Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
about
Small-Molecule Stabilization of the 14-3-3/Gab2 Protein-Protein Interaction (PPI) Interface14-3-3 isoforms bind directly exon B of the 5'-UTR of human surfactant protein A2 mRNARegulatory R region of the CFTR chloride channel is a dynamic integrator of phospho-dependent intra- and intermolecular interactions.Alteration of protein function by a silent polymorphism linked to tRNA abundance.L-type calcium channels play a critical role in maintaining lens transparency by regulating phosphorylation of aquaporin-0 and myosin light chain and expression of connexinsDownregulation of urea transporter UT-A1 activity by 14-3-3 protein.Protein-protein interactions as drug targets.Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Regulation of the cystic fibrosis transmembrane conductance regulator anion channel by tyrosine phosphorylation.Molecular modelling and molecular dynamics of CFTR.Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR.MAST205 competes with cystic fibrosis transmembrane conductance regulator (CFTR)-associated ligand for binding to CFTR to regulate CFTR-mediated fluid transportFinding Our Way in the Dark Proteome.Synergy of cAMP and calcium signaling pathways in CFTR regulation.Functional Rescue of F508del-CFTR Using Small Molecule CorrectorsStructural changes of CFTR R region upon phosphorylation: a plastic platform for intramolecular and intermolecular interactions.Stabilization of a nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator yields insight into disease-causing mutations.Trafficking and function of the cystic fibrosis transmembrane conductance regulator: a complex network of posttranslational modifications.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.Attenuation of Phosphorylation-dependent Activation of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) by Disease-causing Mutations at the Transmission Interface.The Molecular Tweezer CLR01 Stabilizes a Disordered Protein-Protein Interface.A thermodynamic model for multivalency in 14-3-3 protein-protein interactions
P2860
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P2860
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
@ast
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
@en
type
label
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
@ast
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
@en
prefLabel
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
@ast
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
@en
P2093
P2860
P356
P1476
Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis
@en
P2093
Ana Carina Da Paula
Carol A Bertrand
Kathryn W Peters
Raymond A Frizzell
Xiubin Liang
Zoltán Bozóky
P2860
P304
P356
10.1091/MBC.E11-08-0662
P577
2012-01-25T00:00:00Z