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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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SUMOylation in Neurological Diseases

Current Molecular Medicine, 2017
Since 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 ...
Zhongwen Luo   +10 more
openaire   +3 more sources

Concepts in sumoylation: a decade on

Nature Reviews Molecular Cell Biology, 2007
A decade has passed since SUMO (small ubiquitin-related modifier) was discovered to be a reversible post-translational protein modifier. During this time many enzymes that participate in regulated SUMO-conjugation and -deconjugation pathways have been identified and characterized.
Ruth Geiss-Friedlander, Frauke Melchior
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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
openaire   +2 more sources

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
openaire   +3 more sources

Modification of MDMX by sumoylation

Biochemical and Biophysical Research Communications, 2005
MDMX is a homolog of MDM2 and is critical for regulating p53 function during mouse development. MDMX level is regulated by MDM2-mediated poly-ubiquitination, which results in its accelerated degradation after DNA damage or expression of ARF. In this report, we demonstrate that MDMX can be modified by conjugation to SUMO-1 both in vivo and in vitro.
Yu Pan, Jiandong Chen
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Analysis of Protein Sumoylation

Current Protocols in Protein Science, 2006
AbstractThe 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
openaire   +2 more sources

Sumoylation and Apoptosis

2009
Apoptosis is a physiological mechanism to maintain human tissues or cells, and pathological dysfunction of this process explains some disease states or drug resistance. P53, mdm2, sumoylation, signal transduction, and transcriptional control are important in regulation in cancer cells.
Yuko Mishima   +3 more
openaire   +2 more sources

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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SUMOylation of SUMOylation proteins

Reactome - a curated knowledgebase of biological pathways, 2018
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