标题
Regulation of the NaV1.5 cytoplasmic domain by calmodulin
作者
关键词
-
出版物
Nature Communications
Volume 5, Issue 1, Pages -
出版商
Springer Nature
发表日期
2014-11-05
DOI
10.1038/ncomms6126
参考文献
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- (2014) M. Hoshi et al. Circulation-Cardiovascular Genetics
- The structural mechanism of KCNH-channel regulation by the eag domain
- (2013) Yoni Haitin et al. NATURE
- Structural Basis for the Modulation of the Neuronal Voltage-Gated Sodium Channel NaV1.6 by Calmodulin
- (2013) Vishnu Priyanka Reddy Chichili et al. Scientific Reports
- X-ray Structures of Magnesium and Manganese Complexes with the N-Terminal Domain of Calmodulin: Insights into the Mechanism and Specificity of Metal Ion Binding to an EF-Hand
- (2012) F. Timur Senguen et al. BIOCHEMISTRY
- Dominant-negative effect of SCN5A N-terminal mutations through the interaction of Nav1.5 α-subunits
- (2012) Jérôme Clatot et al. CARDIOVASCULAR RESEARCH
- Crystallographic basis for calcium regulation of sodium channels
- (2012) M. F. Sarhan et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Crystal Structure of the Ternary Complex of a NaV C-Terminal Domain, a Fibroblast Growth Factor Homologous Factor, and Calmodulin
- (2012) Chaojian Wang et al. STRUCTURE
- Perturbation of sodium channel structure by an inherited Long QT Syndrome mutation
- (2012) Ian W. Glaaser et al. Nature Communications
- Voltage-Gated Sodium Channels: Biophysics, Pharmacology, and Related Channelopathies
- (2012) Eleonora Savio-Galimberti et al. Frontiers in Pharmacology
- Overview of theCCP4 suite and current developments
- (2011) Martyn D. Winn et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Transforming binding affinities from three dimensions to two with application to cadherin clustering
- (2011) Yinghao Wu et al. NATURE
- Structural and Energetic Determinants of Apo Calmodulin Binding to the IQ Motif of the NaV1.2 Voltage-Dependent Sodium Channel
- (2011) Michael D. Feldkamp et al. STRUCTURE
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Solution NMR Structure of Apo-Calmodulin in Complex with the IQ Motif of Human Cardiac Sodium Channel NaV1.5
- (2010) Benjamin Chagot et al. JOURNAL OF MOLECULAR BIOLOGY
- Long-term inactivation particle for voltage-gated sodium channels
- (2010) Katarzyna Dover et al. JOURNAL OF PHYSIOLOGY-LONDON
- Calcium-Mediated Dual-Mode Regulation of Cardiac Sodium Channel Gating
- (2009) Subrata Biswas et al. CIRCULATION RESEARCH
- Solution Structure of the NaV1.2 C-terminal EF-hand Domain
- (2009) Vesselin Z. Miloushev et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A Double Tyrosine Motif in the Cardiac Sodium Channel Domain III-IV Linker Couples Calcium-dependent Calmodulin Binding to Inactivation Gating
- (2009) Maen F. Sarhan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Crystal contacts as nature's docking solutions
- (2009) Evgeny Krissinel JOURNAL OF COMPUTATIONAL CHEMISTRY
- Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
- (2009) N. Jura et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Solution NMR Structure of the C-terminal EF-hand Domain of Human Cardiac Sodium Channel NaV1.5
- (2008) Benjamin Chagot et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Calmodulin Regulation of NaV1.4 Current: Role of Binding to the Carboxyl Terminus
- (2008) Subrata Biswas et al. JOURNAL OF GENERAL PHYSIOLOGY
- SCN5A channelopathies – An update on mutations and mechanisms
- (2008) Thomas Zimmer et al. PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
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