Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. - Test2 - elhamkhani - TriplyDB

Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.

Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.

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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 cystic fibrosis transmembrane conductance regulator (CFTR) and its stability Stabilization of Nucleotide Binding Domain Dimers Rescues ABCC6 Mutants Associated with Pseudoxanthoma Elasticum.Using a second-order differential model to fit data without baselines in protein isothermal chemical denaturation Complement yourself: Transcomplementation rescues partially folded mutant proteins.Decoding F508del misfolding 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.Regulation of ABCC6 trafficking and stability by a conserved C-terminal PDZ-like sequence 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.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.Some gating potentiators, including VX-770, diminish ΔF508-CFTR functional expression.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.A synonymous codon change alters the drug sensitivity of ΔF508 cystic fibrosis transmembrane conductance regulator.Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.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 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 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.Specific stabilization of CFTR by phosphatidylserine.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.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.

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P2860

Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.

http://www.wikidata.org/entity/Q41148574

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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

Thermal unfolding studies show ...... s nucleotide-binding domain 1.

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type

label

Thermal unfolding studies show ...... s nucleotide-binding domain 1.

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prefLabel

Thermal unfolding studies show ...... s nucleotide-binding domain 1.

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Protein Science

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Thermal unfolding studies show ...... s nucleotide-binding domain 1.

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P2093

Chi Wang

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

Christie G Brouillette

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

Diana Wetmore

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

Irina Protasevich

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

John F Hunt

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

Shane Atwell

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

Spencer Emtage

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

Xun Zhao

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

Zhengrong Yang

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P2860

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

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

Thermodynamic puzzle of apomyoglobin unfolding.

Organic solutes rescue the functional defect in delta F508 cystic fibrosis transmembrane conductance regulator.

Interpreting the effects of small uncharged solutes on protein-folding equilibria.

A molecular mechanism for osmolyte-induced protein stability

Assembly of functional CFTR chloride channels.

Side chain and backbone contributions of Phe508 to CFTR folding.

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10

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19

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2010-10-01T00:00:00Z

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45506533

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20687133

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2998726

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