Cerium oxide nanoparticles decorated on graphene oxide nanosheets as battery-type cathode material for supercapacitors.

Designing advanced materials that effectively mitigate the poor cycle life of battery-type electrodes with high specific capacities is crucial for next-generation energy storage systems. Herein, graphene oxide-ceria (GO-CeO) nanocomposite synthesized via a facile wet chemical route is explored as cathode for high-performance supercapacitors. The morphological analysis suggests fine ceria (CeO) nanoparticles dispersed over ultrathin graphene oxide (GO) sheets while structural studies reveal face-centered cubic phase of CeO in the nanocomposite.

PSMC2 promotes resistance against temozolomide in glioblastoma via suppressing JNK-mediated autophagic cell death.

Temozolomide is universally used to treat glioblastoma due to its unique ability to cross the blood-brain barrier and inhibit tumor growth through DNA alkylation. However, over time, the inevitable emergence of resistance to temozolomide impedes successful treatment of this cancer. As a result, there is an urgent need to identify new therapeutic targets to improve treatment outcomes for this malignancy.

A Cd-based crystalline network material: catalytic properties and post-synthetic metal-ion metathesis with enhanced stability and gas sorption behaviour.

This study presents the synthesis of a Cd(II) based hydrophobic three dimensional crystalline network material (CNM), [Cd(L)(LH)(bpe)], {L = {4,4'-(hexafluroisopropylidine)bis(benzoate)} and 1,2-di(4-pyridyl) ethylene (bpe)}, 1(Cd), by employing the slow-diffusion method. The three-dimensional structure of 1(Cd) was determined by single crystal X-ray diffraction and characterized by powder X-ray diffraction (PXRD), FT-IR spectroscopy and thermogravimetric analysis (TGA). Subsequently, post-synthetic modification of 1(Cd) with Cu(II) at room temperature led to the formation of isostructural 1(Cu) with partial substitution.

Structure of E6AP in complex with HPV16-E6 and p53 reveals a novel ordered domain important for E3 ligase activation.

High-risk human papillomavirus E6 oncoprotein is a model system for the recognition and degradation of cellular p53 tumor suppressor protein. There remains a gap in the understanding of the ubiquitin transfer reaction, including placement of the E6AP catalytic HECT domain of the ligase concerning the p53 substrate and how E6 itself is protected from ubiquitination. We determined the cryoelectron microscopy (cryo-EM) structure of the E6AP/E6/p53 complex, related the structure to in vivo modeling of the tri-molecular complex, and identified structural interactions associated with activation of the ubiquitin ligase function.