Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR. - Wikidata - wikimedia - TriplyDB

Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.

Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.

http://www.wikidata.org/entity/Q39381996

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Mechanisms of CFTR Folding at the Endoplasmic Reticulum The silent codon change I507-ATC->ATT contributes to the severity of the ΔF508 CFTR channel dysfunction Impact of the F508del mutation on ovine CFTR, a Cl- channel with enhanced conductance and ATP-dependent gating.Decoding F508del misfolding in cystic fibrosis.The N-terminal domain allosterically regulates cleavage and activation of the epithelial sodium channel.Cystic fibrosis transmembrane conductance regulator (CFTR) potentiators protect G551D but not ΔF508 CFTR from thermal instability.Potentiator ivacaftor abrogates pharmacological correction of ΔF508 CFTR in cystic fibrosis.Rational Coupled Dynamics Network Manipulation Rescues Disease-Relevant Mutant Cystic Fibrosis Transmembrane Conductance Regulator.Structure-based rational design to enhance the solubility and thermostability of a bacterial laccase Lac15 Full-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics.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.Restoration of NBD1 thermal stability is necessary and sufficient to correct ∆F508 CFTR folding and assembly Dynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stability Mechanism-based corrector combination restores ΔF508-CFTR folding and function.Functional Rescue of F508del-CFTR Using Small Molecule Correctors Cystic fibrosis transmembrane conductance regulator (ABCC7) structure Breakthrough therapies: Cystic fibrosis (CF) potentiators and correctors.Two Small Molecules Restore Stability to a Subpopulation of the Cystic Fibrosis Transmembrane Conductance Regulator with the Predominant Disease-causing Mutation.Thermal stability of purified and reconstituted CFTR in a locked open channel conformation.The major cystic fibrosis causing mutation exhibits defective propensity for phosphorylation.Revertant mutants modify, but do not rescue, the gating defect of the cystic fibrosis mutant G551D-CFTR.Thermal unfolding simulations of NBD1 domain variants reveal structural motifs associated with the impaired folding of F508del-CFTR.Functional reconstitution and channel activity measurements of purified wildtype and mutant CFTR protein.The holy grail of cystic fibrosis research: pharmacological repair of the F508del-CFTR mutation.Membrane protein stability can be compromised by detergent interactions with the extramembranous soluble domains Enhanced thermal stability of Pseudomonas aeruginosa lipoxygenase through modification of two highly flexible regions.Substitution of Yor1p NBD1 residues improves the thermal stability of Human Cystic Fibrosis Transmembrane Conductance Regulator.A role for the cystic fibrosis transmembrane conductance regulator in the nitric oxide-dependent release of Cl- from acidic organelles in amacrine cells.Mapping allosteric linkage to channel gating of extracellular domains in the human epithelial sodium channel.CFTR structure: lassoing cystic fibrosis.Sites associated with Kalydeco binding on human Cystic Fibrosis Transmembrane Conductance Regulator revealed by Hydrogen/Deuterium Exchange.Impact of the cystic fibrosis mutation F508del-CFTR on renal cyst formation and growth Graph-Theoretic Models of Mutations in the Nucleotide Binding Domain 1 of the Cystic Fibrosis Transmembrane Conductance Regulator

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Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.

http://www.wikidata.org/entity/Q39381996

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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name

Allosteric modulation balances ...... stores function of ΔF508 CFTR.

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Allosteric modulation balances ...... stores function of ΔF508 CFTR.

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type

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Allosteric modulation balances ...... stores function of ΔF508 CFTR.

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Allosteric modulation balances ...... stores function of ΔF508 CFTR.

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Allosteric modulation balances ...... stores function of ΔF508 CFTR.

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Allosteric modulation balances ...... stores function of ΔF508 CFTR.

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J.JMB.2012.03.001

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Journal of Molecular Biology

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Allosteric modulation balances ...... stores function of ΔF508 CFTR.

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Alexey E Alekseev

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Andrei A Aleksandrov

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John R Riordan

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Lihua He

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Liying Cui

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Luba A Aleksandrov

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Martina Gentzsch

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Pradeep Kota

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Santiago Reyes

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Tim Jensen

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P2860

Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme

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

Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain

MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology.

Energy landscape along an enzymatic reaction trajectory: hinges or cracks?

Automated minimization of steric clashes in protein structures

Emergence of protein fold families through rational design

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41-60

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1-2

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419

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Nikolay V. Dokholyan

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2012-03-08T00:00:00Z

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221692686

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