Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/1695
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dc.contributor.authorSharma, Rohit-
dc.contributor.authorChirom, Oceania-
dc.contributor.authorMujib, Abdul-
dc.contributor.authorPrasad, Manoj-
dc.contributor.authorPrasad, Ashish-
dc.date.accessioned2025-02-27T07:10:47Z-
dc.date.available2025-02-27T07:10:47Z-
dc.date.issued2025-
dc.identifier.citationPlant Science, 354: 112435en_US
dc.identifier.issn1873-2259-
dc.identifier.issn0168-9452-
dc.identifier.otherhttps://doi.org/10.1016/j.plantsci.2025.112435-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0168945225000536?via%3Dihub-
dc.identifier.urihttp://223.31.159.10:8080/jspui/handle/123456789/1695-
dc.descriptionAccepted date: 18 February 2025en_US
dc.description.abstractUbiquitination 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.sponsorshipAuthors’ 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.isoen_USen_US
dc.publisherElsevier B.V.en_US
dc.subjectPTMen_US
dc.subjectUBLsen_US
dc.subjectUFMylationen_US
dc.subjectUbiquitinen_US
dc.subjectER homeostasisen_US
dc.titleUFMylation: Exploring a lesser known post translational modificationen_US
dc.typeArticleen_US
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