BiFC fluorescence colocalized with LAMP1, a lysosomal membrane protein (Fig. 5k), suggesting that α-synuclein multimers en route to secretion are localized in lysosomes. To further validate the lysosomal localization, we performed correlative light-electron microscopy (CLEM) and found that BiFC ...
Senescence-associated miRNAs enclosed in small extracellular vesicles; SASP: Senescence-associated secretory phenotype; SA-β-gal: Senescence-associated β-galactosidase; SIPS: stress induced premature senescence; SVD: singular value decomposition; TPM: tags per million; TSG10: tumour-susceptibility protein...
Further electrophoretic mobility shift assay (EMSA) and transient expression analysis clearly revealed that BrWRKY65 directly bound to the W-box motifs in the promoters of three senescence-associated genes (SAGs) such as BrNYC1 and BrSGR1 associated with chlorophyll degradation, and BrDIN1, and ...
These cDNA clones encode proteins similar to 尾 -glucosidase (EC 3.2.1.21, din2 ), asparagine synthetase (EC 6.3.5.4, din6 ), phosphomannose isomerase (EC 5.3.1.8, din9 ), seed imbibition protein ( din10) and 2-oxoacid-dependent dioxygenases ( din11 ). Accumulation of the transcripts ...
Cell-to-cell propagation of α-synuclein is thought to be the underlying mechanism of Parkinson’s disease progression. Recent evidence suggests that inflammation plays an important role in the propagation of protein aggregates. However, the mechanism by