This title includes a number of Open Access chapters. This book contains a selection of chapters aimed to provide a better understanding prion structure and biology. Together these chapters provide an overview of prion biology and underscore some of the challenges we face if we want to understand how this lively pathogen propagates and evolves in mammals. There is also mounting evidence that studying prion biology has a wider relevance due to similarities in the processes of protein misfolding and aggregation between prion disorders and other neurodegenerative disorders such as Alzheimer's, Parkinson's, and Huntington's diseases.…mehr
This title includes a number of Open Access chapters. This book contains a selection of chapters aimed to provide a better understanding prion structure and biology. Together these chapters provide an overview of prion biology and underscore some of the challenges we face if we want to understand how this lively pathogen propagates and evolves in mammals. There is also mounting evidence that studying prion biology has a wider relevance due to similarities in the processes of protein misfolding and aggregation between prion disorders and other neurodegenerative disorders such as Alzheimer's, Parkinson's, and Huntington's diseases.
Dr. Vincent Béringue is working in the prion field for almost twenty years. He has obtained his PhD in 1998 from the AgroParisTech Institute in Paris, in the laboratory of late Dr. Dominique Dormont. After a MRC-funded postdoctoral position in the laboratory of Prof. John Collinge and Dr. Simon Hawke at Imperial College School of Medicine in London, he joined Dr. Hubert Laude's laboratory at INRA (National Institute for Agricultural Research) in Jouy-en-Josas in 2001, as permanent staff scientist. He is now head of lab in the Molecular Virology Immunology Department at INRA. His primary research interests include the biochemistry, diversity and evolution of animal and human prions.
Inhaltsangabe
Cellular Prion Protein Protects from Inflammatory and Neuropathic Pain. Brain Transcriptional Stability Upon Prion Protein-encoding Gene Invalidation in Zygotic or Adult Mouse. Highly Efficient Protein Misfolding Cyclic Amplification. The Role of Glycophosphatidylinositol Anchor in the Amplification of the Scrapie Isoform of Prion Protein in vitro. The Octarepeat Region of the Prion Protein Is Conformationally Altered in PrP(Sc). Prion Protein Self-Peptides Modulate Prion Interactions and Conversion. Prpsc Spreading Patterns in the Brain of Sheep Linked to Different Prion Types. Experimental H-type Bovine Spongiform Encephalopathy Characterized by Plaques and Glial- and Stellate-type Prion Protein Deposits. A Novel Form of Human Disease with a Protease-Sensitive Prion Protein and Heterozygosity Methionine/valine at Codon 129: Case Report. Molecular Interactions Between Prions as Seeds and Recombinant Prion Proteins as Substrates Resemble the Biological Interspecies Barrier in vitro. Quantitative Phosphoproteomic Analysis of Prion-infected Neuronal Cells.
Cellular Prion Protein Protects from Inflammatory and Neuropathic Pain. Brain Transcriptional Stability Upon Prion Protein-encoding Gene Invalidation in Zygotic or Adult Mouse. Highly Efficient Protein Misfolding Cyclic Amplification. The Role of Glycophosphatidylinositol Anchor in the Amplification of the Scrapie Isoform of Prion Protein in vitro. The Octarepeat Region of the Prion Protein Is Conformationally Altered in PrP(Sc). Prion Protein Self-Peptides Modulate Prion Interactions and Conversion. Prpsc Spreading Patterns in the Brain of Sheep Linked to Different Prion Types. Experimental H-type Bovine Spongiform Encephalopathy Characterized by Plaques and Glial- and Stellate-type Prion Protein Deposits. A Novel Form of Human Disease with a Protease-Sensitive Prion Protein and Heterozygosity Methionine/valine at Codon 129: Case Report. Molecular Interactions Between Prions as Seeds and Recombinant Prion Proteins as Substrates Resemble the Biological Interspecies Barrier in vitro. Quantitative Phosphoproteomic Analysis of Prion-infected Neuronal Cells.
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