Nat Rev Microbiol. 2004 Nov;2(11):861-71.

The state of the prion.

Source

MRC Prion Unit, Department of Neurodegenerative Disease, Institute of Neurology, Queen Square, London WC1N 3BG, UK. charles.weissmann@prion.ucl.ac.uk

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.

PMID:: 15494743; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances

Publication Types

Review

MeSH Terms

Substances

LinkOut - more resources

Full Text Sources

Other Literature Sources

Labome Researcher Resource - ExactAntigen/Labome

Medical

Supplemental Content

Save items

Related citations in PubMed

Species barrier in prion diseases: a kinetic interpretation based on the conformational adaptation of the prion protein. [Biochem J. 1998]
Species barrier in prion diseases: a kinetic interpretation based on the conformational adaptation of the prion protein.
Kellershohn N, Laurent M. Biochem J. 1998 Sep 15; 334 ( Pt 3):539-45.
Review A general model of prion strains and their pathogenicity. [Science. 2007]
Review A general model of prion strains and their pathogenicity.
Collinge J, Clarke AR. Science. 2007 Nov 9; 318(5852):930-6.
Review [Mechanisms of prion transmission]. [Nihon Rinsho. 2007]
Review [Mechanisms of prion transmission].
Sakaguchi S. Nihon Rinsho. 2007 Aug; 65(8):1391-5.
Review The prion protein and lipid rafts. [Mol Membr Biol. 2006]
Review The prion protein and lipid rafts.
Taylor DR, Hooper NM. Mol Membr Biol. 2006 Jan-Feb; 23(1):89-99.
Review Deadly conformations--protein misfolding in prion disease. [Cell. 1997]
Review Deadly conformations--protein misfolding in prion disease.
Horwich AL, Weissman JS. Cell. 1997 May 16; 89(4):499-510.

See reviews... See all...

Cited by 71 PubMed Central articles

Enzymatic activity of a subtilisin homolog, Tk-SP, from Thermococcus kodakarensis in detergents and its ability to degrade the abnormal prion protein. [BMC Biotechnol. 2013]
Enzymatic activity of a subtilisin homolog, Tk-SP, from Thermococcus kodakarensis in detergents and its ability to degrade the abnormal prion protein.
Hirata A, Hori Y, Koga Y, Okada J, Sakudo A, Ikuta K, Kanaya S, Takano K. BMC Biotechnol. 2013 Feb 28; 13:19. Epub 2013 Feb 28.
Does the central dogma still stand? [Biol Direct. 2012]
Does the central dogma still stand?
Koonin EV. Biol Direct. 2012 Aug 23; 7:27. Epub 2012 Aug 23.
The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc). [J Neurosci. 2012]
The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).
Turnbaugh JA, Unterberger U, Saá P, Massignan T, Fluharty BR, Bowman FP, Miller MB, Supattapone S, Biasini E, Harris DA. J Neurosci. 2012 Jun 27; 32(26):8817-30.

See all...

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.

Recent activity

Clear Turn Off Turn On

The state of the prion.
The state of the prion.
Nat Rev Microbiol. 2004 Nov ;2(11):861-71.

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Result Filters

Display Settings:

Send to: