Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast.
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Mechanisms of CFTR Folding at the Endoplasmic ReticulumLinking yeast genetics to mammalian genomes: identification and mapping of the human homolog of CDC27 via the expressed sequence tag (EST) data baseHuman SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulumAre p.I148T, p.R74W and p.D1270N cystic fibrosis causing mutations?Requirements for Efficient Correction of ΔF508 CFTR Revealed by Analyses of Evolved SequencesDiminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfoldingAllosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTRRibosomal Stalk Protein Silencing Partially Corrects the ΔF508-CFTR Functional Expression DefectDevelopment of CFTR StructureInterplay between ER exit code and domain conformation in CFTR misprocessing and rescue.Complement yourself: Transcomplementation rescues partially folded mutant proteins.Decoding F508del misfolding in cystic fibrosis.Functional complementation of the ste6 gene of Saccharomyces cerevisiae with the pfmdr1 gene of Plasmodium falciparum.Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTRStructural and functional similarities between the nucleotide-binding domains of CFTR and GTP-binding proteinsTargets for cystic fibrosis therapy: proteomic analysis and correction of mutant cystic fibrosis transmembrane conductance regulatorCystic fibrosis transmembrane conductance regulator mutations that disrupt nucleotide bindingThe cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.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.Rational Coupled Dynamics Network Manipulation Rescues Disease-Relevant Mutant Cystic Fibrosis Transmembrane Conductance Regulator.Saccharomyces cerivisiae as a model system for kidney disease: what can yeast tell us about renal function?Probing conformational rescue induced by a chemical corrector of F508del-cystic fibrosis transmembrane conductance regulator (CFTR) mutant.Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms.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.Is congenital bilateral absence of vas deferens a primary form of cystic fibrosis? Analyses of the CFTR gene in 67 patients.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 activityBiogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.Deletion of Phenylalanine 508 in the First Nucleotide-binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator Increases Conformational Exchange and Inhibits Dimerization.The cystic-fibrosis-associated ΔF508 mutation confers post-transcriptional destabilization on the C. elegans ABC transporter PGP-3.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 assemblyDynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stabilityGout-causing Q141K mutation in ABCG2 leads to instability of the nucleotide-binding domain and can be corrected with small moleculesBinding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategyNovel CFTR Mutations in Two Iranian Families with Severe Cystic Fibrosis.Mechanism-based corrector combination restores ΔF508-CFTR folding and function.Proteomics uncovering possible key players in F508del-CFTR processing and trafficking.Cystic fibrosis transmembrane conductance regulator (ABCC7) structure
P2860
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P2860
Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Identification of revertants f ...... g STE6-CFTR chimeras in yeast.
@en
type
label
Identification of revertants f ...... g STE6-CFTR chimeras in yeast.
@en
prefLabel
Identification of revertants f ...... g STE6-CFTR chimeras in yeast.
@en
P2093
P1433
P1476
Identification of revertants f ...... g STE6-CFTR chimeras in yeast.
@en
P2093
P304
P356
10.1016/0092-8674(93)90233-G
P407
P577
1993-04-01T00:00:00Z