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

By Ronald Wetzel, Indu Kheterpal

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

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

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Harris, D. , and Frangione, B. (1999). Cell‐lysate conversion of prion protein into its protease‐resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Commun. 258, 470–475. Schiermeier, Q. (2001). Testing times for BSE. Nature 409, 658–659. [2] prion protein separation by FFF 21 Soto, C. (2001). Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498, 204–207. Soto, C. (2004). Diagnosing prion diseases: Needs, challenges and hopes. Nat.

Diagnosing prion diseases: Needs, challenges and hopes. Nat. Rev. Microbiol. 2, 809–819. , and Saborio, G. P. (2001). Prions: Disease propagation and disease therapy by conformational transmission. Trends Mol. Med. 7, 109–114. , Saborio, G. , and Anderes, L. (2002). Cyclic amplification of protein misfolding: Application to prion‐related disorders and beyond. Trends Neurosci. 25, 390–394. , Frossard, M. , Torres, J. , and Tagliavini, F. (2005). Pre‐symptomatic detection of prions by cyclic amplification of protein misfolding.

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. (1999). Cell‐lysate conversion of prion protein into its protease‐resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Commun. 258, 470–475. Schiermeier, Q. (2001). Testing times for BSE. Nature 409, 658–659. [2] prion protein separation by FFF 21 Soto, C. (2001). Protein misfolding and disease; protein refolding and therapy.

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