Results 11 to 20 of about 31,613 (261)
SUMOylation and De-SUMOylation: Wrestling with Life's Processes [PDF]
Journal of Biological Chemistry, 2008 The small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large number of cellular proteins. SUMO modification has emerged as an important regulatory mechanism for protein function and localization. SUMOylation is a dynamic process that is mediated by activating (E1), conjugating (E2), and ligating (E3) enzymes and
Edward T.H. Yeh
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SUMOylation and de‐SUMOylation in response to DNA damage [PDF]
FEBS Letters, 2011 To maintain genomic integrity, a cell must utilize multiple mechanisms to protect its DNA from the damage generated by environmental agents or DNA metabolism. SUMO (small ubiquitin‐like modifier) can regulate protein stability, protein cellular location, and protein–protein interactions.
Chao Huang +5 more
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Retrovirology, 2013 Background The HIV virus hijacks cellular machineries to replicate. Post-translational modifications, like acetylation, phosphorylation or ubiquitination, are no exception. We are interested in studying the interplay between HIV and the SUMOylation pathway.
Beauclair, Guillaume +2 more
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PML, SUMOylation, and Senescence [PDF]
Frontiers in Oncology, 2013 Since its discovery, 25 years ago, promyelocytic leukemia (PML) has been an enigma. Implicated in the oncogenic PML/RARA fusion, forming elusive intranuclear domains, triggering cell death or senescence, controlled by and perhaps controlling SUMOylation… there are multiple PML-related issues.
Hugues eDe Thé +10 more
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eLife, 2021 The post-translational modification of histones by the small ubiquitin-like modifier (SUMO) protein has been associated with gene regulation, centromeric localization, and double-strand break repair in eukaryotes.
Calvin Jon A Leonen +12 more
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Frontiers in Cell and Developmental Biology, 2021 Protein sumoylation is one of the most important post-translational modifications regulating many biological processes (Flotho A & Melchior F. 2013. Ann Rev. Biochem. 82:357–85).
Qian Nie +21 more
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SUMOylation in development and neurodegeneration [PDF]
Development, 2020 ABSTRACT In essentially all eukaryotes, proteins can be modified by the attachment of small ubiquitin-related modifier (SUMO) proteins to lysine side chains to produce branched proteins. This process of ‘SUMOylation’ plays essential roles in plant and animal development by altering protein function in spatially and temporally controlled ...
Tak-Yu Yau +2 more
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The Role of Sumoylation in the Response to Hypoxia: An Overview
Cells, 2020 Sumoylation is the covalent attachment of the small ubiquitin-related modifier (SUMO) to a vast variety of proteins in order to modulate their function. Sumoylation has emerged as an important modification with a regulatory role in the cellular response ...
Chrysa Filippopoulou +2 more
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Regulation of Smoothened Trafficking and Abundance in Hedgehog Signaling
Frontiers in Cell and Developmental Biology, 2022 The GPCR-family protein Smoothened (Smo) is essential for Hedgehog (Hh) signal transduction in both insects and vertebrates. The regulation of subcellular localization and abundance of Smo is a critical step in Hh signaling.
Jianhang Jia, Jin Jiang
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Analysis of PTP1B sumoylation [PDF]
Methods, 2014 Signaling enzymes are typically regulated by a variety of post-translational modifications. One such enzyme, protein tyrosine phosphatase (PTP) 1B, which plays an important role in metabolic and growth signaling, has recently been shown to be inhibited by posttranslational modifications by ubiquitin-related proteins of the SUMO family.
Sayanti Saha, Jonathan Chernoff
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