Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin. - Wikidata - awgldk - TriplyDB

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

http://www.wikidata.org/entity/Q36498539

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Regulation of renal urea transport by vasopressin The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular Diseases X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating 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 Phosphorylation of aquaporin-2 regulates its endocytosis and protein-protein interactions.Phosphoproteomic profiling reveals vasopressin-regulated phosphorylation sites in collecting duct Sensing, signaling and sorting events in kidney epithelial cell physiology.A protein kinase A-independent pathway controlling aquaporin 2 trafficking as a possible cause for the syndrome of inappropriate antidiuresis associated with polycystic kidney disease 1 haploinsufficiency Adenylate cyclase 6 determines cAMP formation and aquaporin-2 phosphorylation and trafficking in inner medulla.Adaptive evolution of the osmoregulation-related genes in cetaceans during secondary aquatic adaptation Bilateral ureteral obstruction induces early downregulation and redistribution of AQP2 and phosphorylated AQP2.Vasopressin-independent targeting of aquaporin-2 by selective E-prostanoid receptor agonists alleviates nephrogenic diabetes insipidus.pH-dependent regulation of the α-subunit of H+-K+-ATPase (HKα2).Anthrax edema toxin impairs clearance in mice.Opposing Effects of cAMP and T259 Phosphorylation on Plasma Membrane Diffusion of the Water Channel Aquaporin-5 in Madin-Darby Canine Kidney Cells Rapid aquaporin translocation regulates cellular water flow: mechanism of hypotonicity-induced subcellular localization of aquaporin 1 water channel.Characterization of the putative phosphorylation sites of the AQP2 C terminus and their role in AQP2 trafficking in LLC-PK1 cells.Autophagic degradation of aquaporin-2 is an early event in hypokalemia-induced nephrogenic diabetes insipidus Deep proteomic profiling of vasopressin-sensitive collecting duct cells. II. Bioinformatic analysis of vasopressin signaling.Regulation of aquaporin-2 in the kidney: A molecular mechanism of body-water homeostasis.Regulation of the Water Channel Aquaporin-2 via 14-3-3θ and -ζ The phosphorylation state of serine 256 is dominant over that of serine 261 in the regulation of AQP2 trafficking in renal epithelial cells.Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2.Large-scale quantitative LC-MS/MS analysis of detergent-resistant membrane proteins from rat renal collecting duct.Urine concentrating and diluting ability during aging.Acute hypertonicity alters aquaporin-2 trafficking and induces a MAPK-dependent accumulation at the plasma membrane of renal epithelial cells.LC-MS/MS analysis of differential centrifugation fractions from native inner medullary collecting duct of rat Metformin improves urine concentration in rodents with nephrogenic diabetes insipidus.Phosphorylation events and the modulation of aquaporin 2 cell surface expression Vasopressin and the regulation of aquaporin-2 Localization and trafficking of aquaporin 2 in the kidney.The physiology of urinary concentration: an update.AQP2 Plasma Membrane Diffusion Is Altered by the Degree of AQP2-S256 Phosphorylation.Urinary concentration and dilution in the aging kidney.Regulation of the water channel aquaporin-2 by posttranslational modification.Mechanisms of cell polarity and aquaporin sorting in the nephron.Cell culture models and animal models for studying the patho-physiological role of renal aquaporins.Molecular physiology of the medullary collecting duct.

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P2860

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

http://www.wikidata.org/entity/Q36498539

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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2008年學術文章

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2008年學術文章

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name

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

@ast

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

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type

label

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

@ast

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

@en

prefLabel

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

@ast

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Acute regulation of aquaporin-2 phosphorylation at Ser-264 by vasopressin.

@en

P2093

Hanne B Moeller

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Jason D Hoffert

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Mark A Knepper

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Ming-Jiun Yu

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Robert A Fenton

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Søren Nielsen

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P2860

Identification and proteomic profiling of exosomes in human urine

The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers.

Heat shock protein 70 interacts with aquaporin-2 and regulates its trafficking

Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells

Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel

Aquaporins in the kidney: from molecules to medicine.

Severe urinary concentrating defect in renal collecting duct-selective AQP2 conditional-knockout mice.

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

Congenital progressive hydronephrosis (cph) is caused by an S256L mutation in aquaporin-2 that affects its phosphorylation and apical membrane accumulation.

Organization of vesicular trafficking in epithelia.

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phosphorylation

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