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Exp Neurobiol 2020; 29(1): 93-105
Published online February 29, 2020
https://doi.org/10.5607/en.2020.29.1.93
© The Korean Society for Brain and Neural Sciences
Jae Wook Hyeon1, Ran Noh1, Jiwon Choi2, Sol Moe Lee1, Yeong Seon Lee1, Seong Soo A. An3, Kyoung Tai No2,4 and Jeongmin Lee5*
1Division of Bacterial Disease Research, Center for Infectious Disease Research, Korea National Institute of Health, Centers for Disease Control and Prevention, Cheongju 28160, 2Bioinformatics and Molecular Design Research Center, Yonsei University, Seoul 03722, 3Gachon Bio Nano Research Institute, Gachon University, Seongnam 13120, 4Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, 5Division of Research Planning, Korea National Institute of Health, Centers for Disease Control and Prevention, Cheongju 28160, Korea
Correspondence to: *To whom correspondence should be addressed.
TEL: 82-43-719-8024, FAX: 82-43-719-8489
e-mail: jeongminlee@korea.kr
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License
(http://creativecommons.org/licenses/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and
reproduction in any medium, provided the original work is properly cited.
Prion diseases are a group of neurodegenerative and fatal central nervous system disorders. The pathogenic mechanism involves the conversion of cellular prion protein (PrPC) to an altered scrapie isoform (PrPSc), which accumulates in amyloid deposits in the brain. However, no therapeutic drugs have demonstrated efficacy in clinical trials. We previously reported that BMD42-29, a synthetic compound discovered
Keywords: Transmissible spongiform encephalopathy, Prion protein, Anti-prion, Derivatives, In silico