Results 261 to 270 of about 37,758 (275)
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Sumoylation in liver disease

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 ...
Wenhui Liu, Nian Fu, Yang Hu, Min Zeng
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SUMOylation in Neuroplasticity and Neurological Disorders [PDF]

open access: possibleNeuroMolecular Medicine, 2013
[No abstract available]
Feligioni, M   +2 more
openaire   +3 more sources

The Role of Sumoylation in Senescence

2009
Cellular senescence is a program initiated by many stress signals including aberrant activation of oncogenes, DNA damage, oxidative lesions and telomere attrition. Once engaged senescence irreversibly limits cellular proliferation and potently prevents tumor formation in vivo.
Sebastian Haferkamp   +2 more
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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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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.
openaire   +4 more sources

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

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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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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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
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