA profiling shows selective post-transcriptional control of protein expression by vasopressin in kidney cells.

http://www.wikidata.org/entity/Q34454965

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G protein-coupled receptors in the hypothalamic paraventricular and supraoptic nuclei--serpentine gateways to neuroendocrine homeostasis Global analysis of the effects of the V2 receptor antagonist satavaptan on protein phosphorylation in collecting duct Proteomic profiling of the effect of metabolic acidosis on the apical membrane of the proximal convoluted tubule.Endothelin-Mediated Changes in Gene Expression in Isolated Purified Rat Retinal Ganglion Cells Quantitative apical membrane proteomics reveals vasopressin-induced actin dynamics in collecting duct cells Duplication in the microtubule-actin cross-linking factor 1 gene causes a novel neuromuscular condition.Leveraging the complementary nature of RNA-Seq and shotgun proteomics data.Use of LC-MS/MS and Bayes' theorem to identify protein kinases that phosphorylate aquaporin-2 at Ser256.Increased neuronal expression of neurokinin-1 receptor and stimulus-evoked internalization of the receptor in the rostral ventromedial medulla of the rat after peripheral inflammatory injury.Increased astrocyte expression of IL-6 or CCL2 in transgenic mice alters levels of hippocampal and cerebellar proteins.A knowledge base of vasopressin actions in the kidney.Characterization of functional reprogramming during osteoclast development using quantitative proteomics and mRNA profiling.Aquaporin-2 regulation in health and disease.Changes in the disposition of substance P in the rostral ventromedial medulla after inflammatory injury in the rat.A Systems Level Analysis of Vasopressin-mediated Signaling Networks in Kidney Distal Convoluted Tubule Cells.Quantitative proteomics identifies vasopressin-responsive nuclear proteins in collecting duct cells.Deep proteomic profiling of vasopressin-sensitive collecting duct cells. II. Bioinformatic analysis of vasopressin signaling.Deep proteomic profiling of vasopressin-sensitive collecting duct cells. I. Virtual Western blots and molecular weight distributions.Phosphorylation of claudin-2 on serine 208 promotes membrane retention and reduces trafficking to lysosomes Proteomic profiling of nuclear fractions from native renal inner medullary collecting duct cells.Adverse Outcomes Associated with Cigarette Smoke Radicals Related to Damage to Protein-disulfide Isomerase Application of systems biology principles to protein biomarker discovery: urinary exosomal proteome in renal transplantation.Proteome-wide measurement of protein half-lives and translation rates in vasopressin-sensitive collecting duct cells Systems-level analysis reveals selective regulation of Aqp2 gene expression by vasopressin Molecular biology of water and salt regulation in the kidney.The application of quantification techniques in proteomics for biomedical research.Integrative Omics Analysis Reveals Post-Transcriptionally Enhanced Protective Host Response in Colorectal Cancers with Microsatellite Instability.Identification of β-catenin-interacting proteins in nuclear fractions of native rat collecting duct cells.From 20th century metabolic wall charts to 21st century systems biology: database of mammalian metabolic enzymes.Single-tubule RNA-Seq uncovers signaling mechanisms that defend against hyponatremia in SIADH.Systems-level identification of PKA-dependent signaling in epithelial cells.Water transport running deep. Focus on "Deep proteomic profiling of vasopressin-sensitive collecting duct cells".Arkadia protein expression is reduced in the liver during the progression of hepatic fibrosis.Vasopressin-induced serine 269 phosphorylation reduces Sipa1l1 (signal-induced proliferation-associated 1 like 1)-mediated aquaporin-2 endocytosis.

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Quantitative protein and mRNA profiling shows selective post-transcriptional control of protein expression by vasopressin in kidney cells.

http://www.wikidata.org/entity/Q34454965

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Quantitative protein and mRNA ...... y vasopressin in kidney cells.

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Quantitative protein and mRNA ...... y vasopressin in kidney cells.

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Quantitative protein and mRNA ...... y vasopressin in kidney cells.

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type

label

Quantitative protein and mRNA ...... y vasopressin in kidney cells.

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Quantitative protein and mRNA ...... y vasopressin in kidney cells.

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Quantitative protein and mRNA ...... y vasopressin in kidney cells.

@nl

prefLabel

Quantitative protein and mRNA ...... y vasopressin in kidney cells.

@ast

Quantitative protein and mRNA ...... y vasopressin in kidney cells.

@en

Quantitative protein and mRNA ...... y vasopressin in kidney cells.

@nl

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Molecular & Cellular Proteomics

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Quantitative protein and mRNA ...... by vasopressin in kidney cells

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Dane H Slentz

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Guanghui Wang

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Jason D Hoffert

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Mark A Knepper

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Sookkasem Khositseth

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P2860

Identification and proteomic profiling of exosomes in human urine

Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals

Large-scale proteomics and phosphoproteomics of urinary exosomes

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

Correlation between protein and mRNA abundance in yeast

Open mass spectrometry search algorithm

Non-muscle myosin II and myosin light chain kinase are downstream targets for vasopressin signaling in the renal collecting duct

Reciprocal interaction with G-actin and tropomyosin is essential for aquaporin-2 trafficking

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M110.004036

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