LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation. - Wikidata - wikimedia - TriplyDB

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

http://www.wikidata.org/entity/Q43133843

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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 Binding to any ESCRT can mediate ubiquitin-independent cargo sorting Phosphorylation of aquaporin-2 regulates its endocytosis and protein-protein interactions.Ubiquitination of aquaporin-2 in the kidney.Aquaporin-2 in the "-omics" era Lithium causes G2 arrest of renal principal cells Dynamic regulation and dysregulation of the water channel aquaporin-2: a common cause of and promising therapeutic target for water balance disorders.Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5.Molecular mechanisms regulating aquaporin-2 in kidney collecting duct.Reciprocal regulation of aquaporin-2 abundance and degradation by protein kinase A and p38-MAP kinase.Dexamethasone increases aquaporin-2 protein expression in ex vivo inner medullary collecting duct suspensions.Identification and Characterization of BmVta1, a Bombyx mori (Lepidoptera: Bombycidae) Homologue for Vta1 That is Up-Regulated in Development.Aquaporin Protein-Protein Interactions.Physical, Functional and Genetic Interactions between the BEACH Domain Protein SPIRRIG and LIP5 and SKD1 and Its Role in Endosomal Trafficking to the Vacuole in Arabidopsis.The Role of Aquaporins in Ocular Lens Homeostasis.Plant and Mammal Aquaporins: Same but Different.Activation of AQP2 water channels without vasopressin: therapeutic strategies for congenital nephrogenic diabetes insipidus.The Expanding Role of Vesicles Containing Aquaporins

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P2860

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

http://www.wikidata.org/entity/Q43133843

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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2009年學術文章

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name

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

@en

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

@nl

type

label

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

@en

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

@nl

prefLabel

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

@en

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

@nl

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P1433

Journal of the American Society of Nephrology

P1476

LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation.

@en

P2093

Anne van der Voorde

http://www.w3.org/2001/XMLSchema#string

Bas W M van Balkom

http://www.w3.org/2001/XMLSchema#string

Erik-Jan Kamsteeg

http://www.w3.org/2001/XMLSchema#string

Francois van Herp

http://www.w3.org/2001/XMLSchema#string

Giel Hendriks

http://www.w3.org/2001/XMLSchema#string

H Christiaan Stronks

http://www.w3.org/2001/XMLSchema#string

Joris H Robben

http://www.w3.org/2001/XMLSchema#string

Michelle Boone

http://www.w3.org/2001/XMLSchema#string

Peter M T Deen

http://www.w3.org/2001/XMLSchema#string

P2860

The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins

Identification and proteomic profiling of exosomes in human urine

Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly

Deficient peptide loading and MHC class II endosomal sorting in a human genetic immunodeficiency disease: the Chediak-Higashi syndrome

Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A.

Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element

The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells

Polarized trafficking and surface expression of the AQP4 water channel are coordinated by serial and regulated interactions with different clathrin-adaptor complexes

An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex

Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1

P304

990-1001

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scholarly article

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10.1681/ASN.2008060648

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5

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P478

20

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Peter van der Sluijs

P577

2009-04-08T00:00:00Z

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19357255

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2678037

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