Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis. - Wikidata - awgldk - TriplyDB

Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.

Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.

http://www.wikidata.org/entity/Q41148531

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Mechanisms of CFTR Folding at the Endoplasmic Reticulum Disruption of cytokeratin-8 interaction with F508del-CFTR corrects its functional defect New and emerging targeted therapies for cystic fibrosis Requirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved Sequences Allosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTR The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508 Using a second-order differential model to fit data without baselines in protein isothermal chemical denaturation Decoding F508del misfolding in cystic fibrosis.Intragenic suppressing mutations correct the folding and intracellular traffic of misfolded mutants of Yor1p, a eukaryotic drug transporter.VX-809 corrects folding defects in cystic fibrosis transmembrane conductance regulator protein through action on membrane-spanning domain 1.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.Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant.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.Human-mouse cystic fibrosis transmembrane conductance regulator (CFTR) chimeras identify regions that partially rescue CFTR-ΔF508 processing and alter its gating defect.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.Cystic fibrosis lung environment and Pseudomonas aeruginosa infection.Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.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 Binding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategy CFTR: folding, misfolding and correcting the ΔF508 conformational defect.Mechanism-based corrector combination restores ΔF508-CFTR folding and function.Combating cystic fibrosis: in search for CF transmembrane conductance regulator (CFTR) modulators.Functional Rescue of F508del-CFTR Using Small Molecule Correctors Cystic fibrosis transmembrane conductance regulator (ABCC7) structure Breakthrough therapies: Cystic fibrosis (CF) potentiators and correctors.Repairing the basic defect in cystic fibrosis - one approach is not enough.Stabilization of a nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator yields insight into disease-causing mutations.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.Can Cystic Fibrosis Patients Finally Catch a Breath With Lumacaftor/Ivacaftor?Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR.Thermal unfolding simulations of NBD1 domain variants reveal structural motifs associated with the impaired folding of F508del-CFTR.The most common cystic fibrosis-associated mutation destabilizes the dimeric state of the nucleotide-binding domains of CFTR.Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.Conformational changes relevant to channel activity and folding within the first nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator.

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Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.

http://www.wikidata.org/entity/Q41148531

description

2010 nî lūn-bûn

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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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2010年论文

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2010年论文

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name

Integrated biophysical studies ...... is of F508del cystic fibrosis.

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type

label

Integrated biophysical studies ...... is of F508del cystic fibrosis.

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Integrated biophysical studies ...... is of F508del cystic fibrosis.

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Protein Science

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Integrated biophysical studies ...... is of F508del cystic fibrosis.

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Chi Wang

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

Christie G Brouillette

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Derek Seehausen

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Diana R Wetmore

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

Irina Protasevich

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J Spencer Emtage

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John F Hunt

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Shane Atwell

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Timothy Skalak

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Xun Zhao

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P2860

Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

The ABC protein turned chloride channel whose failure causes cystic fibrosis

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast

Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter

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

Crystal structure of the ATP-binding subunit of an ABC transporter

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1932-1947

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10

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19

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45506563

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20687163

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cystic fibrosis

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2998727

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