Multi-dimensional global proteomics describes the SUMO-modified proteome during meiosis and reveals novel roles in regulating the key events of meiotic chromosome metabolism.

SUMO-dependent pathway is responsible for selective repression of damaged rDNA and silencing of intact surplus units revealing an epigenetic mechanism that controls the differential expression of identical sequences in the same cell.

Wss1 is both a metalloprotease and SUMO ligase found in association with Cdc48 and Doa1 and accumulating in the vacuole upon DNA damage.

Analyses using His6-HA-SUMO1 and SUMO1 KO mice indicate that SUMO1 modification of synaptic proteins is either absent or cannot be detected in brain and cultured neurons.

The SUMO-Ub-Cdc48 pathway is a novel regulatory mechanism of Pol III and a potential therapeutic target for Pol III-related human diseases.

The immediate response of the brain to a sudden, harmful drop in oxygen supply is the addition of SUMO proteins to sodium ion channels in neurons, increasing their activity.

The FDA-approved compound and plant extract tannic acid is a non-toxic chemical tool for modulating sumoylation in multiple platforms.

Simulations of molecular dynamics suggest how the binding of the β-grasp domain of SUMO1 induces conformational and dynamic effects to activate SENP1.

SUMOylation regulates mitochondrial UPR signaling through modulation of transcription factors DVE-1 and ATFS-1.

The transcriptomic profiles of the constituent monotherapies of synergistic drug pairs tend to be correlated and result in novel gene expression in the combinations.