Please use this identifier to cite or link to this item:
https://doi.org/10.3389/fcell.2021.673647
DC Field | Value | |
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dc.title | Protein Lipidation by Palmitoylation and Myristoylation in Cancer | |
dc.contributor.author | Fhu, Chee Wai | |
dc.contributor.author | Ali, Azhar | |
dc.date.accessioned | 2022-06-07T09:05:06Z | |
dc.date.available | 2022-06-07T09:05:06Z | |
dc.date.issued | 2021-05-20 | |
dc.identifier.citation | Fhu, Chee Wai, Ali, Azhar (2021-05-20). Protein Lipidation by Palmitoylation and Myristoylation in Cancer. FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY 9. ScholarBank@NUS Repository. https://doi.org/10.3389/fcell.2021.673647 | |
dc.identifier.issn | 2296-634X | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/226655 | |
dc.description.abstract | Posttranslational modification of proteins with lipid moieties is known as protein lipidation. The attachment of a lipid molecule to proteins endows distinct properties, which affect their hydrophobicity, structural stability, localization, trafficking between membrane compartments, and influences its interaction with effectors. Lipids or lipid metabolites can serve as substrates for lipidation, and the availability of these lipid substrates are tightly regulated by cellular metabolism. Palmitoylation and myristoylation represent the two most common protein lipid modifications, and dysregulation of protein lipidation is strongly linked to various diseases such as metabolic syndromes and cancers. In this review, we present recent developments in our understanding on the roles of palmitoylation and myristoylation, and their significance in modulating cancer metabolism toward cancer initiation and progression. | |
dc.language.iso | en | |
dc.publisher | FRONTIERS MEDIA SA | |
dc.source | Elements | |
dc.subject | Science & Technology | |
dc.subject | Life Sciences & Biomedicine | |
dc.subject | Cell Biology | |
dc.subject | Developmental Biology | |
dc.subject | protein lipidation | |
dc.subject | palmitoylation | |
dc.subject | myristoylation | |
dc.subject | depalmitoylation | |
dc.subject | metabolism | |
dc.subject | cancer | |
dc.subject | TRIS DIBENZYLIDENEACETONE DIPALLADIUM | |
dc.subject | N-MYRISTOYLTRANSFERASE | |
dc.subject | MEMBRANE-BINDING | |
dc.subject | DYNAMIC PALMITOYLATION | |
dc.subject | POTENT INHIBITORS | |
dc.subject | S-PALMITOYLATION | |
dc.subject | THIOESTERASES 1 | |
dc.subject | DBA PALLADIUM | |
dc.subject | PALMOSTATIN B | |
dc.subject | FATTY-ACIDS | |
dc.type | Review | |
dc.date.updated | 2022-06-07T01:33:04Z | |
dc.contributor.department | CANCER SCIENCE INSTITUTE OF SINGAPORE | |
dc.description.doi | 10.3389/fcell.2021.673647 | |
dc.description.sourcetitle | FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY | |
dc.description.volume | 9 | |
dc.published.state | Published | |
dc.description.redeposit | completed | |
Appears in Collections: | Staff Publications Elements |
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Files in This Item:
File | Description | Size | Format | Access Settings | Version | |
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Protein Lipidation by Palmitoylation and Myristoylation in Cancer.pdf | 2.23 MB | Adobe PDF | OPEN | None | View/Download | |
2021_FrontiersCDB.pdf | 2.23 MB | Adobe PDF | OPEN | None | View/Download |
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