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Biochemical and biophysical approaches to probe CFTR structure.
scientific article published on January 2011
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3266684
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21594797%20AND%20SRC:MED&resulttype=core&format=json
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1 February 2020
title
Biochemical and biophysical approaches to probe CFTR structure
(English)
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3266684
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1 February 2020
author
Juan Mendoza
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2
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3266684
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1 February 2020
author name string
André Schmidt
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1
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3266684
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21594797%20AND%20SRC:MED&resulttype=core&format=json
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1 February 2020
Philip J Thomas
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3
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3266684
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1 February 2020
language of work or name
English
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publication date
1 January 2011
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3266684
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1 February 2020
published in
Methods in Molecular Biology
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Europe PubMed Central
PMCID
3266684
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21594797%20AND%20SRC:MED&resulttype=core&format=json
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1 February 2020
volume
741
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Europe PubMed Central
PMCID
3266684
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21594797%20AND%20SRC:MED&resulttype=core&format=json
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1 February 2020
page(s)
365-376
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3266684
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1 February 2020
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Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry
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Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
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Cysteine string protein promotes proteasomal degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) by increasing its interaction with the C terminus of Hsp70-interacting protein and promoting CFTR ubiquitylation.
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Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2
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Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms
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Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin
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Side chain and backbone contributions of Phe508 to CFTR folding
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The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR.
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A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
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Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast
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Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator
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Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
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The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
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The cystic fibrosis transmembrane conductance regulator. Overexpression, purification, and characterization of wild type and delta F508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein.
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The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
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Identification of revertants for the cystic fibrosis delta F508 mutation using STE6-CFTR chimeras in yeast
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Degradation of CFTR by the ubiquitin-proteasome pathway
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25 September 2017
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Lipopolysaccharide stabilizes the crystal packing of the ABC transporter MsbA.
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17 June 2018
Mutation of R555 in CFTR-delta F508 enhances function and partially corrects defective processing.
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17 June 2018
Cystic fibrosis with three mutations in the cystic fibrosis transmembrane conductance regulator gene
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17 June 2018
Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
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17 June 2018
Mild course of cystic fibrosis associated with heterozygosity for infrequent mutations in the first nucleotide-binding fold of CFTR.
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17 June 2018
Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure.
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19 August 2018
Expression and characterization of the NBD1-R domain region of CFTR: evidence for subunit-subunit interactions
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19 August 2018
Multiple proteolytic systems, including the proteasome, contribute to CFTR processing.
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19 August 2018
Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
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19 August 2018
Solubilizing Mutations Used to Crystallize One CFTR Domain Attenuate the Trafficking and Channel Defects Caused by the Major Cystic Fibrosis Mutation
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2 December 2018
A Bacterial System for Investigating Transport Effects of Cystic Fibrosis—Associated Mutations
1 reference
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reference URL
https://pubmed.ncbi.nlm.nih.gov/21594797
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Recombinant synthesis, purification, and nucleotide binding characteristics of the first nucleotide binding domain of the cystic fibrosis gene product
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21594797
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Limited proteolysis as a probe for arrested conformational maturation of delta F508 CFTR
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21594797
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1007/978-1-61779-117-8_24
1 reference
stated in
Europe PubMed Central
PMCID
3266684
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21594797%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 February 2020
PMCID
3266684
1 reference
stated in
Europe PubMed Central
PMCID
3266684
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21594797%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 February 2020
PubMed ID
21594797
1 reference
stated in
Europe PubMed Central
PMCID
3266684
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21594797%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 February 2020
ResearchGate publication ID
51148750
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