IMR Press / FBL / Volume 15 / Issue 1 / DOI: 10.2741/3611

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

PrP interactions with nucleic acids and glycosaminoglycans in function and disease
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1 Instituto de Bioquímica Medica, Centro Nacional de Ressonancia Magnetica Nuclear Jiri Jonas, Instituto Nacional de Ciencia e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, CCS, RJ 21941-590, Rio de Janeiro, Brazil
2 Faculdade de Farmacia, Universidade Federal do Rio de Janeiro, RJ 21941-590, Rio de Janeiro, Brazil
Academic Editor:Pradip Nandi
Front. Biosci. (Landmark Ed) 2010, 15(1), 132–150;
Published: 1 January 2010

Since the first description of prion diseases, great effort has been made toward comprehending this new paradigm in biology. Despite large advances in the field, many questions remain unanswered, especially concerning the conversion of PrPC into PrPSc. How this conformational transition evolves is a crucial problem that must be solved in order to attain further progress in therapeutics and prevention. Recent developments have indicated the requirement for partners of the prion protein in triggering the conversion. In the present review, we will explore the interaction of PrP with some of its most intriguing partners, such as sulfated glycans and nucleic acids. These molecules seem to play a dual role in prion biology and could be fundamental to explaining how prion diseases arise, as well as in the development of effective therapeutic approaches.

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