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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5212
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|
pubmed:dateCreated |
1995-6-16
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pubmed:abstractText |
The yeast non-Mendelian factor [psi+] has been suggested to be a self-modified protein analogous to mammalian prions. Here it is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the [psi+] factor. Over-production or inactivation of Hsp104 caused the loss of [psi+]. These results suggest that chaperone proteins play a role in prion-like phenomena, and that a certain level of chaperone expression can cure cells of prions without affecting viability. This may lead to antiprion treatments that involve the alteration of chaperone amounts or activity.
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pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
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pubmed:month |
May
|
|
pubmed:issn |
0036-8075
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
12
|
|
pubmed:volume |
268
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
880-4
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|
pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
|
|
pubmed:year |
1995
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|
pubmed:articleTitle |
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].
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|
pubmed:affiliation |
Department of Biological Sciences, University of Illinois, Chicago 60607-7020, USA.
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|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
