Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator.
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Summary
Results indicated that G85E and G91R mutations affected CFTR folding, not by gross disruption of transmembrane assembly, but rather through insertion of a charged residue within the plane of the bilayer, which in turn influenced higher order tertiary structure.
- Type
- article
- Published
- 1997-09-01
- Cited by
- 74
- References
- 40
- Access
- Open access
- OpenAlex
- https://openalex.org/W9276724
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:34085706
Keywords
Political science
References
- Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP.
- Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator.
- The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide.
- Cl- channel activity in Xenopus oocytes expressing the cystic fibrosis gene.
- Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator.
- Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion.
- The cystic fibrosis transmembrane conductance regulator is a dual ATP and chloride channel.
- Evidence for an alternate model of human P-glycoprotein structure and biogenesis.
- Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product.
- Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences.
- Incorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein
- A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum.
- Membrane protein spanning segments as export signals.
- Identification of mutations in exons 1 through 8 of the cystic fibrosis transmembrane conductance regulator (CFTR) gene.
- Predicting the orientation of eukaryotic membrane-spanning proteins.
- Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein.
- Multiple proteolytic systems, including the proteasome, contribute to CFTR processing.
- Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains.
- The amino-terminal portion of CFTR forms a regulated CI− channel
- Glycerol Reverses the Misfolding Phenotype of the Most Common Cystic Fibrosis Mutation (*)
Cited by
- THERMAL INSTABILITY OF ΔF508 CFTR CHANNEL FUNCTION: PROTECTION BY SINGLE SUPPRESSOR MUTATIONS AND INHIBITING CHANNEL ACTIVITY
- The Role of Molecular Chaperones in the ER Associated Degradation of the Cystic Fibrosis Transmembrane Conductance Regulator in the Budding Yeast S. cerevisiae
- Orphan missense mutations in the cystic fibrosis transmembrane conductance regulator: A three-step biological approach to establishing a correlation between genotype and phenotype.
- CFTR degradation and aggregation.
- Defective folding and rapid degradation of mutant proteins is a common disease mechanism in genetic disorders
- Ubiquitin-Proteasome Protocols
- The role of the UPS in cystic fibrosis
- A haplotype framework for cystic fibrosis mutations in Iran.
- CFTR: new members join the fold.
- Insight in eukaryotic ABC transporter function by mutation analysis
- Defects in processing and trafficking of the cystic fibrosis transmembrane conductance regulator.
- Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase.
- Effect of Two Tyrosine Mutations on the Activity and Regulation of the Renal Type II Na/Pi-Cotransporter Expressed in Oocytes
- Differential Stability of Biogenesis Intermediates Reveals a Common Pathway for Aquaporin-1 Topological Maturation*
- Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function
- An Energy-dependent Maturation Step Is Required for Release of the Cystic Fibrosis Transmembrane Conductance Regulator from Early Endoplasmic Reticulum Biosynthetic Machinery*
- An image analysis method to quantify CFTR subcellular localization.
- N‐terminal CFTR missense variants severely affect the behavior of the CFTR chloride channel
- Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator.
- Development of CFTR Structure
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