rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
2001-7-11
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pubmed:databankReference |
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pubmed:abstractText |
The [URE3] non-Mendelian element of the yeast S. cerevisiae is due to the propagation of a transmissible form of the protein Ure2. The infectivity of Ure2p is thought to originate from a conformational change of the normal form of the prion protein. This conformational change generates a form of Ure2p that assembles into amyloid fibrils. Hence, knowledge of the three-dimensional structure of prion proteins such as Ure2p should help in understanding the mechanism of amyloid formation associated with a number of neurodegenerative diseases.
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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 |
Jan
|
pubmed:issn |
0969-2126
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
9
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
39-46
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:11342133-Amino Acid Sequence,
pubmed-meshheading:11342133-Amyloid,
pubmed-meshheading:11342133-Binding Sites,
pubmed-meshheading:11342133-Crystallography, X-Ray,
pubmed-meshheading:11342133-Dimerization,
pubmed-meshheading:11342133-Fungal Proteins,
pubmed-meshheading:11342133-Glutathione Peroxidase,
pubmed-meshheading:11342133-Glutathione Transferase,
pubmed-meshheading:11342133-Ligands,
pubmed-meshheading:11342133-Models, Molecular,
pubmed-meshheading:11342133-Molecular Sequence Data,
pubmed-meshheading:11342133-Prions,
pubmed-meshheading:11342133-Protein Conformation,
pubmed-meshheading:11342133-Protein Structure, Secondary,
pubmed-meshheading:11342133-Protein Structure, Tertiary,
pubmed-meshheading:11342133-Saccharomyces cerevisiae,
pubmed-meshheading:11342133-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11342133-Sequence Homology, Amino Acid
|
pubmed:year |
2001
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pubmed:articleTitle |
Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae.
|
pubmed:affiliation |
Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|