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Author Correction: TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence. [PDF]
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Targeting SUMOylation in cancer
Current Opinion in Oncology, 2021Purpose of review In the article, we focus on the role of SUMOylation in tumorigenesis and cancer-related processes, including Epithelial–mesenchymal transition (EMT), metastasis, resistance to cancer therapies, and antitumor immunity. Clinical perspective on small ubiquitin-like modifier (SUMO) inhibitors will be discussed.
Li, Du, Wei, Liu, Steven T, Rosen
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SUMOylation in atherosclerosis
Clinica Chimica Acta, 2020Atherosclerosis (AS) is the pathophysiologic basis of many cardiovascular diseases. A number of studies have shown that post-translational modification (PTM) contributes to the initiation and progression of AS. For example, recent studies found that SUMOylation, ie, small ubiquitin-like modifier (SUMO) conjugation to target substrate proteins, was ...
Yi-Zhang Liu +6 more
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2019
Protein regulation by reversible attachment of SUMO (small ubiquitin-related modifier) plays an important role in several cellular processes such as transcriptional regulation, nucleo-cytoplasmic transport, cell-cycle progression, meiosis, and DNA repair.
Breucker , J., Pichler, A.
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Protein regulation by reversible attachment of SUMO (small ubiquitin-related modifier) plays an important role in several cellular processes such as transcriptional regulation, nucleo-cytoplasmic transport, cell-cycle progression, meiosis, and DNA repair.
Breucker , J., Pichler, A.
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Biochemical Society Transactions, 2007
Polycomb proteins are key regulators of transcription in metazoan organisms. Recent work has shed light on the nature of the polycomb protein complexes in flies and mammalian cells. Multiple enzymatic activities have been shown to associate with polycomb complexes, including histone methyltransferase, histone deacetylase and ubiquitination activities ...
D, Wotton, J C, Merrill
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Polycomb proteins are key regulators of transcription in metazoan organisms. Recent work has shed light on the nature of the polycomb protein complexes in flies and mammalian cells. Multiple enzymatic activities have been shown to associate with polycomb complexes, including histone methyltransferase, histone deacetylase and ubiquitination activities ...
D, Wotton, J C, Merrill
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Cancer Letters, 2012
SUMOylation is a post-translational modification characterized by covalent and reversible binding of small ubiquitin-like modifier (SUMO) to a target protein. In mammals, four different isoforms, termed SUMO-1, -2, -3 and -4 have been identified so far.
Bettermann +4 more
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SUMOylation is a post-translational modification characterized by covalent and reversible binding of small ubiquitin-like modifier (SUMO) to a target protein. In mammals, four different isoforms, termed SUMO-1, -2, -3 and -4 have been identified so far.
Bettermann +4 more
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SUMOylation homeostasis in tumorigenesis
Cancer Letters, 2020Small ubiquitin-like modifier (SUMO), a critical regulatory modification protein, is involved in various biological processes, such as gene expression, genome maintenance and DNA damage repair (DDR). Numerous recent studies have revealed that disturbed SUMOylation and deSUMOylation homeostasis contribute to tumorigenesis.
Minyue, Xie +4 more
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Clinica Chimica Acta, 2020
Small ubiquitin-like modifiers (SUMO) are highly conserved post-translational modification proteins that are present in eukaryotic cells. They are extensively expressed in diverse tissues, including the heart, liver, kidney, and lungs. SUMOylation, a crucial post-translational modification, exhibits a strong effect on DNA repair, transcriptional ...
Min, Zeng +3 more
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Small ubiquitin-like modifiers (SUMO) are highly conserved post-translational modification proteins that are present in eukaryotic cells. They are extensively expressed in diverse tissues, including the heart, liver, kidney, and lungs. SUMOylation, a crucial post-translational modification, exhibits a strong effect on DNA repair, transcriptional ...
Min, Zeng +3 more
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Analysis of Protein Sumoylation
Current Protocols in Protein Science, 2006AbstractThe covalent attachment of small ubiquitin‐like modifier (SUMO) proteins to specific lysine residues of target proteins, a process termed sumoylation, is a recently discovered protein modification that plays an important role in regulating many diverse cellular processes.
Roland S, Hilgarth, Kevin D, Sarge
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SUMOylation in Neurological Diseases
Current Molecular Medicine, 2017Since the discovery of SUMOs (small ubiquitin-like modifiers) over 20 years ago, sumoylation has recently emerged as an important posttranslational modification involved in almost all aspects of cellular physiology. In neurons, sumoylation dynamically modulates protein function and consequently plays an important role in neuronal maturation, synapse ...
F-Y, Liu +10 more
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