Results 41 to 50 of about 1,958,325 (325)
Preserving genome integrity: The vital role of SUMO-targeted ubiquitin ligases
Cell Insight, 2023 Various post-translational modifications (PTMs) collaboratively fine-tune protein activities. SUMO-targeted ubiquitin E3 ligases (STUbLs) emerge as specialized enzymes that recognize SUMO-modified substrates through SUMO-interaction motifs and ...
Jinhua Han, Yanhua Mu, Jun Huang
doaj +1 more source
Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9 [PDF]
Angewandte Chemie International Edition, 2016 AbstractConjugation of the small ubiquitin‐like modifier (SUMO) to protein substrates is an important disease‐associated posttranslational modification, although few inhibitors of this process are known. Herein, we report the discovery of an allosteric small‐molecule binding site on Ubc9, the sole SUMO E2 enzyme.
D. Needle +14 more
openaire +4 more sources
International Journal of Molecular Sciences, 2022 DNA damage in early-stage embryos impacts development and is a risk factor for segregation of altered genomes. DNA damage response (DDR) encompasses a sophisticated network of proteins involved in sensing, signaling, and repairing damage.
Zigomar da Silva +7 more
semanticscholar +1 more source
A Method for SUMO Modification of Proteins in vitro
Bio-Protocol, 2018 The Small Ubiquitin-related Modifier (SUMO) is a protein that is post-translationally added to and reversibly removed from other proteins in eukaryotic cells.
Christine Lee +3 more
doaj +1 more source
The SUMO Ligase Protein Inhibitor of Activated STAT 1 (PIAS1) is a constituent PML-NB protein that contributes to the intrinsic antiviral immune response to herpes simplex virus 1 (HSV-1) [PDF]
, 2016 Aspects of intrinsic antiviral immunity are mediated by promyelocytic leukaemia (PML)-nuclear body (PML-NB) constituent proteins. During herpesvirus infection, these antiviral proteins are independently recruited to nuclear domains that contain infecting
Boutell, Chris +7 more
core +1 more source
SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability
International Journal of Molecular Sciences, 2021 Small ubiquitin-like modifier (SUMO)-targeted E3 ubiquitin ligases (STUbLs) are specialized enzymes that recognize SUMOylated proteins and attach ubiquitin to them. They therefore connect the cellular SUMOylation and ubiquitination circuits.
Ya-Chu Chang +2 more
semanticscholar +1 more source
The SUMO conjugating enzyme UBC9 as a biomarker for cervical HPV infections [PDF]
ecancermedicalscience, 2015 Human papillomaviruses (HPVs) infect stratified epithelium and are the causative agents of cervical cancer, the second most common cause of cancer-related death in women. A critical aspect that still persists in the HPV field is the selection of very sensitive and specific HPV diagnostic assays.
Mattoscio D. +4 more
openaire +3 more sources
Versatile recombinant SUMOylation system for the production of SUMO-modified protein. [PDF]
PLoS ONE, 2014 Posttranslational modification by small ubiquitin-like modifiers (SUMO) is being associated with a growing number of regulatory functions in diverse cellular processes.
Alain R Weber +2 more
doaj +1 more source
Physiological Reviews, 2020 Sentrin/small ubiquitin-like modifier (SUMO) is protein modification pathway that regulates multiple biological processes, including cell division, DNA replication/repair, signal transduction, and cellular metabolism.
Hui-Ming Chang, E. Yeh
semanticscholar +1 more source
A role for S-nitrosylation of the SUMO-conjugating enzyme SCE1 in plant immunity [PDF]
Proceedings of the National Academy of Sciences, 2019 Significance S-nitrosylation, the addition of a nitric oxide (NO) moiety to a reactive protein cysteine (Cys) thiol to form an S-nitrosothiol (SNO), is emerging as a pivotal redox-based, posttranslational modification (PTM) during plant immune function.
Steven H. Spoel +7 more
openaire +4 more sources