The abundance change of age-regulated secreted proteins affects lifespan of C. elegans.

Proteome integrity is vital for survival and failure to maintain it results in uncontrolled protein abundances, misfolding and aggregation which cause proteotoxicity. In multicellular organisms, proteotoxic stress is communicated among tissues to maintain proteome integrity for organismal stress resistance and survival. However, the nature of these signalling molecules and their regulation in extracellular space is largely unknown.

Amplifying Flutamide Sensing through the Synergetic Combination of -Derived Carbon Particles and WS Platelets.

The development of electrochemical sensors for flutamide detection is a crucial step in biomedical research and environmental monitoring. In this study, a composite of -derived carbon particles (CPs) and tungsten disulfide (WS) was formed and used as an electrocatalyst for the electrochemical detection of flutamide. The CPs had an average diameter of 500 nm and contained surface hydroxyl and carbonyl groups.

Ultra-sensitive electrochemical detection of levofloxacin using a binder-free copper and graphene composite.

Given the levels of pollution in the aquatic environment and the development of antimicrobial resistance, it is essential to develop sensors, with sensitivity, selectivity, stability, and cost-effectiveness, for the determination of antibiotics. The present article highlights the fabrication of an ultra-sensitive graphene and copper sensor, Gr/Cu, supported on glassy carbon (GCE/Gr/Cu) for the electroanalysis of levofloxacin through a cost-effective electrodeposition method. The sequential electrodeposition of graphene and Cu was optimised to give GCE/Gr/Cu, with the Cu particles well dispersed on the graphene sheets.

Elucidation of Site-Specific Ubiquitination on Chaperones in Response to Mutant Huntingtin.

Huntington's disease (HD) is one of the prominent neurodegenerative diseases, characterized by the progressive decline of neuronal function, due to the accumulation and aggregation of misfolded proteins. Pathological progression of HD is hallmarked by the aberrant aggregation of the huntingtin protein (HTT) and subsequent neurotoxicity. Molecular chaperones (heat shock proteins, HSPs) play a pivotal role in maintaining proteostasis by facilitating protein refolding, degradation, or sequestration to limit the accumulation of misfolded proteins during neurotoxicity.

Mechanisms of readthrough mitigation reveal principles of GCN1-mediated translational quality control.

Readthrough into the 3' untranslated region (3' UTR) of the mRNA results in the production of aberrant proteins. Metazoans efficiently clear readthrough proteins, but the underlying mechanisms remain unknown. Here, we show in Caenorhabditis elegans and mammalian cells that readthrough proteins are targeted by a coupled, two-level quality control pathway involving the BAG6 chaperone complex and the ribosome-collision-sensing protein GCN1.