Summary: Straight from a scientist is a great podcast that I listen to routinely. Connor is the best as well. You basically get the synthesis of two podcasts and hosts while listening to just one episode. Check this one out. It’s fantastic!<br> Connor<br> <a href="https://www.straightfromascientist.com/the-team/">Taken from Website</a><br> “Connor is a second year PhD track graduate student in the pharmacology curriculum at UNC Chapel Hill. As a co-mentored student between the <a href="https://tcohenlab.web.unc.edu/" target="_blank" rel="noopener">Cohen</a> and <a href="https://songlab.web.unc.edu/">Song Lab</a>s at UNC, he studies <a href="https://www.straightfromascientist.com/sfs02-pathways-into-science-and-gaba-in-alzheimers-disease/">GABAergic neural networks in Alzheimer’s Disease.</a> His scientific interests include the interactions between the environment, genetics, and behavior in mood disorders and neurodegenerative diseases. Connor and Julian founded SFS with the idea of connecting people directly with scientists.<br> Outside of the lab, Connor enjoys hobbies such as graphic design, gaming, Brazilian Jiu Jitsu, paintball and caring for his bearded dragon and Madagascar Giant Day geckos. Connor also manages the <a href="https://tcohenlab.web.unc.edu/" target="_blank" rel="noopener">Cohen lab website</a> and a <a href="https://giantdaygeckos.wordpress.com/" target="_blank" rel="noopener">Giant day Gecko care blog. ” </a><br> Education<br> B.S. In Biology and Biochemistry — Chemistry Minor<br> Virginia Tech 2014<br> Publications<br> <br> <br> * <a title=" Related Articles Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program. Nat Commun. 2017 07 19;8(1):82 Authors: Wang P, Wander CM, Yuan CX, Bereman MS, Cohen TJ Abstract TDP-43 pathology marks a spectrum of multisystem proteinopathies including amyotrophic lateral sclerosis, frontotemporal lobar degeneration, and sporadic inclusion body myositis. Surprisingly, it has been challenging to recapitulate this pathology, highlighting an incomplete understanding of TDP-43 regulatory mechanisms. Here we provide evidence supporting TDP-43 acetylation as a trigger for disease pathology. Using cultured cells and mouse skeletal muscle, we show that TDP-43 acetylation-mimics promote TDP-43 phosphorylation and ubiquitination, perturb mitochondria, and initiate degenerative inflammatory responses that resemble sporadic inclusion body myositis pathology. Analysis of functionally linked amyotrophic lateral sclerosis proteins revealed recruitment of p62, ubiquilin-2, and optineurin to TDP-43 aggregates. We demonstrate that TDP-43 acetylation-mimic pathology is potently suppressed by an HSF1-dependent mechanism that disaggregates TDP-43. Our study illustrates bidirectional TDP-43 processing in which TDP-43 aggregation is targeted by a coordinated chaperone response. Thus, activation or restoration of refolding mechanisms may alleviate TDP-43 aggregation in tissues that are uniquely susceptible to TDP-43 proteinopathies.TDP-43 aggregation is linked to various diseases including amyotrophic lateral sclerosis. Here the authors show that acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein. PMID: 28724966 [PubMed - indexed for MEDLINE] " href="https://www.ncbi.nlm.nih.gov/pubmed/28724966?dopt=Abstract">Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program.</a><br> * <br> <br> <br> <br> Straight from a Scientist<br> “Science is moving rapidly- almost too rapidly. New breakthroughs in medicine and the fundamental research behind such breakthroughs seem to emerge every day. While this should be celebrated, it is often hard to keep up with science news. In science, it’s also highly imperative that new information is accurat...
