ATP-dependent interaction of the cytosolic domains of Kir6.2 revealed by fluorescence resonance energy transfer

ATP-dependent interaction of the cytosolic domains of Kir6.2 revealed by fluorescence resonance energy transfer

Podrobná bibliografie
Hlavní autoři:	Tsuboi, T, Lippiat, J, Ashcroft, F, Rutter, G
Médium:	Conference item
Vydáno:	2003

Podobné jednotky

ATP-dependent interaction of the cytosolic domains of the inwardly rectifying K+ channel Kir6.2 revealed by fluorescence resonance energy transfer.
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Identification of residues contributing to the ATP binding site of Kir6.2.
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The role of lysine 185 in the kir6.2 subunit of the ATP-sensitive channel in channel inhibition by ATP.
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Involvement of the N-terminus of Kir6.2 in the inhibition of the KATP channel by ATP.
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Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
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Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.
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Screening for mutations in the Kir6.2 subunit of the beta-cell K-ATP channel
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Vydáno: (1996)

Direct photoaffinity labeling of the Kir6.2 subunit of the ATP-sensitive K+ channel by 8-azido-ATP.
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Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor.
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A novel SUR1/Kir6.2 specific K-ATP channel opener
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Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
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Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
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Molecular basis of Kir6.2 mutations associated with neonatal diabetes or neonatal diabetes plus neurological features.
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Direct photoaffinity labeling of Kir6.2 by [gamma-(32)P]ATP-[gamma]4-azidoanilide.
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Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel.
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Nucleotide modulation of pinacidil stimulation of the cloned K(ATP) channel Kir6.2/SUR2A.
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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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An in-frame deletion in Kir6.2 (KCNJ11) causing neonatal diabetes reveals a site of interaction between Kir6.2 and SUR1.
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Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
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Structure-function studies of the fast gating kinetics of the cloned ATP-sensitive potassium channel, Kir6.2/SUR1
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Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.
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A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.
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Multiple sites of interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
Autor: Jones, P, a další
Vydáno: (2001)

Overlapping distribution of K(ATP) channel-forming Kir6.2 subunit and the sulfonylurea receptor SUR1 in rodent brain.
Autor: Karschin, C, a další
Vydáno: (1997)

Phentolamine block of KATP channels is mediated by Kir6.2.
Autor: Proks, P, a další
Vydáno: (1997)

The Kir6.2-F333I mutation differentially modulates K-ATP channels composed of SUR1 or SUR2 subunits
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Vydáno: (2007)

The Kir6.2-F333I mutation differentially modulates K ATP channels composed of SUR1 and SUR2 subunits
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Vydáno: (2007)

Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
Autor: Reimann, F, a další
Vydáno: (1999)

The N-terminus of Kir6.2 is involved in coupling to SUR1
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Vydáno: (1999)

Functional coupling between Kir6.2 and SUR1 is prerequisite for [H-3]repaglinide, but not [H-3]glibenclamide, binding to pancreatic ATP-sensitive potassium (K-ATP) channels.
Autor: Hansen, A, a další
Vydáno: (2003)

A mouse model of neonatal diabetes caused by the K-ATP channel mutation Kir6.2-V59M
Autor: Girard, C, a další
Vydáno: (2008)

The first clinical case of a mutation at residue K185 of Kir6.2 (KCNJ11): a major ATP-binding residue.
Autor: Shimomura, K, a další
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Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes.
Autor: Gloyn, A, a další
Vydáno: (2004)