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

Bibliográfalaš dieđut
Váldodahkkit:	Tsuboi, T, Lippiat, J, Ashcroft, F, Rutter, G
Materiálatiipa:	Conference item
Almmustuhtton:	2003

Geahča maid

ATP-dependent interaction of the cytosolic domains of the inwardly rectifying K+ channel Kir6.2 revealed by fluorescence resonance energy transfer.
Dahkki: Tsuboi, T, et al.
Almmustuhtton: (2004)

Interaction of the cytosolic domains of the Kir6.2 subunit of the K(ATP) channel is modulated by sulfonylureas.
Dahkki: Lippiat, J, et al.
Almmustuhtton: (2002)

Time-dependent activation of Kir6.2/SUR2A channels but not Kir6.2/SUR1 channels in the presence of ATP
Dahkki: Ashcroft, F, et al.
Almmustuhtton: (2001)

Time-dependent activation of KIR6.2/SUR2A channels but not KIR6.2/SUR1 channels in the presence of MgATP
Dahkki: Song, D, et al.
Almmustuhtton: (2001)

Glimepiride block of Kir6.2/SUR1 Kir6.2/SUR2A and Kir6.2/SUR2A and Kir6.2/SUR2B K-ATP channels.
Dahkki: Ashcroft, F, et al.
Almmustuhtton: (2001)

Mapping the architecture of the ATP-binding site of Kir6.2
Dahkki: Dabrowski, M, et al.
Almmustuhtton: (2002)

Effects of mitiglinide (S 21403) on Kir6.2/SUR1, Kir6.2/SUR2A and Kir6.2/SUR2B types of ATP-sensitive potassium channel.
Dahkki: Reimann, F, et al.
Almmustuhtton: (2001)

Identification of residues contributing to the ATP binding site of Kir6.2.
Dahkki: Trapp, S, et al.
Almmustuhtton: (2003)

The role of lysine 185 in the kir6.2 subunit of the ATP-sensitive channel in channel inhibition by ATP.
Dahkki: Reimann, F, et al.
Almmustuhtton: (1999)

Kir6.2-dependent high-affinity repaglinide binding to beta-cell K(ATP) channels.
Dahkki: Hansen, A, et al.
Almmustuhtton: (2005)

Involvement of the N-terminus of Kir6.2 in the inhibition of the KATP channel by ATP.
Dahkki: Proks, P, et al.
Almmustuhtton: (1999)

Mapping the architecture of the ATP-binding site of the KATP channel subunit Kir6.2.
Dahkki: Dabrowski, M, et al.
Almmustuhtton: (2004)

Focus on Kir6.2: a key component of the ATP-sensitive potassium channel.
Dahkki: Haider, S, et al.
Almmustuhtton: (2005)

Screening for mutations in the Kir6.2 subunit of the beta-cell K-ATP channel
Dahkki: Sakura, H, et al.
Almmustuhtton: (1996)

Direct photoaffinity labeling of the Kir6.2 subunit of the ATP-sensitive K+ channel by 8-azido-ATP.
Dahkki: Tanabe, K, et al.
Almmustuhtton: (1999)

Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor.
Dahkki: Tucker, S, et al.
Almmustuhtton: (1997)

A novel SUR1/Kir6.2 specific K-ATP channel opener
Dahkki: Dabrowski, M, et al.
Almmustuhtton: (2001)

Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
Dahkki: Deacon, R, et al.
Almmustuhtton: (2006)

Behavioral phenotyping of mice lacking the K ATP channel subunit Kir6.2.
Dahkki: Deacon, R, et al.
Almmustuhtton: (2006)

Molecular basis of Kir6.2 mutations associated with neonatal diabetes or neonatal diabetes plus neurological features.
Dahkki: Proks, P, et al.
Almmustuhtton: (2004)

Direct photoaffinity labeling of Kir6.2 by [gamma-(32)P]ATP-[gamma]4-azidoanilide.
Dahkki: Tanabe, K, et al.
Almmustuhtton: (2000)

Mutations within the P-loop of Kir6.2 modulate the intraburst kinetics of the ATP-sensitive potassium channel.
Dahkki: Proks, P, et al.
Almmustuhtton: (2001)

Nucleotide modulation of pinacidil stimulation of the cloned K(ATP) channel Kir6.2/SUR2A.
Dahkki: Gribble, F, et al.
Almmustuhtton: (2000)

Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.
Dahkki: Antcliff, J, et al.
Almmustuhtton: (2005)

An in-frame deletion in Kir6.2 (KCNJ11) causing neonatal diabetes reveals a site of interaction between Kir6.2 and SUR1.
Dahkki: Craig, T, et al.
Almmustuhtton: (2009)

Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
Dahkki: Tucker, S, et al.
Almmustuhtton: (1999)

Structure-function studies of the fast gating kinetics of the cloned ATP-sensitive potassium channel, Kir6.2/SUR1
Dahkki: Proks, P, et al.
Almmustuhtton: (2001)

Kir6.2 mutations causing neonatal diabetes provide new insights into Kir6.2-SUR1 interactions.
Dahkki: Tammaro, P, et al.
Almmustuhtton: (2005)

A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit.
Dahkki: Tammaro, P, et al.
Almmustuhtton: (2007)

Multiple sites of interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2.
Dahkki: Jones, P, et al.
Almmustuhtton: (2001)

Overlapping distribution of K(ATP) channel-forming Kir6.2 subunit and the sulfonylurea receptor SUR1 in rodent brain.
Dahkki: Karschin, C, et al.
Almmustuhtton: (1997)

Phentolamine block of KATP channels is mediated by Kir6.2.
Dahkki: Proks, P, et al.
Almmustuhtton: (1997)

The Kir6.2-F333I mutation differentially modulates K-ATP channels composed of SUR1 or SUR2 subunits
Dahkki: Tammaro, P, et al.
Almmustuhtton: (2007)

The Kir6.2-F333I mutation differentially modulates K ATP channels composed of SUR1 and SUR2 subunits
Dahkki: Tammaro, P, et al.
Almmustuhtton: (2007)

Involvement of the n-terminus of Kir6.2 in coupling to the sulphonylurea receptor.
Dahkki: Reimann, F, et al.
Almmustuhtton: (1999)

The N-terminus of Kir6.2 is involved in coupling to SUR1
Dahkki: Reimann, F, et al.
Almmustuhtton: (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.
Dahkki: Hansen, A, et al.
Almmustuhtton: (2003)

A mouse model of neonatal diabetes caused by the K-ATP channel mutation Kir6.2-V59M
Dahkki: Girard, C, et al.
Almmustuhtton: (2008)

The first clinical case of a mutation at residue K185 of Kir6.2 (KCNJ11): a major ATP-binding residue.
Dahkki: Shimomura, K, et al.
Almmustuhtton: (2010)

Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes.
Dahkki: Gloyn, A, et al.
Almmustuhtton: (2004)