ReviewGenomics, proteomics & bioinformatics2016
UFMylation: A Unique & Fashionable Modification for Life.
Review in Genomics, proteomics & bioinformatics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 89 citations in OpenAlex.
- cGAS in nucleus: The link between immune response and DNA damage repair.Frontiers in immunology · 2022Pooled it
- Narrative review-the emerging role, functions, and mechanisms of UFMylation in cancers.Translational cancer research · 2026Review
- A Practical Experimental Protocol for Identification and Validation of UFMylation Substrate in Human Cells.Bio-protocol · 2026Article
- Optimization of protein UFMylation modification method and its application in substrate identification in human cells.The Journal of biological chemistry · 2026Article
- UFMylation maintains tumor suppressor pVHL stability by activating the deubiquitinase BAP1.Science advances · 2025Article
- Article
- The Role of UFMylation in the Development and Progression of Gastric Cancer.Oncology research · 2025Review
- Mithramycin targets head and neck cancer stem cells by inhibiting Sp1 and UFMylation.Cancer cell international · 2024Article
- The emerging roles of UFMylation in the modulation of immune responses.Clinical and translational medicine · 2024Review
- Role of UFMylation in tumorigenesis and cancer immunotherapy.Frontiers in immunology · 2024Review
- Review
- Ufmylation on UFBP1 alleviates non-alcoholic fatty liver disease by modulating hepatic endoplasmic reticulum stress.Cell death & disease · 2023Article
- The Role of Endoplasmic Reticulum Stress Response in Liver Regeneration.Seminars in liver disease · 2023Review
- A neuroprotective role of Ufmylation through Atg9 in the aging brain of Drosophila.Cellular and molecular life sciences : CMLS · 2023Article
- A hybrid deep forest-based method for predicting synergistic drug combinations.Cell reports methods · 2023Article
- UFL1 promotes antiviral immune response by maintaining STING stability independent of UFMylation.Cell death and differentiation · 2023Article
- UFL1, a UFMylation E3 ligase, plays a crucial role in multiple cellular stress responses.Frontiers in endocrinology · 2023Review
- UFL1 alleviates ER stress and apoptosis stimulated by LPS via blocking the ferroptosis pathway in human granulosa-like cells.Cell stress & chaperones · 2022Article
- Disulfiram Oxy-Derivatives Suppress Protein Retrotranslocation across the ER Membrane to the Cytosol and Initiate Paraptosis-like Cell Death.Membranes · 2022Article
- DDRGK1 is required for the proper development and maintenance of the growth plate cartilage.Human molecular genetics · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitin-fold modifier 1 (UFM1) is one of the newly-identified ubiquitin-like proteins. Similar to ubiquitin, UFM1 is conjugated to its target proteins by a three-step enzymatic reaction. The UFM1-activating enzyme, ubiquitin-like modifier-activating enzyme 5 (UBA5), serves as the E1 to activate UFM1; UFM1-conjugating enzyme 1 (UFC1) acts as the E2 to transfer the activated UFM1 to the active site of the E2; and the UFM1-specific ligase 1 (UFL1) acts as the E3 to recognize its substrate, transfer, and ligate the UFM1 from E2 to the substrate. This process is called ufmylation. UFM1 chains can be cleaved from its target proteins by UFM1-specific proteases (UfSPs), suggesting that the ufmylation modification is reversible. UFM1 cascade is conserved among nearly all of the eukaryotic organisms, but not in yeast, and associated with several cellular activities including the endoplasmic reticulum stress response and hematopoiesis. Furthermore, the UFM1 cascade is closely related to a series of human diseases. In this review, we summarize the molecular details of this reversible modification process, the recent progress of its functional studies, as well as its implication in tumorigenesis and potential therapeutic targets for cancer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.