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| http://purl.uniprot.org/citations/8031301 | http://www.w3.org/2000/01/rdf-schema#comment | "The Y-box proteins are the most evolutionarily conserved nucleic acid binding proteins yet defined in bacteria, plants and animals. The central nucleic acid binding domain of the vertebrate proteins is 43% identical to a 70-amino-acid-long protein (CS7.4) from E. coli. The structure of this domain consists of an antiparallel five-stranded beta-barrel that recognizes both DNA and RNA. The diverse biological roles of these Y-box proteins range from the control of the E. coli cold-shock stress response to the translational masking of messenger RNA in vertebrate gametes. This review discusses the organization of the prokaryotic and eukaryotic Y-box proteins, how they interact with nucleic acids, and their biological roles, both proven and potential."xsd:string |
| http://purl.uniprot.org/citations/8031301 | http://purl.org/dc/terms/identifier | "doi:10.1002/bies.950160407"xsd:string |
| http://purl.uniprot.org/citations/8031301 | http://purl.uniprot.org/core/author | "Wolffe A.P."xsd:string |
| http://purl.uniprot.org/citations/8031301 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8031301 | http://purl.uniprot.org/core/name | "Bioessays"xsd:string |
| http://purl.uniprot.org/citations/8031301 | http://purl.uniprot.org/core/pages | "245-251"xsd:string |
| http://purl.uniprot.org/citations/8031301 | http://purl.uniprot.org/core/title | "Structural and functional properties of the evolutionarily ancient Y-box family of nucleic acid binding proteins."xsd:string |
| http://purl.uniprot.org/citations/8031301 | http://purl.uniprot.org/core/volume | "16"xsd:string |
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