NMR Analysis of KChIP4a Reveals Structural Basis for Control of Surface Expression of Kv4 Channel Complexes
Open Access
- 1 July 2008
- journal article
- Published by Elsevier
- Vol. 283 (27) , 18937-18946
- https://doi.org/10.1074/jbc.m800976200
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Three-dimensional structure of the KChIP1–Kv4.3 T1 complex reveals a cross-shaped octamerNature Structural & Molecular Biology, 2006
- NMR-Derived Dynamic Aspects of N-Type Inactivation of a Kv Channel Suggest a Transient Interaction with the T1 DomainBiochemistry, 2006
- SWISS-MODEL: an automated protein homology-modeling serverNucleic Acids Research, 2003
- HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical InformationJournal of the American Chemical Society, 2003
- Remodelling inactivation gating of Kv4 channels by KChIP1, a small‐molecular‐weight calcium‐binding proteinThe Journal of Physiology, 2002
- Prediction of Sterically Induced Alignment in a Dilute Liquid Crystalline Phase: Aid to Protein Structure Determination by NMRJournal of the American Chemical Society, 2000
- TROSY-type Triple-Resonance Experiments for Sequential NMR Assignments of Large ProteinsJournal of the American Chemical Society, 1999
- Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR SpectraJournal of Magnetic Resonance, 1998
- Characterizing the Use of Perdeuteration in NMR Studies of Large Proteins:13C,15N and1H Assignments of Human Carbonic Anhydrase IIJournal of Molecular Biology, 1996
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996