Ahcyl2 upregulates NBCe1-B via multiple serine residues of the PEST domain-mediated association. - Wikidata - thesis-toulmin - TriplyDB

Ahcyl2 upregulates NBCe1-B via multiple serine residues of the PEST domain-mediated association.

Ahcyl2 upregulates NBCe1-B via multiple serine residues of the PEST domain-mediated association.

http://www.wikidata.org/entity/Q37060307

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Splicing variation of Long-IRBIT determines the target selectivity of IRBIT family proteins.

P2860

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P2860

Ahcyl2 upregulates NBCe1-B via multiple serine residues of the PEST domain-mediated association.

http://www.wikidata.org/entity/Q37060307

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 23 June 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Ahcyl2 upregulates NBCe1-B via ...... T domain-mediated association.

@en

Ahcyl2 upregulates NBCe1-B via ...... T domain-mediated association.

@nl

type

label

Ahcyl2 upregulates NBCe1-B via ...... T domain-mediated association.

@en

Ahcyl2 upregulates NBCe1-B via ...... T domain-mediated association.

@nl

prefLabel

Ahcyl2 upregulates NBCe1-B via ...... T domain-mediated association.

@en

Ahcyl2 upregulates NBCe1-B via ...... T domain-mediated association.

@nl

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P356

KJPP.2016.20.4.433

P1433

Korean Journal of Physiology and Pharmacology

P1476

Ahcyl2 upregulates NBCe1-B via ...... T domain-mediated association.

@en

P2093

Dongki Yang

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

Jeong Yeal Ahn

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

Pil Whan Park

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

P2860

IRBIT, an inositol 1,4,5-trisphosphate receptor-binding protein, specifically binds to and activates pancreas-type Na+/HCO3- cotransporter 1 (pNBC1)

IRBIT suppresses IP3 receptor activity by competing with IP3 for the common binding site on the IP3 receptor

An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage

IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor

Molecular cloning, chromosomal localization, tissue distribution, and functional expression of the human pancreatic sodium bicarbonate cotransporter

IRBIT coordinates epithelial fluid and HCO3- secretion by stimulating the transporters pNBC1 and CFTR in the murine pancreatic duct

IRBIT governs epithelial secretion in mice by antagonizing the WNK/SPAK kinase pathway

The solute carrier 26 family of proteins in epithelial ion transport.

The IRBIT domain adds new functions to the AHCY family.

A molecular mechanism for aberrant CFTR-dependent HCO(3)(-) transport in cystic fibrosis.

P304

433-440

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scholarly article

P356

10.4196/KJPP.2016.20.4.433

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

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4

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20

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2016-06-23T00:00:00Z

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27382360

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4930912

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