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| http://purl.uniprot.org/citations/21081964 | http://www.w3.org/2000/01/rdf-schema#comment | "Despite their distinct biological functions, there is a surprising similarity between the composition of the machinery that imports proteins into peroxisomes and the machinery that degrades endoplasmic reticulum (ER)-associated proteins. The basis of this similarity lies in the fact that both machineries make use of the same basic mechanistic principle: the tagging of a substrate by monoubiquitylation or polyubiquitylation and its subsequent recognition and ATP-dependent removal from a membrane by ATPases of the ATPases associated with diverse cellular activities (AAA) family of proteins. We propose that the ER-associated protein degradation (ERAD)-like removal of the peroxisomal import receptor is mechanically coupled to protein translocation into the organelle, giving rise to a new concept of export-driven import."xsd:string |
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| http://purl.uniprot.org/citations/21081964 | http://purl.uniprot.org/core/author | "Schliebs W."xsd:string |
| http://purl.uniprot.org/citations/21081964 | http://purl.uniprot.org/core/author | "Erdmann R."xsd:string |
| http://purl.uniprot.org/citations/21081964 | http://purl.uniprot.org/core/author | "Girzalsky W."xsd:string |
| http://purl.uniprot.org/citations/21081964 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/21081964 | http://purl.uniprot.org/core/name | "Nat Rev Mol Cell Biol"xsd:string |
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| http://purl.uniprot.org/citations/21081964 | http://purl.uniprot.org/core/title | "Peroxisomal protein import and ERAD: variations on a common theme."xsd:string |
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