Literature DB >> 18576153

Expression and purification of full-length recombinant PrP of high purity.

Natallia Makarava1, Ilia V Baskakov.   

Abstract

Certain applications in the prion field require recombinant prion protein (PrP) of high purity and quality. Here, we report an experimental procedure for expression and purification of full-length mammalian prion protein. This protocol has been proved to yield PrP of extremely high purity that lacks PrP adducts, which are normally generated as a result of spontaneous oxidation or degradation.

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Year:  2008        PMID： 18576153     DOI： 10.1007/978-1-59745-234-2_10

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN： 1064-3745


  14 in total

1.  Cofactor molecules induce structural transformation during infectious prion formation.

Authors:  Michael B Miller; Daphne W Wang; Fei Wang; Geoffrey P Noble; Jiyan Ma; Virgil L Woods; Sheng Li; Surachai Supattapone
Journal:  Structure       Date:  2013-10-10       Impact factor: 5.006

2.  Low density subcellular fractions enhance disease-specific prion protein misfolding.

Authors:  James F Graham; Sonya Agarwal; Dominic Kurian; Louise Kirby; Teresa J T Pinheiro; Andrew C Gill
Journal:  J Biol Chem       Date:  2010-01-27       Impact factor: 5.157

3.  Protocol for aerosol-free recombinant production and NMR analysis of prion proteins.

Authors:  Peter Rehbein; Krishna Saxena; Kai Schlepckow; Harald Schwalbe
Journal:  J Biomol NMR       Date:  2014-04-26       Impact factor: 2.835

4.  Non-reducing alkaline solubilization and rapid on-column refolding of recombinant prion protein.

Authors:  Daniel J Walsh; Geoffrey P Noble; Justin R Piro; Surachai Supattapone
Journal:  Prep Biochem Biotechnol       Date:  2012       Impact factor: 2.162

5.  Highly neurotoxic monomeric α-helical prion protein.

Authors:  Minghai Zhou; Gregory Ottenberg; Gian Franco Sferrazza; Corinne Ida Lasmézas
Journal:  Proc Natl Acad Sci U S A       Date:  2012-02-07       Impact factor: 11.205

6.  Oxidation of Helix-3 methionines precedes the formation of PK resistant PrP.

Authors:  Tamar Canello; Kati Frid; Ronen Gabizon; Silvia Lisa; Assaf Friedler; Jackob Moskovitz; María Gasset; Ruth Gabizon
Journal:  PLoS Pathog       Date:  2010-07-01       Impact factor: 6.823

7.  Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein.

Authors:  Jason C Sang; Chung-Yu Lee; Frederick Y Luh; Ya-Wen Huang; Yun-Wei Chiang; Rita P-Y Chen
Journal:  Prion       Date:  2012-09-17       Impact factor: 3.931

8.  Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.

Authors:  Michael B Miller; James C Geoghegan; Surachai Supattapone
Journal:  PLoS Pathog       Date:  2011-07-14       Impact factor: 6.823

9.  Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.

Authors:  James F Graham; Dominic Kurian; Sonya Agarwal; Lorna Toovey; Lawrence Hunt; Louise Kirby; Teresa J T Pinheiro; Steven J Banner; Andrew C Gill
Journal:  PLoS One       Date:  2011-11-02       Impact factor: 3.240

10.  Amyloid core formed of full-length recombinant mouse prion protein involves sequence 127-143 but not sequence 107-126.

Authors:  Biswanath Chatterjee; Chung-Yu Lee; Chen Lin; Eric H-L Chen; Chao-Li Huang; Chien-Chih Yang; Rita P-Y Chen
Journal:  PLoS One       Date:  2013-07-03       Impact factor: 3.240
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