Results 31 to 40 of about 31,472 (217)

Single-particle cryo-EM of the ryanodine receptor channel

open access: yesEuropean Journal of Translational Myology, 2015
Ryanodine receptors (RyRs) are tetrameric ligand-gated Ca2+ release channels that are responsible for the increase of cytosolic Ca2+ concentration leading to muscle contraction.
Mariah R. Baker   +2 more
doaj   +1 more source

CaV1 and CaV2 calcium channels mediate the release of distinct pools of synaptic vesicles

open access: yeseLife, 2023
Activation of voltage-gated calcium channels at presynaptic terminals leads to local increases in calcium and the fusion of synaptic vesicles containing neurotransmitter.
Brian D Mueller   +12 more
doaj   +1 more source

Dysregulation of RyR Calcium Channel Causes the Onset of Mitochondrial Retrograde Signaling

open access: yesiScience, 2020
Summary: This study shows that multiple modes of mitochondrial stress generated by partial mtDNA depletion or cytochrome c oxidase disruption cause ryanodine receptor channel (RyR) dysregulation, which instigates the release of Ca2+ in the cytoplasm of ...
Anindya Roy Chowdhury   +4 more
doaj   +1 more source

Loss of dysferlin or myoferlin results in differential defects in excitation–contraction coupling in mouse skeletal muscle

open access: yesScientific Reports, 2021
Muscular dystrophies are disorders characterized by progressive muscle loss and weakness that are both genotypically and phenotypically heterogenous. Progression of muscle disease arises from impaired regeneration, plasma membrane instability, defective ...
David Y. Barefield   +5 more
doaj   +1 more source

MG53 suppresses interferon-β and inflammation via regulation of ryanodine receptor-mediated intracellular calcium signaling

open access: yesNature Communications, 2020
TRIM proteins are known to play critical roles in the context of viral infection. Here the authors establish MG53 (TRIM72) suppresses IFN and inflammation by modulation of ryanodine receptor related intracellular calcium induction.
Matthew Sermersheim   +11 more
doaj   +1 more source

Kinetics and mapping of Ca-driven calmodulin conformations on skeletal and cardiac muscle ryanodine receptors

open access: yesNature Communications
Calmodulin transduces [Ca2+] information regulating the rhythmic Ca2+ cycling between the sarcoplasmic reticulum and cytoplasm during contraction and relaxation in cardiac and skeletal muscle.
Robyn T. Rebbeck   +6 more
doaj   +1 more source

Additive‐Manufactured, Multifunctional Bioreactor Technology for Dynamic Culture of 3D Bioprinted Tissue Models

open access: yesAdvanced Materials Technologies, EarlyView.
We introduce an additively manufactured bioreactor with a perfusion flow system and integrated temperature and pH sensors for skeletal muscle tissue biofabrication. The bioreactor's performance was evaluated by assessing the viability, spreading of the myoblast cells in a printed scaffold, and contraction of the isolated murine musculi interossei ...
Lys Sprenger   +9 more
wiley   +1 more source

Calcium-induced calcium release and type 3 ryanodine receptors modulate the slow afterhyperpolarising current, sIAHP, and its potentiation in hippocampal pyramidal neurons.

open access: yesPLoS ONE, 2020
The slow afterhyperpolarising current, sIAHP, is a Ca2+-dependent current that plays an important role in the late phase of spike frequency adaptation.
Angelo Tedoldi   +5 more
doaj   +1 more source

The E3 Ligase RNF115 Aggravates Pathological Cardiac Hypertrophy via Ubiquitin‐Mediated Degradation of SPTBN1

open access: yesAdvanced Science, EarlyView.
In response to hypertrophic stimuli, increased c‑JUN phosphorylation upregulates RNF115, leading to SPTBN1 ubiquitination and degradation. which promotes F‑actin depolymerization and YAP activation, driving cardiac hypertrophy. The RNF115 inhibitor DTD effectively suppresses SPTBN1 ubiquitination and cardiac hypertrophy.
Yan Zu   +12 more
wiley   +1 more source

Presenilin-ryanodine receptor connection [PDF]

open access: yesProceedings of the National Academy of Sciences, 2013
The Presenilins (PS) gene family is composed of two members: PS1 and PS2. Mutations in PSs are linked to familial Alzheimer's disease (FAD) (1). PSs are the catalytic subunits of the γ-secretase multimolecular complex, which mediates the intramembranous cleavage of many type I membrane proteins, including amyloid precursor protein (APP) and Notch (2, 3)
Luciano, D'Adamio, Pablo E, Castillo
openaire   +2 more sources

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