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Conformational changes in the catalytically inactive nucleotide-binding site of CFTR.
scientific article published on 10 June 2013
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Europe PubMed Central
PMC publication ID
3691448
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
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2 March 2020
title
Conformational changes in the catalytically inactive nucleotide-binding site of CFTR
(English)
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Europe PubMed Central
PMC publication ID
3691448
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
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2 March 2020
author
László Csanády
series ordinal
1
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Europe PubMed Central
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3691448
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
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2 March 2020
Andras Szollosi
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3
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Europe PubMed Central
PMC publication ID
3691448
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
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2 March 2020
Paola Vergani
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5
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3691448
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2 March 2020
author name string
Csaba Mihályi
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2
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3691448
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2 March 2020
Beáta Töröcsik
series ordinal
4
1 reference
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Europe PubMed Central
PMC publication ID
3691448
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 March 2020
publication date
10 June 2013
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stated in
Europe PubMed Central
PMC publication ID
3691448
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 March 2020
published in
The Journal of General Physiology
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PMC publication ID
3691448
reference URL
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2 March 2020
volume
142
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PMC publication ID
3691448
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2 March 2020
issue
1
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Europe PubMed Central
PMC publication ID
3691448
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retrieved
2 March 2020
page(s)
61-73
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3691448
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retrieved
2 March 2020
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ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
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Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains
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Severed molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH(2)-terminal nucleotide binding domain
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9 September 2017
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Successive openings of the same acetylcholine receptor channel are correlated in open time
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High affinity ATP/ADP analogues as new tools for studying CFTR gating
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The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover
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Block by MOPS reveals a conformation change in the CFTR pore produced by ATP hydrolysis.
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29 September 2017
Involvement of F1296 and N1303 of CFTR in induced-fit conformational change in response to ATP binding at NBD2
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27 June 2018
CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
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27 June 2018
Generation of cAMP-Activated Chloride Currents by Expression of CFTR
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27 June 2018
Identifiers
DOI
10.1085/JGP.201210954
1 reference
stated in
Europe PubMed Central
PMC publication ID
3691448
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 March 2020
PMC publication ID
3691448
1 reference
stated in
Europe PubMed Central
PMC publication ID
3691448
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 March 2020
PubMed publication ID
23752332
1 reference
stated in
Europe PubMed Central
PMC publication ID
3691448
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23752332%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 March 2020
ResearchGate publication ID
237096869
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