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Sumoylation in neurodegenerative diseases

Cellular and Molecular Life Sciences, 2012
The yeast SUMO (small ubiquitin-like modifier) orthologue SMT3 was initially discovered in a genetic suppressors screen for the centromeric protein Mif2 (Meluh and Koshland in Mol Bio Cell 6:793-807, 1). Later, it turned out that the homologous mammalian proteins SUMO1 to SUMO4 are reversible protein modifiers that can form isopeptide bonds with lysine
Petranka, Krumova, Jochen H, Weishaupt
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Introduction to Sumoylation

2009
Reversible post-translational modification is a rapid and efficient system to control the activity of pre-existing proteins. Modifiers range from small chemical moieties, such as phosphate groups, to proteins themselves as the modifier. The patriarch of the protein modifiers is ubiquitin which plays a central role in protein degradation and protein ...
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SUMOylation in Neurodegenerative Diseases

Gerontology, 2019
Posttranslational modifications are ubiquitous regulators of cellular processes. The regulatory role of SUMOylation, the attachment of a small ubiquitin-related modifier to a target protein, has been implicated in fundamental processes like cell division, DNA damage repair, mitochondrial homeostasis, and stress responses.
Princz, Andrea, Tavernarakis, Nektarios
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Inflammasome SUMOylation

Science Signaling, 2018
NLRP3 inflammasome activity is inhibited by SUMOylation.
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Analysis of Sumoylation

2008
Reversible attachment of SUMO (small ubiquitin related modifi er) regulates a large number of proteins and plays an important role in processes such as transcriptional regulation, nucleo-cytoplasmic transport, genome integrity, and cell cycle progression.
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Synaptic Sumoylation

Science's STKE, 2007
Sumoylation--the posttranslational modification of proteins with the small ubiquitin-like modifier protein (SUMO)--is most familiar in the context of transcriptional regulation and nuclear transport; increasingly, however, roles for extranuclear sumoylation have begun to surface. Martin et al .
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Detection of Sumoylated Proteins

2008
Small ubiquitin-related modifier (SUMO) is an ubiquitin-like protein that is covalently attached to a variety of target proteins. Unlike ubiquitination, sumoylation does not target proteins for proteolytic breakdown, but is instead involved in regulating a variety of different protein functional properties, including protein-protein interactions and ...
Ok-Kyong, Park-Sarge, Kevin D, Sarge
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Sumoylating NEMO

Science's STKE, 2003
Huang et al. investigated activation of the transcription factor nuclear factor-κB (NF-κB) and implicated two distinct signaling pathways in the response to genotoxic stress. NF-κB, which mediates cellular responses to stress, is sequestered in the cytoplasm through interactions with its inhibitors, IκBα and IκBβ ...
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Sumoylation in Craniofacial Disorders

2009
Craniofacial development requires a complex series of coordinated and finely tuned events to take place, during a relatively short time frame. These events are set in motion by switching on and off transcriptional cascades that involve the use of numerous signalling pathways and a multitude of factors that act at the site of gene transcription.
Erwin, Pauws, Philip, Stanier
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Analysis of Protein Sumoylation

Current Protocols in Protein Science, 2016
AbstractSumoylation, wherein small ubiquitin‐like modifier (SUMO) proteins are covalently attached to specific lysine residues of target proteins, plays an important role in regulating many diverse cellular processes via its control of the functional properties of the modified proteins.
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