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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Sharma, Rohit | - |
| dc.contributor.author | Chirom, Oceania | - |
| dc.contributor.author | Mujib, Abdul | - |
| dc.contributor.author | Prasad, Manoj | - |
| dc.contributor.author | Prasad, Ashish | - |
| dc.date.accessioned | 2025-02-27T07:10:47Z | - |
| dc.date.available | 2025-02-27T07:10:47Z | - |
| dc.date.issued | 2025 | - |
| dc.identifier.citation | Plant Science, 354: 112435 | en_US |
| dc.identifier.issn | 1873-2259 | - |
| dc.identifier.issn | 0168-9452 | - |
| dc.identifier.other | https://doi.org/10.1016/j.plantsci.2025.112435 | - |
| dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0168945225000536?via%3Dihub | - |
| dc.identifier.uri | http://223.31.159.10:8080/jspui/handle/123456789/1695 | - |
| dc.description | Accepted date: 18 February 2025 | en_US |
| dc.description.abstract | Ubiquitination is a highly conserved post-translational modification (PTM) in which ubiquitin (Ub) is covalently attached to substrate proteins resulting in the alteration of protein structure, function, and stability. Another class of PTM mediated by ubiquitin-like proteins (UBLs) has gained significant attention among researchers in recent years. This article focuses on one such UBL-mediated PTM i.e. UFMylation. The enzymatic mechanism of UFMylation is similar to ubiquitination, involving three steps regulated by three different enzymes. In plants, reports suggest that UFMylation is predominantly involved in maintaining ER homeostasis including ER-phagy. However, studies related to this PTM are limited and future studies might reveal other molecular pathways regulated by UFMylation. | en_US |
| dc.description.sponsorship | Authors’ work is supported by Startup Research Grant from Science and Engineering Research Board (SERB), Govt. of India, India (SRG/2023/000578) and INSPIRE Faculty Research Grant from Department of Science and Technology, Govt. of India, India (IFA22-LSPA 152). RS acknowledges the fellowship received from the University Grants Commission, Govt. of India. | en_US |
| dc.language.iso | en_US | en_US |
| dc.publisher | Elsevier B.V. | en_US |
| dc.subject | PTM | en_US |
| dc.subject | UBLs | en_US |
| dc.subject | UFMylation | en_US |
| dc.subject | Ubiquitin | en_US |
| dc.subject | ER homeostasis | en_US |
| dc.title | UFMylation: Exploring a lesser known post translational modification | en_US |
| dc.type | Article | en_US |
| Appears in Collections: | Institutional Publications | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Prasad M_2025_1.pdf Restricted Access | 1.66 MB | Adobe PDF | View/Open Request a copy |
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