Amyloid, prions, and other protein aggregates, Part B by Ronald Wetzel, Indu Kheterpal PDF

By Ronald Wetzel, Indu Kheterpal

ISBN-10: 0121828174

ISBN-13: 9780121828172

The facility of polypeptides to shape then again folded, polymeric buildings comparable to amyloids and comparable aggregates is being more and more famous as an incredible new frontier in protein study. This new quantity of tools in Enzymology besides half C (volume 413) on Amyloid, Prions and different Protein Aggregates proceed within the culture of the 1st quantity (309) in containing particular protocols and methodological insights, supplied by way of leaders within the box, into the newest equipment for investigating the constructions, mechanisms of formation, and organic actions of this crucial classification of protein assemblies. * offers specific protocols* comprises troubleshooting assistance* presents assurance on structural biology, computational tools, and biology

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Additional resources for Amyloid, prions, and other protein aggregates, Part B

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And Caughey, B. (1995). Species specificity in the cell‐free conversion of prion protein to protease‐resistant forms: A model for the scrapie species barrier. Proc. Natl. Acad. Sci. USA 92, 3923–3927. , and Schimmer, H. (1999). Test for BSE evaluated. Nature 400, 105. , and Supattapone, S. (2004). Ionic strength and transition metals control PrPSc protease resistance and conversion‐inducing activity. J. Biol. Chem. 43, 2613–2621. Pan, K. , and Prusiner, S. B. (1993). Conversion of alpha‐helices into b‐sheets features in the formation of scrapie prion proteins.

1995). Species specificity in the cell‐free conversion of prion protein to protease‐resistant forms: A model for the scrapie species barrier. Proc. Natl. Acad. Sci. USA 92, 3923–3927. , and Schimmer, H. (1999). Test for BSE evaluated. Nature 400, 105. , and Supattapone, S. (2004). Ionic strength and transition metals control PrPSc protease resistance and conversion‐inducing activity. J. Biol. Chem. 43, 2613–2621. Pan, K. , and Prusiner, S. B. (1993). Conversion of alpha‐helices into b‐sheets features in the formation of scrapie prion proteins.

Smits, M. , Lansbury, P. , and Caughey, B. (1997). Molecular assessment of the potential transmissibilities of BSE and scrapie to humans. Nature 388, 285–288. , Gajdusek, D. , and Gibbs, C. , Jr. (1973). The clinical characteristics of transmissible Creutzfeldt‐Jakob disease. Brain 96, 1–20. Saborio, G. , and Soto, C. (2001). Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411, 810–813. Saborio, G. , Kascsak, R. , Harris, D. , and Frangione, B.

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Amyloid, prions, and other protein aggregates, Part B by Ronald Wetzel, Indu Kheterpal


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