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Michael Chen on Muck Rack

Michael Chen

As seen in: National Institutes of Health, Color Research & Application, Nature, Patient Education and Counseling, JAMA (The Journal of the American Medical Association), JAMA Oncology, Science Magazine, Business 2 Community, BioRxiv, Cell Press and

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Michael Chen’s Biography

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Current student at University of Toronto Scarborough and Centennial College's joint journalism program.

Interning at Rogers Publishing for Benefits Canada.

Articles

Buntanetap treatment in mild to moderate Alzheimer’s disease: phase 2/3 study

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By Cheng Fang, David Feng, Melissa Gaines, Daniel T. Laskowitz, Laurie Sanders, Kore Liow, Elizabeth M. Peckham, Angela Ritter, Michael Chen, Alexander Morin, Rajeev Kumar, Rekha Gandhi, Kathleen A. Welsh-Bohmer, Martin R Farlow, Kim Johnson, Alidad Mireskandari, Maria Maccecchini
| Nature Verified
Abstract Buntanetap is an orally available small RNA targeting molecule that inhibits the translation of multiple neurotoxic aggregating proteins, including amyloid precursor protein (APP) and Tau. It has been evaluated in 13 clinical trials involving over 1000 participants, including healthy volunteers, patients with Alzheimer’s disease (AD) and Parkinson’s disease (PD), and has shown a favorable safety and tolerability profile.
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Direct observation and control of non-classical crystallization pathways in binary colloidal systems - Nature Communications

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By Shihao Zang, Sanjib Paul, Cheuk W. Leung, Michael Chen, Glen M. Hocky
| Nature Verified
Abstract Crystallization stands as a prime example of self-assembly. Elementary building blocks converge, seemingly adhering to an intricate blueprint, orchestrating order from chaos. While classical theories describe crystallization as a monomer-by-monomer addition, non-classical pathways introduce complexity. Using microscopic charged particles as monomers, we uncover the mechanisms governing the formation of ionic colloidal crystals.
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Phase transition pathways encode distinct physicochemical properties of biomolecular condensates

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By Xiaokang Ren, Michael Chen, Yifan Dai, Leshan Yang
| BioRxiv
Abstract The same intrinsically disordered proteins (IDPs) can form biomolecular condensates through distinct thermodynamic phase transition processes, such as temperature-dependent and osmosis-dependent pathways. These distinct thermodynamic driving forces should, in principle, induce phase transition by modulating different features of the solvent environments, so that different driving forces should correspond with distinct sequence grammars for phase transition.
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