Results 101 to 110 of about 37,758 (275)

Ligand binding reduces SUMOylation of the peroxisome proliferator-activated receptor γ (PPARγ) activation function 1 (AF1) domain. [PDF]

open access: yesPLoS ONE, 2013
Peroxisome proliferator-activated receptor gamma (PPARγ) is a ligand-activated nuclear receptor regulating adipogenesis, glucose homeostasis and inflammatory responses.
Rolf Diezko, Guntram Suske
doaj   +1 more source

BLM Sumoylation Is Required for Replication Stability and Normal Fork Velocity During DNA Replication

open access: yesFrontiers in Molecular Biosciences, 2022
BLM is sumoylated in response to replication stress. We have studied the role of BLM sumoylation in physiologically normal and replication-stressed conditions by expressing in BLM-deficient cells a BLM with SUMO acceptor-site mutations, which we refer to
Christelle de Renty   +4 more
doaj   +1 more source

The post-translational modification, SUMOylation, and cancer (Review)

open access: yesInternational Journal of Oncology, 2018
SUMOylation is a reversible post-translational modification which has emerged as a crucial molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune responses, carcinogenesis, cell cycle progression and apoptosis.
Zhi-Jian Han   +4 more
semanticscholar   +1 more source

Activation of Kir4.1 Channels by 2‐D08 Promotes Myelin Repair in Multiple Sclerosis

open access: yesAdvanced Science, EarlyView.
Multiple sclerosis causes myelin loss and neurological dysfunction. This study shows that 2‐D08, a small molecule targeting Kir4.1 channels, promotes OPCs differentiation via FYN tyrosine kinase phosphorylation and the FYN/MYRF pathway. It significantly improves myelin repair and motor deficits in EAE mice and marmosets, highlighting its potential as a
Mingdong Liu   +17 more
wiley   +1 more source

Mycobacteria modulate SUMOylation to suppresses protective responses in dendritic cells.

open access: yesPLoS ONE, 2023
Post translational modifications (PTMs) are exploited by various pathogens in order to escape host immune responses. SUMOylation is one of the PTMs which is involved in regulation of a variety of cellular responses.
Vandana Anang   +7 more
doaj   +1 more source

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

open access: yesFrontiers in Neurology, 2021
Post-translational modifications (PTMs) on tau have long been recognized as affecting protein function and contributing to neurodegeneration. The explosion of information on potential and observed PTMs on tau provides an opportunity to better understand ...
Carolina Alquezar   +2 more
doaj   +1 more source

SUMOylation is a Translatable Target in Hypoxic MNPs Regulating Retinal Vasculopathy

open access: yesAdvanced Science, EarlyView.
During ischemic retinopathy/retinal vasculopathy, UBC9‐mediated SUMOylation in retinal macrophages enhances their pro‐angiogenic capacity via hypoxia‐induced SUMOylation of FUS at K327/K502. This modification suppresses FUS binding to the Vegfa mRNA 3’UTR, stabilizing transcripts and facilitating VEGFA production. Targeting UBC9 inhibition can serve as
Zheng Zhong   +9 more
wiley   +1 more source

Rhes, a Physiologic Regulator of Sumoylation, Enhances Cross-sumoylation between the Basic Sumoylation Enzymes E1 and Ubc9 [PDF]

open access: yesJournal of Biological Chemistry, 2010
We recently reported that the small G-protein Rhes has the properties of a SUMO-E3 ligase and mediates mutant huntingtin (mHtt) cytotoxicity. We now demonstrate that Rhes is a physiologic regulator of sumoylation, which is markedly reduced in the corpus striatum of Rhes-deleted mice.
SUBRAMANIAM SIRINIVASA   +5 more
openaire   +4 more sources

MdDSK2a‐Like‐MdMTA Module Functions in Apple Cold Response via Regulating ROS Detoxification and Cell Wall Deposition

open access: yesAdvanced Science, EarlyView.
Under cold stress, MdDSK2a‐like is degraded via the 26S proteasome pathway, thereby alleviating the degradation of MdMTA induced by the 26S proteasome and autophagy pathways mediated by MdDSK2a‐like. The accumulated MdMTA increases the m6A levels of cold‐responsive genes, thereby contributing to increased ROS detoxification, deposition of cell wall, as
Nan Hou   +18 more
wiley   +1 more source

Tumor Small Extracellular Vesicle‐Transmitted LncRNA CATED Promotes Platinum‐Resistance in High‐Grade Serous Ovarian Cancer

open access: yesAdvanced Science, EarlyView.
Overcoming platinum resistance in high‐grade serous ovarian cancer (HGSOC) is critical for improving outcomes. This study identifies lncRNA CATED, elevated in platinum‐resistant small extracellular vesicles (sEVs) and tumors, which drives cisplatin resistance by enhancing DHX36 SUMOylation, boosting RAP1A translation, and activating MAPK signaling ...
Yi Liu   +7 more
wiley   +1 more source

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