MULTILEARNING Group Academy

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Welcome to this demonstration on how Magic Webinar® transforms your slide-based webinar recordings and how our player genuinely strengthens the educational impact of your content
 
The primary feature is our Slide Navigation, which cuts your webinars into easy-to-navigate slides with utmost accuracy. This lets you move forward and back as you please and quickly navigate to slides of interest.

Another great feature is the ability to track your progress. As slide navigation allows you to watch a video in a non-linear way, the slides you've watched are highlighted in green, giving you the ability to resume where you left off. 

Furthermore, Magic Webinar® allows you to search for words of interest, and rather than bring you to the exact time where the word is shown, it brings you to the beginning of the slide where the word is mentioned, providing you with the full context behind the search without having to fiddle with the time slider.

And thanks to the Matching Slides function, Magic Webinar® finds keywords within all related video lectures and stitches them together in a single presentation.

Finally, Magic Webinar® offers you a unique and dynamic opportunity to attract sponsors through short skippable video ads at the beginning of each video lecture.  

With Magic Webinar®, you make the most out of your message and reach your audience in a way they can understand, remember, and enjoy.

Restoration of cardiac intracellular pH (pHi) following acidification is of crucial importance for the maintenance of myocardial contractility. The predominant mechanism responsible for this is the function of the sodium/hydrogen exchanger isoform 1 (NHE1), which is the primary isoform of mammalian myocardium. NHE1 is localized predominantly at the intercalated disks and along the transverse tubular system where it is believed to play an essential role in cardiac pH homeostasis, impulse conductance and excitation-contraction coupling. However, the factors that control the membrane targeting and regulation of NHE1 in heart are poorly understood. Yeast-two hybrid screening identified a cardiac-predominant member of the calcineurin B homologous protein (CHP) family, called CHP3/Tescalcin, that binds directly to the cytoplasmic C-terminal domain of NHE1. However, the functional significance of this interaction has yet to be elucidated. This study undertook biochemical and cellular analysis to determine both the significance of the NHE1-CHP3 complex for pH regulation in cardiac tissue, as well as the significance of calcium-binding in this complex. These studies suggest that CHP3 acts to stabilize the mature form of NHE1 at the plasma membrane, rather than exhibiting a kinetic effect. DiagramDescription automatically generated

This results in higher expression of the exchanger at the cellular membrane, accounting for this increase in exchange activity. Furthermore, the binding of Calcium to the CHP3 protein is crucial for the stability of this NHE1-CHP3 complex, suggesting the CHP3 acts as the calcium-myristoyl switch protein.

 

Restoration of cardiac intracellular pH (pHi) following acidification is of crucial importance for the maintenance of myocardial contractility. The predominant mechanism responsible for this is the function of the sodium/hydrogen exchanger isoform 1 (NHE1), which is the primary isoform of mammalian myocardium. NHE1 is localized predominantly at the intercalated disks and along the transverse tubular system where it is believed to play an essential role in cardiac pH homeostasis, impulse conductance and excitation-contraction coupling. However, the factors that control the membrane targeting and regulation of NHE1 in heart are poorly understood. Yeast-two hybrid screening identified a cardiac-predominant member of the calcineurin B homologous protein (CHP) family, called CHP3/Tescalcin, that binds directly to the cytoplasmic C-terminal domain of NHE1. However, the functional significance of this interaction has yet to be elucidated. This study undertook biochemical and cellular analysis to determine both the significance of the NHE1-CHP3 complex for pH regulation in cardiac tissue, as well as the significance of calcium-binding in this complex. These studies suggest that CHP3 acts to stabilize the mature form of NHE1 at the plasma membrane, rather than exhibiting a kinetic effect. DiagramDescription automatically generated

This results in higher expression of the exchanger at the cellular membrane, accounting for this increase in exchange activity. Furthermore, the binding of Calcium to the CHP3 protein is crucial for the stability of this NHE1-CHP3 complex, suggesting the CHP3 acts as the calcium-myristoyl switch protein.

 
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