Influence of phosphorylation by protein kinase A on CFTR at the cell surface and endoplasmic reticulum.
about
CFTR gating I: Characterization of the ATP-dependent gating of a phosphorylation-independent CFTR channel (DeltaR-CFTR).Continuous mucociliary transport by primary human airway epithelial cells in vitro.Domain-domain associations in cystic fibrosis transmembrane conductance regulator.Naturally occurring mutations in the canine CFTR gene.Regulation of the cystic fibrosis transmembrane conductance regulator anion channel by tyrosine phosphorylation.Cell and gene therapy for genetic diseases: inherited disorders affecting the lung and those mimicking sudden infant death syndromePreferential phosphorylation of R-domain Serine 768 dampens activation of CFTR channels by PKA.Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domainsRole for SUR2A ED domain in allosteric coupling within the K(ATP) channel complex.The CFTR ion channel: gating, regulation, and anion permeationCLC-0 and CFTR: chloride channels evolved from transporters.IFN{gamma} regulates retinal pigment epithelial fluid transport.Regulation of ABC transporter function via phosphorylation by protein kinases.The secret life of CFTR as a calcium-activated chloride channel.Potential sites of CFTR activation by tyrosine kinases.The major cystic fibrosis causing mutation exhibits defective propensity for phosphorylation.Current insights into the role of PKA phosphorylation in CFTR channel activity and the pharmacological rescue of cystic fibrosis disease-causing mutants.Role of tyrosine phosphorylation in the muscarinic activation of the cystic fibrosis transmembrane conductance regulator (CFTR).Posttranslational regulation of Abcc2 expression by SUMOylation system.On the mechanism of gating defects caused by the R117H mutation in cystic fibrosis transmembrane conductance regulator.The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover.The Walker B motif of the second nucleotide-binding domain (NBD2) of CFTR plays a key role in ATPase activity by the NBD1-NBD2 heterodimer.Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR.Effects of butyrate on active sodium and chloride transport in rat and rabbit distal colon.Nucleoside triphosphate pentose ring impact on CFTR gating and hydrolysis.Dibasic phosphorylation sites in the R domain of CFTR have stimulatory and inhibitory effects on channel activation.Structural mechanisms of CFTR function and dysfunction.
P2860
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P2860
Influence of phosphorylation by protein kinase A on CFTR at the cell surface and endoplasmic reticulum.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Influence of phosphorylation b ...... ace and endoplasmic reticulum.
@ast
Influence of phosphorylation b ...... ace and endoplasmic reticulum.
@en
type
label
Influence of phosphorylation b ...... ace and endoplasmic reticulum.
@ast
Influence of phosphorylation b ...... ace and endoplasmic reticulum.
@en
prefLabel
Influence of phosphorylation b ...... ace and endoplasmic reticulum.
@ast
Influence of phosphorylation b ...... ace and endoplasmic reticulum.
@en
P2093
P1476
Influence of phosphorylation b ...... ace and endoplasmic reticulum.
@en
P2093
A A Aleksandrov
D M Clarke
F S Seibert
J R Riordan
J W Hanrahan
P304
P356
10.1016/S0005-2736(99)00163-7
P407
P577
1999-12-01T00:00:00Z