Sumoylation in Physiology, Pathology and Therapy
Sumoylation is an essential post-translational modification that has evolved to regulate intricate networks within emerging complexities of eukaryotic cells.
Umut Sahin +2 more
doaj +1 more source
Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley +1 more source
The role of histone modifications in transcription regulation upon DNA damage
This review discusses the critical role of histone modifications in regulating gene expression during the DNA damage response (DDR). By modulating chromatin structure and recruiting repair factors, these post‐translational modifications fine‐tune transcriptional programmes to maintain genomic stability.
Angelina Job Kolady, Siyao Wang
wiley +1 more source
Protein SUMOylation and Its Research Progress in Maize
Small ubiquitin-like modification (SUMOylation) is a crucial post-translational modification of proteins that plays a vital role in various biological processes in plants.
Ruiqiang LAI +5 more
doaj +1 more source
Nuclear pore links Fob1‐dependent rDNA damage relocation to lifespan control
Damaged rDNA accumulates at a specific perinuclear interface that couples nucleolar escape with nuclear envelope association. Nuclear pores at this site help inhibit Fob1‐induced rDNA instability. This spatial organization of damage handling supports a functional link between nuclear architecture, rDNA stability, and replicative lifespan in yeast.
Yamato Okada +5 more
wiley +1 more source
Correction to 'SUMOylation of PUM2 promotes the vasculogenic mimicry of glioma cells via regulating CEBPD'. [PDF]
Clinical and Translational Medicine, Volume 16, Issue 1, January 2026.
europepmc +2 more sources
The proximity labeling enzyme APEX2 is displayed on extracellular vesicle (EV) surfaces via genetic fusion with EV‐sorting scaffolds, enabling in situ biotinylation of native surface proteins, adsorbed corona components, and interacting cellular proteins.
Wenyi Zheng +5 more
wiley +1 more source
Correlation between serum SUMO1 level and hypertriglyceridemia in type 2 diabetes mellitus patients
Objective·To explore the correlation between serum small ubiquitin-like modifier 1 (SUMO1) levels and hypertriglyceridemia in patients with type 2 diabetes mellitus (T2DM).Methods·A total of 239 newly diagnosed T2DM patients were recruited from the ...
ZHANG Xinyan +4 more
doaj +1 more source
Correlationship between total proteins SUMOylation and papillary thyroid carcinoma in males [PDF]
Objective To investigate the relationship between protein SUMOylation level and the prognosis of papillary thyroid carcinoma(PTC) in males. Methods Protein SUMOylation levels in PTC was analyzed by bioinformatics based on GTEx and TCGA databases and ...
WU Qiao, LIU Wei, ZHENG Jiaojiao, WANG Cong, AI Zhilong
doaj +1 more source
Ubc9-Mediated SUMOylation of RPL3, an Unappreciated Mechanism against Hepatocyte Senescence by Repressing the DHX9-p16 Axis. [PDF]
Liver aging is characterized by a decline in the expression of the SUMO‐conjugating enzyme Ubc9, resulting in reduced SUMOylation levels in hepatocytes, particularly in the case of ribosomal protein RPL3. Disruption of RPL3 SUMOylation increases its nuclear translocation. Interestingly, ribosome‐free RPL3 facilitates the recruitment of helicase DHX9 to
Xie H +22 more
europepmc +2 more sources

