Results 151 to 160 of about 125,351 (338)
This study reveals that the E3 ubiquitin ligase TRIM56 exacerbates neuronal ferroptosis and brain damage by mediating K48‐linked ubiquitination and degradation of KLF4, leading to suppression of the xCT/GSH/GPX4 axis. Targeting TRIM56 alleviates cerebral ischemia‐reperfusion injury in vivo and in vitro, highlighting its therapeutic potential.
Qiangping Wang +15 more
wiley +1 more source
Longitudinal RNA-Seq analysis of acute and chronic neurogenic skeletal muscle atrophy. [PDF]
Skeletal muscle is a highly adaptable tissue capable of changes in size, contractility, and metabolism according to functional demands. Atrophy is a decline in mass and strength caused by pathologic loss of myofibrillar proteins, and can result from ...
Coppola, Giovanni +4 more
core
Phosphorylation of Optineurin by TBK1 induces the formation of filaments that condensate upon binding to linear polyubiquitin. Membrane‐anchored LC3 partitions into these condensates, suggesting that phase separation of filamentous Optineurin with ubiquitylated cargo promotes the sequestration of cargo and its subsequent alignment with LC3‐positive ...
Maria G. Herrera +10 more
wiley +1 more source
MARCH family E3 ubiquitin ligases selectively target and degrade cadherin family proteins.
Cadherin family proteins play a central role in epithelial and endothelial cell-cell adhesion. The dynamic regulation of cell adhesion is achieved in part through endocytic membrane trafficking pathways that modulate cadherin cell surface levels.
Tadahiko Seo +6 more
doaj +1 more source
Two Novel S‐methyltransferases Confer Dimethylsulfide Production in Actinomycetota
This study identifies two novel S‐adenosine‐methionine‐dependent methyltransferases, MddM1 and MddM2, in actinomycetes from the Mariana Trench. These enzymes can convert toxic hydrogen sulfide (H2S) and methanethiol (MeSH) into dimethylsulfide (DMS), serving as a cellular detoxification and oxidative stress response.
Ruihong Guo +11 more
wiley +1 more source
Lactylation‐Driven YTHDC1 Alleviates MASLD by Suppressing PTPN22‐Mediated Dephosphorylation of NLRP3
In MASLD, YTHDC1 undergoes increased lactylation and ubiquitination, reducing its expression. AARS1 mediates lactylation at lysine 565, while disrupted binding to LDHA further promotes lactylation, suppressing YTHDC1. This downregulation enhances PTPN22 mRNA stability, leading to NLRP3 dephosphorylation and activation, which exacerbates inflammation ...
Feng Zhang +16 more
wiley +1 more source
RNF144A, an E3 ubiquitin ligase for DNA-PKcs, promotes apoptosis during DNA damage [PDF]
Shiuh‐Rong Ho +3 more
openalex +1 more source

