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Literature DB >> 15494743

The state of the prion.

Abstract

There is little doubt that the main component of the transmissible agent of spongiform encephalopathies - the prion - is a conformational variant of the ubiquitous host protein PrP(C), and that the differing properties of various prion strains are associated with different abnormal conformations of this protein. The precise structure of the prion is not yet known, nor are the mechanisms of infection, conformational conversion and pathogenesis understood.

Entities: Disease Species

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Year: 2004 PMID： 15494743 DOI： 10.1038/nrmicro1025

Source DB: PubMed Journal: Nat Rev Microbiol ISSN： 1740-1526 Impact factor: 60.633

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Cited

124 in total

1. Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process.

Authors: Kei-ichi Yamaguchi; Tomoharu Matsumoto; Kazuo Kuwata
Journal: Protein Sci Date: 2011-11-22 Impact factor: 6.725

Review 2. Allosteric function and dysfunction of the prion protein.

Authors: Rafael Linden; Yraima Cordeiro; Luis Mauricio T R Lima
Journal: Cell Mol Life Sci Date: 2011-10-09 Impact factor: 9.261

3. Agent strain variation in human prion disease: insights from a molecular and pathological review of the National Institutes of Health series of experimentally transmitted disease.

Authors: Piero Parchi; Maura Cescatti; Silvio Notari; Walter J Schulz-Schaeffer; Sabina Capellari; Armin Giese; Wen-Quan Zou; Hans Kretzschmar; Bernardino Ghetti; Paul Brown
Journal: Brain Date: 2010-09-07 Impact factor: 13.501

The state of the prion.

1. Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process.

Review 2. Allosteric function and dysfunction of the prion protein.

3. Agent strain variation in human prion disease: insights from a molecular and pathological review of the National Institutes of Health series of experimentally transmitted disease.

4. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast.

5. Protein structure by mechanical triangulation.

6. Contact-induced structure transformation in transmembrane prion propagation.

Review 7. Prion diseases and their biochemical mechanisms.

Review 8. Copper and the prion protein: methods, structures, function, and disease.

9. Prion propagation and toxicity occur in vitro with two-phase kinetics specific to strain and neuronal type.

Review 10. Prion-like propagation of cytosolic protein aggregates: insights from cell culture models.