論文 - 詳細
| RRC ID | 36196 |
|---|---|
| 著者 | Nakatsukasa K, Kamura T, Brodsky JL. |
| タイトル | Recent technical developments in the study of ER-associated degradation. |
| ジャーナル | Curr Opin Cell Biol |
| Abstract |
Endoplasmic reticulum-associated degradation (ERAD) is a mechanism during which native and misfolded proteins are recognized and retrotranslocated across the ER membrane to the cytosol for degradation by the ubiquitin-proteasome system. Like other cellular pathways, the factors required for ERAD have been analyzed using both conventional genetic and biochemical approaches. More recently, however, an integrated top-down approach has identified a functional network that underlies the ERAD system. In turn, bottom-up reconstitution has become increasingly sophisticated and elucidated the molecular mechanisms underlying substrate recognition, ubiquitylation, retrotranslocation, and degradation. In addition, a live cell imaging technique and a site-specific in vivo photo-crosslinking approach have further dissected specific steps during ERAD. These technical developments have revealed an unexpected dynamicity of the membrane-associated ERAD complex. In this article, we will discuss how these technical developments have improved our understanding of the ERAD pathway and have led to new questions. |
| 巻・号 | 29 |
| ページ | 82-91 |
| 公開日 | 2014-8-1 |
| DOI | 10.1016/j.ceb.2014.04.008 |
| PII | S0955-0674(14)00050-7 |
| PMID | 24867671 |
| PMC | PMC4130770 |
| MeSH | Animals Endoplasmic Reticulum / metabolism* Endoplasmic Reticulum-Associated Degradation* Humans Proteasome Endopeptidase Complex / metabolism Protein Binding Proteins / metabolism Ubiquitination |
| IF | 8.24 |
| 引用数 | 17 |
| WOS 分野 | CELL BIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 各媒体での言及数の合計 | 0 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
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