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Distinct RGK GTPases differentially use α1- and auxiliary β-binding-dependent mechanisms to inhibit CaV1.2/CaV2.2 channels

PloS one, 2012-05, Vol.7 (5), p.e37079-e37079

2012

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Engineering selectivity into RGK GTPase inhibition of voltage-dependent calcium channels

Proceedings of the National Academy of Sciences - PNAS, 2018-11, Vol.115 (47), p.12051-12056

2018

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hERG 1a LQT2 C-terminus truncation mutants display hERG 1b-dependent dominant negative mechanisms

Heart rhythm, 2016-05, Vol.13 (5), p.1121-1130

2016

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Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaV1.2 channels

Channels (Austin, Tex.), 2016-09, Vol.10 (5), p.379-394

2016

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Engineering Selectivity in RGK Protein Inhibition of Cav1/Cav2 Channels

Biophysical journal, 2015-01, Vol.108 (2), p.578a-578a

Puckerin, Akil

2015

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Similar molecular determinants on Rem mediate two distinct modes of inhibition of Ca V 1.2 channels

Channels (Austin, Tex.), 2016-09, Vol.10 (5), p.379-394

2016

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β-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a β-Arrestin 1-mediated Pathway

The Journal of biological chemistry, 2008-06, Vol.283 (25), p.17221-17226

2008

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Arrestin Is Required for Agonist-induced Trafficking of Voltage-dependent Calcium Channels

The Journal of biological chemistry, 2006-10, Vol.281 (41), p.31131-31141

2006

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Distinct RGK GTPases Differentially Use [alpha].sub.1- and Auxiliary [beta]-Binding-Dependent Mechanisms to Inhibit Ca.sub.V1.2/Ca.sub.V2.2 Channels

PloS one, 2012-05, Vol.7 (5), p.e37079

2012

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Profiling Mechanisms of RGK Inhibition Across the Family of High-Voltage-Activated Cav1/Cav2 Calcium Channels

Biophysical journal, 2014-01, Vol.106 (2), p.329a-329a

2014

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Trafficking and Gating Mechanisms of HERG1A C-Terminus (LQTS-2) Truncation Mutations on HERG1A-HERG1B Hetero-Multimeric Channel

Biophysical journal, 2015-01, Vol.108 (2), p.196a-196a

2015

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Rem Inhibits Cav1.2 Channels using both Beta-Binding Dependent and Independent Mechanisms

Biophysical journal, 2012-01, Vol.102 (3), p.431a-431a

2012

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Perturbation of sodium channel structure by an inherited Long QT Syndrome mutation

Nature communications, 2012-02, Vol.3 (1), p.706-706, Article 706

2012

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Inhibition of Voltage-dependent Calcium Channels by Small G-proteins: Determinants, Mechanisms & Applications

Puckerin, Akil

2015

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Mapping the Structure of the Cardiac Voltage-Gated Sodium Channel (Nav1.5) C-Terminus: Implications of An Lqt3 Mutant

Biophysical journal, 2011-02, Vol.100 (3), p.15a-15a

2011

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Arrestin is required for agonist-induced trafficking of voltage-dependent calcium channels

The Journal of biological chemistry, 2011-06, Vol.286 (24), p.21952-21952

2011

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β-Adrenergic receptor activation induces internalization of cardiac Cav1.2 channel complexes through a β-arrestin 1-mediated pathway

The Journal of biological chemistry, 2011-06, Vol.286 (24), p.21952-21952

2011

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Abstract 5309: beta-Arrestin 1 (bArr1) and Ankyrin 2 (ANK2) Regulate Cav1.2 Trafficking through Complex G Protein Mediated Signaling

Circulation (New York, N.Y.), 2008-10, Vol.118 (suppl_18)

2008

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β-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a β-Arrestin 1-mediated PathwayS

The Journal of biological chemistry, 2008-06, Vol.283 (25), p.17221-17226

2008

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beta -Adrenergic Receptor Activation Induces Internalization of Cardiac Ca sub(v)1.2 Channel Complexes through a beta -Arrestin 1-mediated Pathway

The Journal of biological chemistry, 2008-06, Vol.283 (25), p.17221-17226

2008

Volltextzugriff (PDF)

Î²-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a Î²-Arrestin 1-mediated Pathway

The Journal of biological chemistry, 2008-06, Vol.283 (25), p.17221

2008

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Distinct RGK GTPases differentially use α1- and auxiliary β-binding-dependent mechanisms to inhibit CaV1.2/CaV2.2 channels

Engineering selectivity into RGK GTPase inhibition of voltage-dependent calcium channels

hERG 1a LQT2 C-terminus truncation mutants display hERG 1b-dependent dominant negative mechanisms

Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaV1.2 channels

Engineering Selectivity in RGK Protein Inhibition of Cav1/Cav2 Channels

Similar molecular determinants on Rem mediate two distinct modes of inhibition of Ca V 1.2 channels

β-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a β-Arrestin 1-mediated Pathway

Arrestin Is Required for Agonist-induced Trafficking of Voltage-dependent Calcium Channels

Distinct RGK GTPases Differentially Use [alpha].sub.1- and Auxiliary [beta]-Binding-Dependent Mechanisms to Inhibit Ca.sub.V1.2/Ca.sub.V2.2 Channels

Profiling Mechanisms of RGK Inhibition Across the Family of High-Voltage-Activated Cav1/Cav2 Calcium Channels

Trafficking and Gating Mechanisms of HERG1A C-Terminus (LQTS-2) Truncation Mutations on HERG1A-HERG1B Hetero-Multimeric Channel

Rem Inhibits Cav1.2 Channels using both Beta-Binding Dependent and Independent Mechanisms

Perturbation of sodium channel structure by an inherited Long QT Syndrome mutation

Inhibition of Voltage-dependent Calcium Channels by Small G-proteins: Determinants, Mechanisms & Applications

Mapping the Structure of the Cardiac Voltage-Gated Sodium Channel (Nav1.5) C-Terminus: Implications of An Lqt3 Mutant

Arrestin is required for agonist-induced trafficking of voltage-dependent calcium channels

β-Adrenergic receptor activation induces internalization of cardiac Cav1.2 channel complexes through a β-arrestin 1-mediated pathway

Abstract 5309: beta-Arrestin 1 (bArr1) and Ankyrin 2 (ANK2) Regulate Cav1.2 Trafficking through Complex G Protein Mediated Signaling

β-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a β-Arrestin 1-mediated PathwayS

beta -Adrenergic Receptor Activation Induces Internalization of Cardiac Ca sub(v)1.2 Channel Complexes through a beta -Arrestin 1-mediated Pathway

Î²-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a Î²-Arrestin 1-mediated Pathway

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