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.) ...
Analysis of the SUMO2 Proteome during HSV-1 Infection.
Glasgow, United Kingdom. In Plos Pathog, 31 Jul 2015
Covalent linkage to members of the small ubiquitin-like (SUMO) family of proteins is an important mechanism by which the functions of many cellular proteins are regulated.
[Research on Molecular Biological Characteristics of Proto-oncogene pim-2].
In Sheng Wu Yi Xue Gong Cheng Xue Za Zhi, Apr 2015
A plurality of covalent modification sites, two ubiquitination sites, four glycosylation sites, an SUMO sumoylation site, a nitrosation site, two palmitoylation sites and sixteen regions with higher antigenic index were distributed in the protein sequence.
Sumo and the cellular stress response.
Oslo, Norway. In Cell Div, Dec 2014
The ubiquitin family member Sumo has important functions in many cellular processes including DNA repair, transcription and cell division.
Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity.
Gold Coast, Australia. In Biomolecules, Dec 2014
UNASSIGNED: 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.