Linked Life Data

18809261

Source:http://linkedlifedata.com/resource/pubmed/id/18809261

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-12-29
pubmed:abstractText
The "protein-only" hypothesis of prion diseases views the infectious agent as devoid of nucleic acids and consisting of misfolded prion proteins (PrP(Sc)) which, upon infiltration into host cells, act as a template that induces transformation of wild-type protein (PrP(C)) to the pathological form by unknown mechanisms. The two isoforms are identical in amino-acid composition. By analogy to reported "silent" mutations in which utilization of relatively rare tRNAs alter protein folding pattern, we postulate that misfolded PrP(Sc) alters tRNAs abundance in prion-infected cells and results in different rates of co-translational folding of PrP, leading to the formation of additional misfolded PrP(Sc). We analyze experiments that might link tRNAs to prions. This concept of "PrP-seed and tRNA-soil" envisages a vicious cycle in which PrP(Sc) levels govern specific tRNA usage, whose alteration subsequently transforms resident PrP(C) to PrP(Sc), causing the cycle to repeat itself ad infinitum.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0306-9877
pubmed:author
pubmed:issnType
Print
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-5
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Prion and anti-codon usage: does infectious PrP alter tRNA abundance to induce misfolding of PrP?
pubmed:affiliation
Department of Neurobiology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel-Aviv, Israel. odedrechavi@gmail.com
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't