Prion diseases : a review.
Prion diseases are caused by a misfolded protein which have the uncanny ability to escape destruction by the immune system in vivo and autoclaving in vitro. The pattern of these diseases was so eccentric as it defied the central dogma of molecular biology, because these prion proteins were infectiou...
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sg-ntu-dr.10356-508862023-02-28T18:07:16Z Prion diseases : a review. Cheng, Jason Chang Lin. Yu Chin-Wen Kenneth School of Biological Sciences DRNTU::Science::Biological sciences Prion diseases are caused by a misfolded protein which have the uncanny ability to escape destruction by the immune system in vivo and autoclaving in vitro. The pattern of these diseases was so eccentric as it defied the central dogma of molecular biology, because these prion proteins were infectious and could multiply to greater amounts even though they lacked the genetic material of DNA and RNA. The impact from prion diseases is great, with sporadic outbreaks worldwide that affect human life and out animal livestock. Though the misfolded prion protein structure has been elucidated, much work is still required to determine the cellular pathogenesis and treatment of these prion diseases. Recent studies have given new insight into the disease, including interactions with a possible E3 ligase correlated to the spongiform pathogenesis and a possible anti-prion defence and clearance system. This present report reviews the history, the types of prion diseases, pathogenesis, emerging theories regarding prion strain-like behavior and propagation and possible treatments of prion diseases. Bachelor of Science in Biological Sciences 2012-12-13T08:07:40Z 2012-12-13T08:07:40Z 2012 2012 Final Year Project (FYP) http://hdl.handle.net/10356/50886 en Nanyang Technological University 29 p. application/pdf |
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DRNTU::Science::Biological sciences Cheng, Jason Chang Lin. Prion diseases : a review. |
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Prion diseases are caused by a misfolded protein which have the uncanny ability to escape destruction by the immune system in vivo and autoclaving in vitro. The pattern of these diseases was so eccentric as it defied the central dogma of molecular biology, because these prion proteins were infectious and could multiply to greater amounts even though they lacked the genetic material of DNA and RNA. The impact from prion diseases is great, with sporadic outbreaks worldwide that affect human life and out animal livestock. Though the misfolded prion protein structure has been elucidated, much work is still required to determine the cellular pathogenesis and treatment of these prion diseases. Recent studies have given new insight into the disease, including interactions with a possible E3 ligase correlated to the spongiform pathogenesis and a possible anti-prion defence and clearance system. This present report reviews the history, the types of prion diseases, pathogenesis, emerging theories regarding prion strain-like behavior and propagation and possible treatments of prion diseases. |
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Yu Chin-Wen Kenneth |
author_facet |
Yu Chin-Wen Kenneth Cheng, Jason Chang Lin. |
format |
Final Year Project |
author |
Cheng, Jason Chang Lin. |
author_sort |
Cheng, Jason Chang Lin. |
title |
Prion diseases : a review. |
title_short |
Prion diseases : a review. |
title_full |
Prion diseases : a review. |
title_fullStr |
Prion diseases : a review. |
title_full_unstemmed |
Prion diseases : a review. |
title_sort |
prion diseases : a review. |
publishDate |
2012 |
url |
http://hdl.handle.net/10356/50886 |
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1759855273833398272 |