| http://purl.uniprot.org/citations/16873066 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16873066 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16873066 | http://www.w3.org/2000/01/rdf-schema#comment | "Many misfolded endoplasmic reticulum (ER) proteins are eliminated by ERAD, a process in which substrates are polyubiquitylated and moved into the cytosol for proteasomal degradation. We have identified in S. cerevisiae distinct ubiquitin-ligase complexes that define different ERAD pathways. Proteins with misfolded ER-luminal domains use the ERAD-L pathway, in which the Hrd1p/Hrd3p ligase forms a near stoichiometric membrane core complex by binding to Der1p via the linker protein Usa1p. This core complex associates through Hrd3p with Yos9p, a substrate recognition protein in the ER lumen. Substrates with misfolded intramembrane domains define a pathway (ERAD-M) that differs from ERAD-L by being independent of Usa1p and Der1p. Membrane proteins with misfolded cytosolic domains use the ERAD-C pathway and are directly targeted to the Doa10p ubiquitin ligase. All three pathways converge at the Cdc48p ATPase complex. These results lead to a unifying concept for ERAD that may also apply to mammalian cells."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2006.05.043"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2006.05.043"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/author | "Rapoport T.A."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/author | "Rapoport T.A."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/author | "Carvalho P."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/author | "Carvalho P."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/author | "Goder V."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/author | "Goder V."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/pages | "361-373"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/pages | "361-373"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/title | "Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/title | "Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins."xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/volume | "126"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://purl.uniprot.org/core/volume | "126"xsd:string |
| http://purl.uniprot.org/citations/16873066 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16873066 |
| http://purl.uniprot.org/citations/16873066 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16873066 |
| http://purl.uniprot.org/citations/16873066 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16873066 |
| http://purl.uniprot.org/citations/16873066 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16873066 |