Enhanced Stabilities and Production Yields of MAPbBr Quantum Dots and Their Applications as Stretchable and Self-Healable Color Filters.

Organic-inorganic hybrid CHNHPbBr (MAPbBr) perovskite quantum dots (PQDs) are considered as promising and cost-effective building blocks for various optoelectronic devices. However, during centrifugation for the purification of these PQDs, commonly used polar protic and aprotic non-solvents (e.g.

Conformational Dynamics and Functional Implications of Phosphorylated β-Arrestins.

Arrestins desensitize and/or internalize G-protein-coupled receptors by interacting with phosphorylated receptors. A few studies have reported that arrestins themselves can be phosphorylated, and the phosphorylation status modulates their cellular functions. However, the effects of phosphorylation on arrestin structure have not been studied.

Efficient Debundling of Few-Walled Carbon Nanotubes by Wrapping with Donor-Acceptor Polymers for Improving Thermoelectric Properties.

Organic thermoelectric (TE) materials have great potential as sustainable energy sources for powering flexible and wearable electronic devices via harvesting of human body heat. Recent advances in soluble conjugated polymer/carbon nanotube (CNT) composites have facilitated achievement of high TE power factors. However, the effects of conjugated polymers on the debundling and electrical percolation of CNTs and on the TE properties of their composites are not yet fully understood.

Role of Helix 8 in Dopamine Receptor Signaling.

G protein-coupled receptors (GPCRs) are membrane receptors whose agonist-induced dynamic conformational changes trigger heterotrimeric G protein activation, followed by GRK-mediated phosphorylation and arrestin-mediated desensitization. Cytosolic regions of GPCRs have been studied extensively because they are direct contact sites with G proteins, GRKs, and arrestins. Among various cytosolic regions, the role of helix 8 is least understood, although a few studies have suggested that it is involved in G protein activation, receptor localization, and/or internalization.

Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase.

DOT1L is a histone H3 Lys79 methyltransferase whose activity is stimulated by histone H2B Lys120 ubiquitination, suggesting cross-talk between histone H3 methylation and H2B ubiquitination. Here, we present cryo-EM structures of DOT1L complexes with unmodified or H2B ubiquitinated nucleosomes, showing that DOT1L recognizes H2B ubiquitin and the H2A/H2B acidic patch through a C-terminal hydrophobic helix and an arginine anchor in DOT1L, respectively. Furthermore, the structures combined with single-molecule FRET experiments show that H2B ubiquitination enhances a noncatalytic function of the DOT1L-destabilizing nucleosome.