- H Bonding at the Helix-Bundle Crossing Controls Gating in Kir Potassium Channels
- Ion Mobility Mass Spectrometry of Two Tetrameric Membrane Protein Complexes Reveals Compact Structures and Differences in Stability and
- 1992 Oxford University Press Human Molecular Genetics, Vol. 1, No. 2 77--82 Identification and developmental expression of the
- TheJournalofGeneralPhysiology 2008 Tucker and Baukrowitz
- A NOVEL KCNA1 MUTATION IDENTIFIED IN AN ITALIAN FAMILY AFFECTED BY EPISODIC ATAXIA TYPE 1
- Non-equivalent cooperation between the two nucleotide-binding folds of P-glycoprotein
- University departmentsColleges and Halls University museums, libraries and places of interest
- FEBS 17244 FEBS Letters 390 (1996) 253-257 Heteromeric channel formation and Ca2
- Genetic Inactivation of Kcnj16 Identifies Kir5.1 as an Important Determinant of Neuronal PCO2/pH Sensitivity*
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- A touching case of channel regulation: the ATP-sensitive Stephen J Tucker and Frances M Ashcroft
- ATP-sensitive potassium (KATP) channels are found in pancreatic _cells, heart, smooth and skeletal muscle and
- Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels
- DOI: 10.1002/cbic.200800133 Peptide Backbone Mutagenesis of Putative Gating Hinges in a Potassium
- Conformational Changes During the Gating of a Potassium Channel Revealed
- Long Chain CoA Esters as Competitive Antagonists of Phosphatidylinositol 4,5-Bisphosphate Activation in Kir Channels*
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- The EMBO Journal Vol.18 No.4 pp.847853, 1999 Inward rectification in KATP channels: a pH switch in
- The EMBO Journal Vol.17 No.12 pp.32903296, 1998 Molecular determinants of KATP channel inhibition
- Direct Photoaffinity Labeling of the Kir6.2 Subunit of the
- Inhibitory Interactions between Two Inward Rectifier K Channel Subunits Mediated by the Transmembrane Domains*
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- Supplementary Information A dominant-negative mutation in the TRESK potassium channel
- Supporting Information: Ion mobility mass spectrometry of two tetrameric membrane protein complexes
- SupplementaryFigure1 SLIDE-HELIX_TM1_PORE-HELIX__
- Channels 4:5, 390-397; September/October 2010; 2010 Landes Bioscience ReSeaRCh papeR
- Structure 18 Supplemental Information
- Kir5.1 underlies long-lived subconductance levels in heteromeric Kir4.1/Kir5.1 channels from Xenopus tropicalis
- 2007LANDESBIOSCIENCE.DONOTDISTRIBUTE. [Channels 1:5, e1-e4, EPUB Ahead of Print: http://www.landesbioscience.com/journals/channels/article/5186; September/October 2007]; 2007 Landes Bioscience
- Khalili, K., Del Valle, L., Muralidharan, V., Gault, W.J., Darbinian, N., Otte, J., Meier,
- CALL FOR PAPERS Comparative Genomics Cloning and functional characterization of a superfamily of microbial
- Structural and functional analysis of the putative pH sensor in the Kir1.1 (ROMK) potassium channel
- NEM modication prevents high-anity ATP binding to the rst nucleotide binding fold of the sulphonylurea receptor, SUR1
- ATP-sensitive potassium (KATP) channels are found in pancreatic _cells, cardiac, smooth and skeletal muscles, and
- The ATP-sensitive potassium channel (KATP) serves to couple the metabolic status of the cell to its electrical
- the membrane, and they provide a mechanis-tic framework for understanding the hallmark
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- Sulphonylureas, such as tolbutamide and glibenclamide, are widely used to treat non-insulin-dependent diabetes
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- Short Communication Functional characterisation of missense variations in the Kir4.1 potassium
- Inward Rectifier Potassiwn Channels Cloning, Expression and Structure~FunctionStudies
- Activatory mutations in KcsA www.landesbioscience.com Channels 413
- 1412 DIABETES, VOL. 47, SEPTEMBER 1998 Tissue Specificity of Sulfonylureas
- Functional Complementation and Genetic Deletion Studies of KirBac Channels
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- Renal phenotype in mice lacking the Kir5.1 (Kcnj16) channel subunit contrasts with that observed in
- Molecular Dynamics Simulations of Inwardly Rectifying (Kir) Potassium Channels: A Comparative Study
- Intrinsic Sensitivity of Kir1.1 (ROMK) to Glibenclamide in the Absence of SUR2B
- Abstract The activity of voltage-gated potassium (Kv) channels can be dynamically modulated by several
- pH Dependence of the Inwardly Rectifying Potassium Channel,
- A Novel Method for Measurement of Submembrane ATP Concentration*
- Inwardly rectifying potassium (Kir) channels are found in almost every cell type where they play key roles in
- Cystic Fibrosis Transmembrane Conductance Regulator-dependent Up-regulation of Kir1.1 (ROMK) Renal K Channels by the
- Direct Photoaffinity Labeling of Kir6.2 P]ATP-[ ]4-Azidoanilide
- The pore structure and gating mechanism of K2P Paula L Piechotta1,7
- Identification of a Heteromeric Interaction That Influences the Rectification, Gating, and pH Sensitivity of Kir4.1/Kir5.1
- KvAP1ORQ MthK3LDC Kv12R9R Supplementary Figure S1: Detailed view of TPenA docked into the 3 bestfit
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