The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain
about
Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTppMechanisms of CFTR Folding at the Endoplasmic ReticulumModulation of the maladaptive stress response to manage diseases of protein foldingRequirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved SequencesCo- and Post-Translational Protein Folding in the ERTime, space, and disorder in the expanding proteome universe.Development of CFTR StructureEnhancing the Potency of F508del Correction: A Multi-Layer Combinational Approach to Drug Discovery for Cystic Fibrosis.Complement yourself: Transcomplementation rescues partially folded mutant proteins.A chaperone trap contributes to the onset of cystic fibrosis.Rational Coupled Dynamics Network Manipulation Rescues Disease-Relevant Mutant Cystic Fibrosis Transmembrane Conductance Regulator.Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant.Biophysical characterisation of calumenin as a charged F508del-CFTR folding modulatorAlteration of CFTR transmembrane span integration by disease-causing mutations.Human-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-ΔF508 processing and alter its gating defect.Some gating potentiators, including VX-770, diminish ΔF508-CFTR functional expression.FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stabilityThermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: protection by single suppressor mutations and inhibiting channel activityMolecular modelling and molecular dynamics of CFTR.Hallmarks of therapeutic management of the cystic fibrosis functional landscape.Combination of Correctors Rescue ΔF508-CFTR by Reducing Its Association with Hsp40 and Hsp27.Correctors of ΔF508 CFTR restore global conformational maturation without thermally stabilizing the mutant protein.Dynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stabilityGout-causing Q141K mutation in ABCG2 leads to instability of the nucleotide-binding domain and can be corrected with small moleculesTranscomplementation by a truncation mutant of cystic fibrosis transmembrane conductance regulator (CFTR) enhances ΔF508 processing through a biomolecular interactionCFTR: folding, misfolding and correcting the ΔF508 conformational defect.Protein folding in the endoplasmic reticulumRepairing the basic defect in cystic fibrosis - one approach is not enough.From the endoplasmic reticulum to the plasma membrane: mechanisms of CFTR folding and trafficking.CFTR potentiators partially restore channel function to A561E-CFTR, a cystic fibrosis mutant with a similar mechanism of dysfunction as F508del-CFTRRevertant mutants modify, but do not rescue, the gating defect of the cystic fibrosis mutant G551D-CFTR.Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.Matrine modulates HSC70 levels and rescues ΔF508-CFTR.Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide.Correctors Rescue CFTR Mutations in Nucleotide-Binding Domain 1 (NBD1) by Modulating Proteostasis.Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.Structural mechanisms of CFTR function and dysfunction.
P2860
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P2860
The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The primary folding defect and ...... anslation of the mutant domain
@ast
The primary folding defect and ...... anslation of the mutant domain
@en
The primary folding defect and ...... anslation of the mutant domain
@nl
type
label
The primary folding defect and ...... anslation of the mutant domain
@ast
The primary folding defect and ...... anslation of the mutant domain
@en
The primary folding defect and ...... anslation of the mutant domain
@nl
prefLabel
The primary folding defect and ...... anslation of the mutant domain
@ast
The primary folding defect and ...... anslation of the mutant domain
@en
The primary folding defect and ...... anslation of the mutant domain
@nl
P2093
P2860
P1433
P1476
The primary folding defect and ...... anslation of the mutant domain
@en
P2093
Andre Schmidt
Bertrand Kleizen
Hanneke Hoelen
Ineke Braakman
John Richardson
Paraskevi Charitou
Philip J Thomas
P2860
P304
P356
10.1371/JOURNAL.PONE.0015458
P407
P577
2010-11-30T00:00:00Z