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For over a decade, MULTILEARNING has helped hundreds of In-Person event organizers embrace ePosters and get the thumbs-up from delegates and authors.

With the move to virtual and hybrid events, poster sessions can get “hidden away” and lose their vitality. Thanks to multilearning eposter solution you can put Poster Sessions back on center-stage during your Virtual & Hybrid Events.

We offer a complete and robust solution composed of the following elements: 

INTERACTIVE ePOSTERS WITH AUDIO NARRATION
With section-by-section viewing, multimedia capability and interactive tools, our ePoster solution walks the walk when it comes to engaging the audience.

INDIVIDUAL VIRTUAL ROOMS FOR POSTER SESSIONS
​Poster sessions have never been so exciting! Run your sessions with hundreds of individual virtual classrooms simultaneously.

ONSITE EPOSTERS ON TOUCH SCREENS
Our intuitive, stand-alone solution allows your delegates to either “self-present” posters or opt for scheduling oral presentations

ORAL ePOSTER SESSIONS
Organize oral ePoster sessions with our onsite pre-management tool regardless of the number of sessions you are planning to include. We work with your onsite AV Provider and provide turnkey services from inception to onsite delivery.

API INTEGRATION WITH VIRTUAL EVENT PLATFORMS 
Developed as a stand-alone platform, our ePoster solution also connects with your Virtual Event Platform via API to provide seamless Single-Sign-On (SSO) experience for your attendees.  We also provide meeting app vendors with embedded links allowing them to display ePosters, with full zoom in and narration features directly from their mobile app.

ePOSTER SUBMISSION
The MULTILEARNING LMS contains a submission and review section that allows poster authors to upload poster files and videos, give consent to publish, and self-record audio narration on each section. Throughout the process, our clients have an at-a-glance view of submission progress. Your authors, submitters, and attendees will appreciate our 24/7 support agents available to help them throughout the process.

The MULTILEARNING ePoster solution is the most complete and engaging solution you'll ever find. 

Contact our business development team at sales@multilearning.com or click on the communication widget to connect live with our support agents. 

The Role of Calcium in the Stabilization of the NHE1-CHP3 Complex

Hans-Christian Zaun, Ph. D., Scientific Advisor, MultiLearning Group, 

Montreal, QC, Canada


This poster is adapted for promotional purposes by  Dr. Zaun, on research performed in the laboratory of Dr. John Orlowski, Professor, Department of Physiology, McGill University, Montreal, QC, Canada


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.

 

The Role of Calcium in the Stabilization of the NHE1-CHP3 Complex

Hans-Christian Zaun, Ph. D., Scientific Advisor, MultiLearning Group, 

Montreal, QC, Canada


This poster is adapted for promotional purposes by  Dr. Zaun, on research performed in the laboratory of Dr. John Orlowski, Professor, Department of Physiology, McGill University, Montreal, QC, Canada


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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