Varaico: Literature-Extracted Genetic Variants

Gene:CFTR
Variant:p.S712A
Back to variants list

CFTR

NM_000492.4:p.S712A

Associated Papers

Role of tyrosine phosphorylation in the muscarinic activation of the cystic fibrosis transmembrane conductance regulator (CFTR).

Billet A et al.

The Journal of Biological Chemistry, 2013

AMP-activated protein kinase phosphorylation of the R domain inhibits PKA stimulation of CFTR.

King JD et al.

American Journal of Physiology. Cell Physiology, 2009

Cystic fibrosis transmembrane conductance regulator: a chloride channel gated by ATP binding and hydrolysis.

Bompadre SG et al.

Sheng Li Xue Bao : [acta Physiologica Sinica], 2007

Capsaicin potentiates wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride-channel currents.

Ai T et al.

Molecular Pharmacology, 2004

Protein kinase A regulates ATP hydrolysis and dimerization by a CFTR (cystic fibrosis transmembrane conductance regulator) domain.

Howell LD et al.

The Biochemical Journal, 2004

CFTR activation: additive effects of stimulatory and inhibitory phosphorylation sites in the R domain.

Wilkinson DJ et al.

The American Journal of Physiology, 1997

Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by negative charge in the R domain.

Berger HA et al.

The Japanese Journal of Physiology, 1994

Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by negative charge in the R domain.

Rich DP et al.

The Journal of Biological Chemistry, 1993

Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all 10 PKA consensus phosphorylation sites.

Chang XB et al.

The Journal of Biological Chemistry, 1993

Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel.

Cheng SH et al.

Cell, 1991

Select a paper to view details
UCSC Genome Browser·Imprint·Privacy·Terms·Feedback·Email Updates·

Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."