Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR - Wikidata - awgldk - TriplyDB

Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR

Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR

http://www.wikidata.org/entity/Q34017049

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Correcting the cystic fibrosis disease mutant, A455E CFTR Mechanisms of CFTR Folding at the Endoplasmic Reticulum The Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): THREE-DIMENSIONAL STRUCTURE AND LOCALIZATION OF A CHANNEL GATE The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain Stabilization of Nucleotide Binding Domain Dimers Rescues ABCC6 Mutants Associated with Pseudoxanthoma Elasticum.Enhancing the Potency of F508del Correction: A Multi-Layer Combinational Approach to Drug Discovery for Cystic Fibrosis.Complement yourself: Transcomplementation rescues partially folded mutant proteins.Decoding F508del misfolding in cystic fibrosis.Targets for cystic fibrosis therapy: proteomic analysis and correction of mutant cystic fibrosis transmembrane conductance regulator Intragenic suppressing mutations correct the folding and intracellular traffic of misfolded mutants of Yor1p, a eukaryotic drug transporter.Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant.Human-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-ΔF508 processing and alter its gating defect.Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels.Thermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: protection by single suppressor mutations and inhibiting channel activity Molecular modelling and molecular dynamics of CFTR.Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.Correctors of ΔF508 CFTR restore global conformational maturation without thermally stabilizing the mutant protein.Dynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stability CFTR: folding, misfolding and correcting the ΔF508 conformational defect.Crucial role for phylogenetically conserved cytoplasmic loop 3 in ABCC4 protein expression Mechanism-based corrector combination restores ΔF508-CFTR folding and function.Cystic fibrosis transmembrane conductance regulator (ABCC7) structure Cystic fibrosis transmembrane regulator correctors and potentiators.Orkambi® and amplifier co-therapy improves function from a rare CFTR mutation in gene-edited cells and patient tissue.Stabilization of a nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator yields insight into disease-causing mutations.The major cystic fibrosis causing mutation exhibits defective propensity for phosphorylation.Thermal unfolding simulations of NBD1 domain variants reveal structural motifs associated with the impaired folding of F508del-CFTR.The V510D suppressor mutation stabilizes DeltaF508-CFTR at the cell surface.Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1 Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.Fixing cystic fibrosis by correcting CFTR domain assembly.Synonymous codon usage affects the expression of wild type and F508del CFTR.Membrane protein stability can be compromised by detergent interactions with the extramembranous soluble domains Molecular dynamics simulation study on the structural instability of the most common cystic fibrosis-associated mutant ΔF508-CFTR.

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P2860

Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR

http://www.wikidata.org/entity/Q34017049

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@ast

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@en

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

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type

label

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@ast

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@en

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@nl

prefLabel

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@ast

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@en

Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@nl

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Restoration of domain folding ...... the DeltaF508 mutation in CFTR

@en

P2093

John R Riordan

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

Kenneth L Nesbitt

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

Lihua He

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

Liying Cui

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

Luba A Aleksandrov

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

Timothy J Jensen

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

P2860

Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator

Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator

Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry

Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding

Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms.

Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function

Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2

CFTR function and prospects for therapy.

Cooperative assembly and misfolding of CFTR domains in vivo.

Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast.

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3103-3112

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42109023

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20233947

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2909275

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