Publications by authors named "N Beauchemin"
Background: Alternative splicing is a fundamental mechanism in the post-transcriptional regulation of genes. The multifunctional transmembrane glycoprotein receptor carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) undergoes extensive alternative splicing to allow for tunable functions in cell signalling, adhesion and modulation of immune and metabolic responses. Splice isoforms that differ in their ectodomain and short or long cytoplasmic tail (CEACAM1-S/CEACAM1-L) have distinct functional roles.
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- - CEACAM1 is a crucial membrane protein involved in various immune and non-immune functions, acting as both a homophilic and heterophilic ligand with host proteins like CEACAM5 and TIM-3.
- - The protein is targeted by several pathogens to help them invade hosts and evade the immune system, linking it to issues like infectious diseases, autoimmunity, and cancer.
- - The review details the structural interactions of CEACAM1, examining its different states (monomeric, dimeric, oligomeric) and their implications for signaling and function, including the impact of avidity on its activity.
Computer-based learning has gained popularity in recent years, providing learners greater flexibility and freedom. However, these learning environments do not consider the learner's mental state in real-time, resulting in less optimized learning experiences. This research aimed to explore the effect on the learning experience of a novel EEG-based Brain-Computer Interface (BCI) that adjusts the speed of information presentation in real-time during a learning task according to the learner's cognitive load.
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- CEACAM1 is a cell surface protein that affects immune responses, but its role in tumors is not well understood.
- The study used specialized antibodies to analyze the presence of CEACAM1 alongside PD1 and PD-L1 in various immune cells from melanoma patients and healthy controls.
- Results showed high levels of CEACAM1 on immune cells in melanoma patients, particularly in those resistant to treatment, indicating potential pathways for targeted therapies.
Article Synopsis
- - SHP-1 is a protein that helps regulate glucose and lipid balance and its role in regulating PPARγ2, a key player in fat cell development (adipogenesis), was previously unexplored.
- - The study found that SHP-1 interacts with PPARγ2 via its SH2 domain and can reduce the tyrosine phosphorylation on PPARγ2, leading to decreased stability of this protein.
- - When SHP-1 is lost, PPARγ2's activation increases, resulting in higher expression of its target genes and more lipid accumulation in cells, but blocking PPARγ2's phosphorylation can lessen this effect.