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

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

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

http://www.wikidata.org/entity/Q35215090

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Mechanisms of CFTR Folding at the Endoplasmic Reticulum Disruption of cytokeratin-8 interaction with F508del-CFTR corrects its functional defect Deletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperone Requirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved Sequences ABCG2: the molecular mechanisms of urate secretion and gout Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain The silent codon change I507-ATC->ATT contributes to the severity of the ΔF508 CFTR channel dysfunction Deletion of CFTR translation start site reveals functional isoforms of the protein in CF patients.Folding and rescue of a cystic fibrosis transmembrane conductance regulator trafficking mutant identified using human-murine chimeric proteins Interplay between ER exit code and domain conformation in CFTR misprocessing and rescue.Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR Contribution of casein kinase 2 and spleen tyrosine kinase to CFTR trafficking and protein kinase A-induced activity.Cystic fibrosis transmembrane conductance regulator (CFTR) potentiator VX-770 (ivacaftor) opens the defective channel gate of mutant CFTR in a phosphorylation-dependent but ATP-independent manner.Targets for cystic fibrosis therapy: proteomic analysis and correction of mutant cystic fibrosis transmembrane conductance regulator The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.Dual activity of aminoarylthiazoles on the trafficking and gating defects of the cystic fibrosis transmembrane conductance regulator chloride channel caused by cystic fibrosis mutations.Orphan missense mutations in the cystic fibrosis transmembrane conductance regulator: A three-step biological approach to establishing a correlation between genotype and phenotype Thermally unstable gating of the most common cystic fibrosis mutant channel (ΔF508): "rescue" by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops.Measurements of Functional Responses in Human Primary Lung Cells as a Basis for Personalized Therapy for Cystic Fibrosis.Human-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-ΔF508 processing and alter its gating defect.Phosphorylation-dependent 14-3-3 protein interactions regulate CFTR biogenesis Processing and function of CFTR-DeltaF508 are species-dependent.Thermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: protection by single suppressor mutations and inhibiting channel activity Gout-causing Q141K mutation in ABCG2 leads to instability of the nucleotide-binding domain and can be corrected with small molecules Cooperative assembly and misfolding of CFTR domains in vivo.Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR trafficking Proteomics uncovering possible key players in F508del-CFTR processing and trafficking.Targeting F508del-CFTR to develop rational new therapies for cystic fibrosis.Primary ciliary dyskinesia: recent advances in epidemiology, diagnosis, management and relationship with the expanding spectrum of ciliopathy.Managing the underlying cause of cystic fibrosis: a future role for potentiators and correctors.Repairing 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-CFTR Revertant 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.Effect of Annexin A5 on CFTR: regulated traffic or scaffolding?The most common cystic fibrosis-associated mutation destabilizes the dimeric state of the nucleotide-binding domains of CFTR.N-terminal CFTR missense variants severely affect the behavior of the CFTR chloride channel.Biochemical and biophysical approaches to probe CFTR structure.

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

http://www.wikidata.org/entity/Q35215090

description

2006 nî lūn-bûn

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2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Revertant mutants G550E and 4R ...... CFTR by different mechanisms.

@ast

Revertant mutants G550E and 4R ...... CFTR by different mechanisms.

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type

label

Revertant mutants G550E and 4R ...... CFTR by different mechanisms.

@ast

Revertant mutants G550E and 4R ...... CFTR by different mechanisms.

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prefLabel

Revertant mutants G550E and 4R ...... CFTR by different mechanisms.

@ast

Revertant mutants G550E and 4R ...... CFTR by different mechanisms.

@en

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PNAS.0608312103

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Revertant mutants G550E and 4R ...... CFTR by different mechanisms.

@en

P2093

André Schmidt

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

Cláudio M Soares

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

David N Sheppard

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Margarida D Amaral

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Mário Neto

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Mónica Roxo-Rosa

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Zhe Xu

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Zhiwei Cai

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P2860

Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis

The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70

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

Structure and function of the CFTR chloride channel

Histone acetyltransferases

The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

Degradation of CFTR by the ubiquitin-proteasome pathway

Conformational and temperature-sensitive stability defects of the delta F508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments.

Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin

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17891-17896

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10.1073/PNAS.0608312103

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47

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103

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2006-11-10T00:00:00Z

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6698389

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17098864

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cystic fibrosis

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1693843

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