Results 231 to 240 of about 226,212 (308)
Full androgen deprivation (FAD) induces paracrine cholesterol in prostate cancer that drives the polarization of cancer‐associated fibroblasts (CAFs) and subsequent elevated matrix stiffness. Matrix stiffness in turn potentiates tumor cell survival under FAD pressure via dual mechanotransductive activation of the IRE1α‐XBP1s stress‐response axis ...
Shaojie Liu +20 more
wiley +1 more source
Heterozygous pathogenic variants in the splicing factor SF1 lead to a large spectrum of neurodevelopmental disorders. [PDF]
Bou-Rouphael J +44 more
europepmc +1 more source
A pro‐inflammatory microglial subset persists after decompression in chronic compressive cervical spinal cord injury and shows enhanced Dnmt3a‐driven m5C signaling. By stabilizing RelA mRNA, this axis sustains NF‐κB activation and postoperative neuroinflammation.
Tianyu Qin +15 more
wiley +1 more source
Molecular basis of the autoregulatory mechanism of motor neuron-related splicing factor 30. [PDF]
Izumikawa K +11 more
europepmc +1 more source
In the pathological state of PD induced by MPP+, the upregulated PRMT9 in dopaminergic neurons translocates into mitochondrion and interacts with DUSP26 and catalyzes its arginine methylation, leading to the ubiquitin‐proteasomal degradation of DUSP26 mediated by Trim32.
Tengfei Liu +13 more
wiley +1 more source
Chromatin-bound U2AF2 splicing factor ensures exon inclusion. [PDF]
Wu W, Ahmad K, Henikoff S.
europepmc +1 more source
This study uncovers that quercetin naturally targets mitochondria. By coordinating quercetin with Fe3+, we engineer an ultrasmall cascade nanozyme (MCN) with superoxide dismutase‐catalase activities. MCN crosses the damaged blood–brain barrier, scavenges mitochondrial ROS, prevents mitochondrial DNA leakage, and blocks the cGAS‐STING pathway, thereby ...
Wenxuan Zheng +14 more
wiley +1 more source
RP9 revisited; RP9 p.(H137L) remains a likely cause of dominant splicing factor-Retinitis Pigmentosa. [PDF]
Chang L +8 more
europepmc +1 more source
TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Luca Zangrando +2 more
wiley +1 more source

