Results 211 to 220 of about 35,698 (247)
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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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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, Shengfang Ge, Xianqun Fan
exaly +3 more sources
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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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 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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The Role of Sumoylation in Senescence
2009Cellular 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.
Lyndee L, Scurr +2 more
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Sumoylation in Development and Differentiation
2009Tissue morphogenesis is a fascinating aspect of both developmental biology and regeneration of certain adult organs, and timely control of cellular differentiation is a key to these processes. During development, events interrupting cellular differentiation and leading to organ failure are embryonic lethal; likewise, perturbation of differentiation in ...
Adeline F, Deyrieux, Van G, Wilson
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Concepts in sumoylation: a decade on
Nature Reviews Molecular Cell Biology, 2007A 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 +1 more
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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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Modification of MDMX by sumoylation
Biochemical and Biophysical Research Communications, 2005MDMX 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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Detection of Sumoylated Proteins
2008Small 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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