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Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.
scientific article published on 2 August 2007
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Europe PubMed Central
PMC publication ID
1952224
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17673911%20AND%20SRC:MED&resulttype=core&format=json
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3 January 2020
title
Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis
(English)
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1952224
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3 January 2020
author
Shozeb Haider
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1
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1952224
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3 January 2020
Andrei I Tarasov
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2
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1952224
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3 January 2020
Tim J Craig
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3
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1952224
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3 January 2020
Mark S.P. Sansom
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4
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3 January 2020
author name string
Frances M Ashcroft
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5
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1952224
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3 January 2020
language of work or name
English
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publication date
2 August 2007
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Europe PubMed Central
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1952224
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3 January 2020
published in
The EMBO Journal
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1952224
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3 January 2020
volume
26
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3 January 2020
issue
16
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1952224
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3 January 2020
page(s)
3749-3759
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Europe PubMed Central
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1952224
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3 January 2020
describes a project that uses
molecular modelling
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A novel KCNJ11 mutation associated with congenital hyperinsulinism reduces the intrinsic open probability of beta-cell ATP-sensitive potassium channels
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Focus on Kir6.2: a key component of the ATP-sensitive potassium channel
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Conformational dynamics of the ligand-binding domain of inward rectifier K channels as revealed by molecular dynamics simulations: toward an understanding of Kir channel gating.
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Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.
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Stabilization of the activity of ATP-sensitive potassium channels by ion pairs formed between adjacent Kir6.2 subunits
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Crystal structure of the potassium channel KirBac1.1 in the closed state
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Specificity of activation by phosphoinositides determines lipid regulation of Kir channels
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Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution
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Alterations in conserved Kir channel-PIP2 interactions underlie channelopathies
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Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma
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Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor
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Anionic phospholipids activate ATP-sensitive potassium channels
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Cloning and functional expression of the cDNA encoding a novel ATP-sensitive potassium channel subunit expressed in pancreatic beta-cells, brain, heart and skeletal muscle
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Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate
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The C42R mutation in the Kir6.2 (KCNJ11) gene as a cause of transient neonatal diabetes, childhood diabetes, or later-onset, apparently type 2 diabetes mellitus.
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Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
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Phosphatidylinositol 4,5-bisphosphate (PIP2) modulation of ATP and pH sensitivity in Kir channels. A tale of an active and a silent PIP2 site in the N terminus
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16 August 2018
Compromised ATP binding as a mechanism of phosphoinositide modulation of ATP-sensitive K+ channels
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Phospholipids as modulators of K(ATP) channels: distinct mechanisms for control of sensitivity to sulphonylureas, K(+) channel openers, and ATP.
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Molecular dynamics simulations of inwardly rectifying (Kir) potassium channels: a comparative study
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12 December 2020
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Molecular dynamics with coupling to an external bath
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Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
1 reference
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https://api.crossref.org/works/10.1038%2FSJ.EMBOJ.7601809
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based on heuristic
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PROCHECK: a program to check the stereochemical quality of protein structures
1 reference
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Crossref
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https://api.crossref.org/works/10.1038%2FSJ.EMBOJ.7601809
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GROMACS 3.0: a package for molecular simulation and trajectory analysis
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Identifiers
DOI
10.1038/SJ.EMBOJ.7601809
1 reference
stated in
Europe PubMed Central
PMC publication ID
1952224
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17673911%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 January 2020
PMC publication ID
1952224
1 reference
stated in
Europe PubMed Central
PMC publication ID
1952224
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17673911%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 January 2020
PubMed publication ID
17673911
1 reference
stated in
Europe PubMed Central
PMC publication ID
1952224
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17673911%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 January 2020
ResearchGate publication ID
6165289
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