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| http://purl.uniprot.org/citations/19519514 | http://www.w3.org/2000/01/rdf-schema#comment | "Heat shock proteins protect cells from various conditions of stress. Hsp70, the most ubiquitous and highly conserved Hsp, helps proteins adopt native conformation or regain function after misfolding. Various co-chaperones specify Hsp70 function and broaden its substrate range. We discuss Hsp70 structure and function, regulation by co-factors and influence on propagation of yeast prions."xsd:string |
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| http://purl.uniprot.org/citations/19519514 | http://purl.uniprot.org/core/author | "Sharma D."xsd:string |
| http://purl.uniprot.org/citations/19519514 | http://purl.uniprot.org/core/author | "Masison D.C."xsd:string |
| http://purl.uniprot.org/citations/19519514 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19519514 | http://purl.uniprot.org/core/name | "Protein Pept Lett"xsd:string |
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| http://purl.uniprot.org/citations/19519514 | http://purl.uniprot.org/core/title | "Hsp70 structure, function, regulation and influence on yeast prions."xsd:string |
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