New PDF release: Prions: the new biology of proteins

New PDF release: Prions: the new biology of proteins

By Claudio Soto

"Prions: the hot Biology of Proteins offers a well-organized assessment of what's shortly identified approximately prion-related ailments. This complete paintings experiences the scientific indicators, epidemiology, and neuropathology of the affliction. It makes a speciality of facts aiding the concept TSEs end result from a completely novel illness mechanism, concerning transmission by way of replication of the misfolding of a unmarried protein in the Read more...

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Extra resources for Prions: the new biology of proteins

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USA, 97, 5836–5841, 2000. , Scrapie prions: a three-dimensional model of an infectious fragment, Fold. , 1, 13–19, 1996. T. , Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer’s disease and scrapie? Cell, 73, 1055–1058, 1993. Kaneko, K. , A synthetic peptide initiates Gerstmann-Straussler-Scheinker (GSS) disease in transgenic mice, J. Mol. , 295, 997–1007, 2000. Kaneko, K. , Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform, Proc.

However, the exact mechanism underlying the conversion is not known. From molecular genetic studies as well as from the analysis of the requirements for PrP conversion in vitro, it has been postulated that a chaperone-like protein, provisionally called protein X, facilitates PrPC → PrPSc conversion (see below). However, the nature of this factor is still unknown. The precise molecular mechanism of PrPC → PrPSc conversion is not well understood. 3), namely: 1. 3A), which postulates that a physical interaction between the isoforms is a precondition to the structural changes that underlie the pathogenic conversion of PrPC.

1999]. Despite the evidence in favor of a neuroprotective signaling role for PrPC, it is not clear how a GPI-anchored protein can initiate a signaling cascade, since activation of adenyl cyclase is dependent on the activity of G-proteins located in the inner side of the plasma membrane. Thus, the possible mechanism of PrPC-mediated signaling remains speculative, and more research is required to clarify this key issue. 3 PrPC ligands indicate a potential role in apoptosis The search for PrP-interacting proteins has been pursued in an attempt to understand the function of PrPC.

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