Engineering selectivity into RGK GTPase inhibition of voltage-dependent calcium channels von Puckerin, Akil A., Chang, Donald D., Shuja, Zunaira, Choudhury, Papiya, Scholz, Joachim, Colecraft, Henry M.

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Distinct RGK GTPases differentially use α1- and auxiliary β-binding-dependent mechanisms to inhibit CaV1.2/CaV2.2 channels von Yang, Tingting, Puckerin, Akil, Colecraft, Henry M

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hERG 1a LQT2 C-terminus truncation mutants display hERG 1b-dependent dominant negative mechanisms von Puckerin, Akil, PhD, Aromolaran, Kelly A., PhD, Chang, Donald D., PhD, Zukin, R. Suzanne, PhD, Colecraft, Henry M., PhD, Boutjdir, Mohamed, PhD, Aromolaran, Ademuyiwa S., PhD

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Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaV1.2 channels von Puckerin, Akil A., Chang, Donald D., Subramanyam, Prakash, Colecraft, Henry M.

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Engineering Selectivity in RGK Protein Inhibition of Cav1/Cav2 Channels von Puckerin, Akil

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Similar molecular determinants on Rem mediate two distinct modes of inhibition of Ca V 1.2 channels von Puckerin, Akil A, Chang, Donald D, Subramanyam, Prakash, Colecraft, Henry M

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β-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a β-Arrestin 1-mediated Pathway von Lipsky, Rachele, Potts, Essie M., Tarzami, Sima T., Puckerin, Akil A., Stocks, Joanne, Schecter, Alison D., Sobie, Eric A., Akar, Fadi G., Diversé-Pierluissi, María A.

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Arrestin Is Required for Agonist-induced Trafficking of Voltage-dependent Calcium Channels von Puckerin, Akil, Liu, Lanying, Permaul, Natasha, Carman, Paul, Lee, Jessica, Diversé-Pierluissi, María A.

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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 von Yang, Tingting, Puckerin, Akil, Colecraft, Henry M

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Profiling Mechanisms of RGK Inhibition Across the Family of High-Voltage-Activated Cav1/Cav2 Calcium Channels von Puckerin, Akil A., Chang, Donald D., Colecraft, Henry M.

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Trafficking and Gating Mechanisms of HERG1A C-Terminus (LQTS-2) Truncation Mutations on HERG1A-HERG1B Hetero-Multimeric Channel von Puckerin, Akil, Chang, Donald D., Subramanyam, Prakash, Colecraft, Henry M., Aromolaran, Ademuyiwa S.

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Rem Inhibits Cav1.2 Channels using both Beta-Binding Dependent and Independent Mechanisms von Yang, Tingting, Puckerin, Akil, He, Lin-ling, Colecraft, Henry

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Perturbation of sodium channel structure by an inherited Long QT Syndrome mutation von Glaaser, Ian W., Osteen, Jeremiah D., Puckerin, Akil, Sampson, Kevin J., Jin, Xiangshu, Kass, Robert S.

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Mapping the Structure of the Cardiac Voltage-Gated Sodium Channel (Nav1.5) C-Terminus: Implications of An Lqt3 Mutant von Glaaser, Ian W., Osteen, Jeremiah D., Puckerin, Akil, Kass, Robert S.

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Arrestin is required for agonist-induced trafficking of voltage-dependent calcium channels von Puckerin, Akil, Liu, Lanying, Permaul, Natasha, Carman, Paul, Lee, Jessica, Diversé-Pierluissi, María A.

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β-Adrenergic receptor activation induces internalization of cardiac Cav1.2 channel complexes through a β-arrestin 1-mediated pathway von Lipsky, Rachele, Potts, Essie M., Tarzami, Sima T., Puckerin, Akil A., Stocks, Joanne, Schecter, Alison D., Sobie, Eric A., Akar, Fadi G., Diversé-Pierluissi, María A.

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Abstract 5309: beta-Arrestin 1 (bArr1) and Ankyrin 2 (ANK2) Regulate Cav1.2 Trafficking through Complex G Protein Mediated Signaling von Diverse-Pierluissi, Maria A, Lipsky, Rachele, Puckerin, Akil A, Stocks, Joanne, Patel, Vivek, Akar, Fadi G

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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 von Lipsky, Rachele, Potts, Essie M, Tarzami, Sima T, Puckerin, Akil A, Stocks, Joanne, Schecter, Alison D, Sobie, Eric A, Akar, Fadi G, Diverse-Pierluissi, Maria A

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β-Adrenergic Receptor Activation Induces Internalization of Cardiac Cav1.2 Channel Complexes through a β-Arrestin 1-mediated Pathway von Rachele Lipsky, Essie M. Potts, Sima T. Tarzami, Akil A. Puckerin, Joanne Stocks, Alison D. Schecter, Eric A. Sobie, Fadi G. Akar, María A. Diversé-Pierluissi

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