Results 81 to 90 of about 37,758 (275)
The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis
SUMOylation plays a crucial role in regulating diverse cellular processes including ribosome biogenesis. Proteomic analyses and experimental evidence showed that a number of nucleolar proteins involved in ribosome biogenesis are modified by SUMO. However,
Hyunju Ryu+12 more
semanticscholar +1 more source
These findings elucidate the innovative role of HIC1 as a transcriptional activator in GC, driving the initiation of pyroptosis and enhancing CD8+ T cell infiltration, which has certain novelty and creative significance. Collectively, targeting HIC1 can present an appealing immunotherapeutic strategy to improve outcomes in GC patients.
Mengjie Kang+4 more
wiley +1 more source
Posttranslational modifications, such as SUMOylation, play specific roles in the life cycle of invading pathogens. However, the effect of SUMOylation on the adaptation, pathogenesis, and transmission of influenza A virus (IAV) remains largely unknown ...
Junping Li+17 more
semanticscholar +1 more source
Post‐Translational Modifications in Cilia and Ciliopathies
This review synthesizes current understanding of post‐translational modifications (PTMs) in ciliary proteins and emphasizes their roles in ciliary formation, homeostasis, and signaling. This review also discusses the implication of PTM dysregulation in ciliopathies and explores therapeutic strategies targeting PTM‐modifying enzymes.
Jie Ran, Jun Zhou
wiley +1 more source
LRRC4 deficiency disrupts the metabolic homeostasis of mitochondrial aerobic respiration and glycolysis during GC differentiation by inhibiting the ubiquitination‐mediated degradation of YAP, which ultimately leads to POI. These findings reveal the novel molecular etiology of POI and provide a promising target for prevention and treatment.
Yujie Shang+5 more
wiley +1 more source
A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation. [PDF]
A variety of cellular pathways are regulated by protein modifications with ubiquitin-family proteins. SUMO, the Small Ubiquitin-like MOdifier, is covalently attached to lysine on target proteins via a cascade reaction catalyzed by E1, E2, and E3 enzymes.
Claudio P Albuquerque+5 more
doaj +1 more source
Ovarian cancer‐derived extracellular vesicles (EVs) transfer INAVA mRNA to normal ovarian fibroblasts (NOFs). Translated INAVA protein inhibits HMGA2 phosphorylation‐dependent ubiquitylation and proteasomal degradation, promoting NOF activation.
Lingkai Gu+12 more
wiley +1 more source
SUMOylation and deSUMOylation at a glance
Small ubiquitin-related modifiers (SUMOs) are ubiquitin-like polypeptides that become covalently conjugated to cellular proteins in a manner similar to ubiquitylation ([Johnson, 2004][1]).
Yonggang Wang, Mary Dasso
openaire +4 more sources
The role of SUMOylation during development
During the development of multicellular organisms, transcriptional regulation plays an important role in the control of cell growth, differentiation and morphogenesis. SUMOylation is a reversible post-translational process involved in transcriptional regulation through the modification of transcription factors and through chromatin remodelling (either ...
Orhi Barroso-Gomila+8 more
openaire +5 more sources
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