Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway.
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Mechanisms of CFTR Folding at the Endoplasmic ReticulumDeletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperonePerturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasomeThe 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 Hsp70The crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporterStructure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulatorRequirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved SequencesDistinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.The C-terminal hinge region of lipoic acid-bearing domain of E2b is essential for domain interaction with branched-chain alpha-keto acid dehydrogenase kinaseDiminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfoldingThe primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domainDevelopment of CFTR StructureFolding and rescue of a cystic fibrosis transmembrane conductance regulator trafficking mutant identified using human-murine chimeric proteinsCystic fibrosis as a disease of misprocessing of the cystic fibrosis transmembrane conductance regulator glycoproteinInterplay between ER exit code and domain conformation in CFTR misprocessing and rescue.Protein misfolding and degradation in genetic diseases.ABCMdb reloaded: updates on mutations in ATP binding cassette proteins.Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexinOrganic solutes rescue the functional defect in delta F508 cystic fibrosis transmembrane conductance regulator.Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTRCharge-rich regions modulate the anti-aggregation activity of Hsp90.The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.Cysteine string protein monitors late steps in cystic fibrosis transmembrane conductance regulator biogenesis.Rescuing protein conformation: prospects for pharmacological therapy in cystic fibrosisSmall heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation.Global analysis of protein folding thermodynamics for disease state characterizationA foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase.Side chain and backbone contributions of Phe508 to CFTR folding.Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.CFTR: folding, misfolding and correcting the ΔF508 conformational defect.Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR traffickingIn vitro pharmacologic restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR.Mis-trafficking of bicarbonate transporters: implications to human diseases.Functional Rescue of F508del-CFTR Using Small Molecule CorrectorsApoptotic process in cystic fibrosis cells.Nucleotide-binding domain 1 of cystic fibrosis transmembrane conductance regulator production of a suitable protein for structural studies.Two Small Molecules Restore Stability to a Subpopulation of the Cystic Fibrosis Transmembrane Conductance Regulator with the Predominant Disease-causing Mutation.From the endoplasmic reticulum to the plasma membrane: mechanisms of CFTR folding and trafficking.Effect of Annexin A5 on CFTR: regulated traffic or scaffolding?Thermal unfolding simulations of NBD1 domain variants reveal structural motifs associated with the impaired folding of F508del-CFTR.
P2860
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P2860
Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway.
@en
type
label
Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway.
@en
prefLabel
Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway.
@en
P356
P1476
Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway.
@en
P304
P356
10.1074/JBC.271.13.7261
P407
P577
1996-03-01T00:00:00Z