SUMO-2/3 regulates topoisomerase II in mitosis
In The Journal of Cell Biology, 1986
... The processed and full-length forms of SUMO-2 and -3 were cloned into pGEX4T-1, fused at their NH2 termini to an EGFP fragment that was excised from a pEGFP C-1 plasmid (CLONTECH Laboratories, Inc.) ...
Role of RSUME in inflammation and cancer.
Buenos Aires, Argentina. In Febs Lett, 14 Dec 2015
RSUME enhances SUMO conjugation by interacting with the SUMO conjugase Ubc9, increases Ubc9 thioester formation and therefore favors sumoylation of specific targets.
Evolution of SUMO function and chain formation in insects.
Barcelona, Spain. In Mol Biol Evol, 04 Dec 2015
UNASSIGNED: SUMOylation, the covalent binding of Small Ubiquitin-like Modifier (SUMO) to target proteins, is a posttranslational modification that regulates critical cellular processes in eukaryotes.
Use of the Nanofitin Alternative Scaffold as a GFP-Ready Fusion Tag.
Nantes, France. In Plos One, Dec 2014
To illustrate the potential of the Nanofitin-based tag as a fusion partner, we compared the expression level in Escherichia coli and activity profile of recombinant human tumor necrosis factor alpha (TNFα) constructs, fused to a SUMO or GFP-ready tag.
Viral Mimicry to Usurp Ubiquitin and SUMO Host Pathways.
Nürnberg, Germany. In Viruses, Dec 2014
Posttranslational modifications (PTMs) of proteins include enzymatic changes by covalent addition of cellular regulatory determinants such as ubiquitin (Ub) and small ubiquitin-like modifier (SUMO) moieties.
Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity.
Gold Coast, Australia. In Biomolecules, Dec 2014
α-Synuclein inclusion bodies are a pathological hallmark of several neurodegenerative diseases, including Parkinson's disease, and contain aggregated α-synuclein and a variety of recruited factors, including protein chaperones, proteasome components, ubiquitin and the small ubiquitin-like modifier, SUMO-1.