Results 41 to 50 of about 21,278 (246)

Computational evidence for protein-mediated fatty acid transport across the sarcolemma [PDF]

open access: yes, 2006
Long-chain fatty acids (FAs) are important substrates used by the heart to fulfil its energy requirements. Prior to mitochondrial oxidation, blood-borne FAs must pass through the cell membrane of the cardiac myocyte (sarcolemma). The mechanism underlying
Vusse, van der, G.J.   +4 more
core   +1 more source

Nanodysferlins support membrane repair and binding to TRIM72/MG53 but do not localize to t-tubules or stabilize Ca2+ signaling

open access: yesMolecular Therapy: Methods & Clinical Development
Mutations in the DYSF gene, encoding the protein dysferlin, lead to several forms of muscular dystrophy. In healthy skeletal muscle, dysferlin concentrates in the transverse tubules and is involved in repairing the sarcolemma and stabilizing Ca2 ...
Joaquin Muriel   +10 more
doaj   +1 more source

Light‐Driven Quadrupedal Walking Biohybrid Robot With Antagonistic Muscle‐Rings and Inclined Joints

open access: yesAdvanced Robotics Research, EarlyView.
This work presents a light‐driven quadrupedal walking biohybrid robot powered by antagonistic muscle‐rings that achieve alternating walking gait. Optical training improved reproducibility of cultured muscle tissues, while caffeine treatment enhanced contractile force.
Shotaro Saito   +5 more
wiley   +1 more source

Effects of myofiber isolation technique on sarcolemma biomechanics

open access: yesBioTechniques, 2020
Isolated myofibers are commonly used to understand the function of skeletal muscle in vivo. This can involve single isolated myofibers obtained from dissection or from enzymatic dissociation.
Karla P Garcia-Pelagio   +2 more
doaj   +1 more source

Proteomics characterization of the cardiac sarcolemma [PDF]

open access: yes, 2006
As the plasma membrane of the cardiac muscle cell (sarcolemma) plays a major role in the cardiac physiology and homeostasis, the aim of this study is to identify using mass spectrometry (MS) and data base mining the integral and peripheral proteins that ...
Elghawanmeh, Omar.
core  

Immunohistochemical demonstration of the binding of bothrops asper myotoxin to skeletal muscle sarcolemma [PDF]

open access: yes, 1987
The binding of Bothrops asper myotoxin to mouse skeletal muscle was studied at both the light and electron microscope levels using the peroxidase anti-peroxidase technique. The toxin binds to muscle cell sarcolemma, and there are no intracellular binding
Lomonte, Bruno   +2 more
core   +1 more source

Small-conductance Ca<sup>2</sup>⁺-activated K⁺ channels in cardiac excitation-contraction coupling: Bridging mitochondria, sarcolemma and antiarrhythmic therapy. [PDF]

open access: yesJ Physiol
Abstract figure legend Mitochondrial SK channel enhancement reduces cardiac arrhythmia trigger. Spontaneous sarcoplasmic reticulum (SR) Ca2+ release via hyperactive RyR2s underlies an increased arrhythmia trigger, promoting early and delayed afterdepolarizations during stress. Hyperactive RyR2s causes rise in cytosolic [Ca2+] during diastole. Clearance
Terentyev D   +7 more
europepmc   +2 more sources

Enhancing Maturation of Human Neuromuscular Organoids via Electrical Stimulation

open access: yesAdvanced Science, EarlyView.
A framework for on‐demand and non‐invasive exposure of human neuromuscular organoids (NMOs) to electrical stimuli is established to promote their maturation. The robustness and effectiveness of different stimulation regimes are evaluated via thorough characterization of organoid tissue structure and contraction capacity. Chronic electrical stimulation,
Chrysanthi‐Maria Moysidou   +12 more
wiley   +1 more source

TAURINE AND THE CARDIAC SARCOLEMMA. [PDF]

open access: yes, 1987
Taurine is by far the most abundant of the sulfur amino acids, levels in the heart exceeding the combined quantities of all others. Taurine exhibits extensive cardiovascular pharmacology, including inotropic and antiarrhythmic properties.
SEBRING, LESLIE ANN.
core  

Absence of aquaporin-4 in skeletal muscle alters proteins involved in bioenergetic pathways and calcium handling. [PDF]

open access: yesPLoS ONE, 2011
Aquaporin-4 (AQP4) is a water channel expressed at the sarcolemma of fast-twitch skeletal muscle fibers, whose expression is altered in several forms of muscular dystrophies.
Davide Basco   +5 more
doaj   +1 more source

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