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- Fumiyo Ikeda
- Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan
抄録
<jats:p> Ubiquitin regulates a wide variety of biological functions by modifying diverse substrates, via many different conjugation types. Classically, the C-terminus of ubiquitin conjugates to protein substrates via an isopeptide or peptide bond. Recent studies revealed that ubiquitin can form an atypical oxyester bond, which can target protein and even nonproteinaceous substrates, including sugars and lipids. How nonprotein ubiquitination affects substrate and cellular functions is incompletely understood. This review covers recent discoveries in ubiquitination and its potential impacts on biology. </jats:p>
収録刊行物
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- American Journal of Physiology-Cell Physiology
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American Journal of Physiology-Cell Physiology 324 (5), C1053-C1060, 2023-05-01
American Physiological Society
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詳細情報 詳細情報について
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- CRID
- 1360298754845775232
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- ISSN
- 15221563
- 03636143
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- データソース種別
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- Crossref
- KAKEN