Calcium-release channels: structure and function of IP3 receptors and ryanodine receptors
KA Woll, F Van Petegem - Physiological Reviews, 2022 - journals.physiology.org
Ca2+-release channels are giant membrane proteins that control the release of Ca2+ from
the endoplasmic and sarcoplasmic reticulum. The two members, ryanodine receptors …
the endoplasmic and sarcoplasmic reticulum. The two members, ryanodine receptors …
Calcium signaling and endoplasmic reticulum stress
J Groenendyk, LB Agellon, M Michalak - International review of cell and …, 2021 - Elsevier
Cellular homeostasis is essential for healthy functioning of cells and tissues as well as
proper organ development and maintenance. A disruption in cellular homeostasis triggers …
proper organ development and maintenance. A disruption in cellular homeostasis triggers …
[HTML][HTML] Molecular, subcellular, and arrhythmogenic mechanisms in genetic RyR2 disease
ED Fowler, S Zissimopoulos - Biomolecules, 2022 - mdpi.com
The ryanodine receptor (RyR2) has a critical role in controlling Ca2+ release from the
sarcoplasmic reticulum (SR) throughout the cardiac cycle. RyR2 protein has multiple …
sarcoplasmic reticulum (SR) throughout the cardiac cycle. RyR2 protein has multiple …
Chronic intermittent tachypacing by an optogenetic approach induces arrhythmia vulnerability in human engineered heart tissue
M Lemme, I Braren, M Prondzynski… - Cardiovascular …, 2020 - academic.oup.com
Aims Chronic tachypacing is commonly used in animals to induce cardiac dysfunction and to
study mechanisms of heart failure and arrhythmogenesis. Human induced pluripotent stem …
study mechanisms of heart failure and arrhythmogenesis. Human induced pluripotent stem …
The journey of Ca2+ through the cell – pulsing through the network of ER membrane contact sites
Calcium is the third most abundant metal on earth, and the fundaments of its homeostasis
date back to pre-eukaryotic life forms. In higher organisms, Ca2+ serves as a cofactor for a …
date back to pre-eukaryotic life forms. In higher organisms, Ca2+ serves as a cofactor for a …
Calsequestrin, a key protein in striated muscle health and disease
D Rossi, A Gamberucci, E Pierantozzi, C Amato… - Journal of Muscle …, 2021 - Springer
Calsequestrin (CASQ) is the most abundant Ca 2+ binding protein localized in the
sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. The genome of vertebrates …
sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. The genome of vertebrates …
[HTML][HTML] Unbalance Between Sarcoplasmic Reticulum Ca2 + Uptake and Release: A First Step Toward Ca2 + Triggered Arrhythmias and Cardiac Damage
The present review focusses on the regulation and interplay of cardiac SR Ca2+ handling
proteins involved in SR Ca2+ uptake and release, ie, SERCa2/PLN and RyR2. Both RyR2 …
proteins involved in SR Ca2+ uptake and release, ie, SERCa2/PLN and RyR2. Both RyR2 …
Calsequestrin. Structure, function, and evolution
Q Wang, M Michalak - Cell Calcium, 2020 - Elsevier
Calsequestrin is the major Ca 2+ binding protein in the sarcoplasmic reticulum (SR), serves
as the main Ca 2+ storage and buffering protein and is an important regulator of Ca 2+ …
as the main Ca 2+ storage and buffering protein and is an important regulator of Ca 2+ …
Molecular insights into calcium dependent regulation of ryanodine receptor calcium release channels
N Yamaguchi - Calcium Signaling, 2020 - Springer
Ryanodine receptor calcium release channels (RyRs) play central roles in controlling
intracellular calcium concentrations in excitable and non-excitable cells. RyRs are located in …
intracellular calcium concentrations in excitable and non-excitable cells. RyRs are located in …
[HTML][HTML] Pacing Dynamics Determines the Arrhythmogenic Mechanism of the CPVT2-Causing CASQ2G112+5X Mutation in a Guinea Pig Ventricular Myocyte …
Calsequestrin Type 2 (CASQ2) is a high-capacity, low-affinity, Ca2+-binding protein
expressed in the sarcoplasmic reticulum (SR) of the cardiac myocyte. Mutations in CASQ2 …
expressed in the sarcoplasmic reticulum (SR) of the cardiac myocyte. Mutations in CASQ2 …