Yingjie Liu

发表

S4153R is a gain-of-function mutation in the cardiac Ca(2+) release channel ryanodine receptor associated with catecholaminergic polymorphic ventricular tachycardia and paroxysmal atrial fibrillation.

G. Oudit, P. Zhabyeyev, Florian Hiess, 2013, The Canadian journal of cardiology.

S 4153 R Is a Gain-of-Function Mutation in the Cardiac Ca 2 þ Release Channel Ryanodine Receptor Associated With Catecholaminergic Polymorphic Ventricular Tachycardia and Paroxysmal Atrial Fibrillation

G. Oudit, P. Zhabyeyev, S. Chen, 2013 .

Two pools of IRE1α in cardiac and skeletal muscle cells

Q. Wang, M. Michalak, B. Knollmann, 2019, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

The ryanodine receptor store-sensing gate controls Ca2+ waves and Ca2+-triggered arrhythmias

D. Tieleman, Qiang Zhou, H. Duff, 2014, Nature Medicine.

Red fluorescent genetically encoded Ca2+ indicators for use in mitochondria and endoplasmic reticulum

Robert E. Campbell, Colin W. Taylor, Yi Shen, 2014, The Biochemical journal.

Reduced threshold for store overload-induced Ca2+ release is a common defect of RyR1 mutations associated with malignant hyperthermia and central core disease.

D. Maclennan, R. Dirksen, Wenting Guo, 2017, The Biochemical journal.

Diminished inhibition and facilitated activation of RyR2‐mediated Ca2+ release is a common defect of arrhythmogenic calmodulin mutations

M. Overgaard, Wenting Guo, M. Brohus, 2019, The FEBS journal.

Arrhythmogenic Calmodulin Mutations Affect the Activation and Termination of Cardiac Ryanodine Receptor-mediated Ca2+ Release*

W. Chazin, M. Overgaard, Michael T Overgaard, 2015, The Journal of Biological Chemistry.

Two potential calmodulin-binding sequences in the ryanodine receptor contribute to a mobile, intra-subunit calmodulin-binding domain

T. Wagenknecht, Andrea Koop, Ruiwu Wang, 2013, Journal of Cell Science.

Role of cardiac ryanodine receptor calmodulin‐binding domains in mediating the action of arrhythmogenic calmodulin N‐domain mutation N54I

M. Overgaard, Wenting Guo, Ruiwu Wang, 2019, The FEBS journal.

CPVT-associated cardiac ryanodine receptor mutation G357S with reduced penetrance impairs Ca2+ release termination and diminishes protein expression

F. van Petegem, Ruiwu Wang, Yingjie Liu, 2017, PloS one.

The CPVT-associated RyR2 mutation G230C enhances store overload-induced Ca2+ release and destabilizes the N-terminal domains.

F. van Petegem, Lynn Kimlicka, Florian Hiess, 2013, The Biochemical journal.

Identification of loss-of-function RyR2 mutations associated with idiopathic ventricular fibrillation and sudden death

S. Priori, C. Napolitano, Wenting Guo, 2021, Bioscience reports.

Enhanced Cytosolic Ca2+ Activation Underlies a Common Defect of Central Domain Cardiac Ryanodine Receptor Mutations Linked to Arrhythmias*

Wenting Guo, T. G. Back, Ruiwu Wang, 2016, The Journal of Biological Chemistry.

Calmodulin modulates the termination threshold for cardiac ryanodine receptor-mediated Ca2+ release.

Ruiwu Wang, Yingjie Liu, Yijun Tang, 2013, The Biochemical journal.

The EF-hand Ca2+ Binding Domain Is Not Required for Cytosolic Ca2+ Activation of the Cardiac Ryanodine Receptor*

Wenting Guo, Ruiwu Wang, Yingjie Liu, 2015, The Journal of Biological Chemistry.

The Arrhythmogenic Calmodulin p.Phe142Leu Mutation Impairs C-domain Ca2+ Binding but Not Calmodulin-dependent Inhibition of the Cardiac Ryanodine Receptor*

Michael Fill, Christian Holt, Michael Toft Overgaard, 2016, The Journal of Biological Chemistry.

Ligand-dependent Conformational Changes in the Clamp Region of the Cardiac Ryanodine Receptor*

T. Wagenknecht, Ruiwu Wang, Yingjie Liu, 2012, The Journal of Biological Chemistry.

Generation and Characterization of a Mouse Model Harboring the Exon-3 Deletion in the Cardiac Ryanodine Receptor

James D. Johnson, A. Gillis, Ju Chen, 2014, PloS one.

Roles of the NH2-terminal Domains of Cardiac Ryanodine Receptor in Ca2+ Release Activation and Termination*

F. van Petegem, Wenting Guo, Ruiwu Wang, 2015, The Journal of Biological Chemistry.