An ultrathin solid polymer electrolyte (SPE) consisting of modified polyethylene (PE) as the host and poly(ethylene glycol) methyl ether acrylate and lithium salts as fillers is presented. The porous poly(methyl methacrylate)–polystyrene interface layers closely attached on both sides of the PE effectively improve the interface compatibility among electrolytes and electrodes. The resultant 10 μm‐thick SPEs possess an ultrahigh ionic conductance of 34.84 mS at room temperature and excellent mechanical properties of 103.0 MPa with elongation up to 142.3%. The Li//Li symmetric cell employing an optimized solid electrolyte can stably cycle more than 1500 h at 60 °C. Moreover, the LiFePO4//Li pouch cell can stably cycle over 1000 cycles at 1 C rate and with a capacity retention of 76.4% from 148.9 to 113.7 mAh g−1 at 60 °C. The LiCoO2//Li pouch cell can stably operate at 0.1 and 0.2 C rate for each 100 cycles. Furthermore, the LiFePO4//Li pouch cell can work stably after curling and folding, which proves its excellent flexibility and safety simultaneously. This work offers a promising strategy to realize ultrathinness, excellent compatibility, high strength, as well as safe solid electrolytes for all‐solid‐state lithium‐metal batteries.

E2F-1 plays a crucial role in the regulation of cell-cycle progression at the G1-S transition. In keeping with the fact that, when overproduced, it is both an oncoprotein and a potent inducer of apoptosis, its transcriptional activity is subject to multiple controls. Among them are binding by the retinoblastoma gene product (pRb), activation by cdk3, and S-phase-dependent down-regulation of DNA-binding capacity by cyclin A-dependent kinase. Here we report that E2F-1 is actively degraded by the ubiquitin-proteasome pathway. Efficient degradation depends on the availability of selected E2F-1 sequences. Unphosphorylated pRb stabilized E2F-1, protecting it from in vivo degradation, pRb-mediated stabilization was not an indirect consequence of Ga arrest, but rather depended on the ability of pRb to interact physically with E2F-1. Thus, in addition to binding E2F-1 and transforming it into a transcriptional repressor, pRb has another function, protection of E2F-1 from efficient degradation during a period when pRb/E2F complex formation is essential to regulating the cell cycle. In addition, there may be a specific mechanism for limiting free E2F-1 levels, failure of which could compromise cell survival and/or homeostasis.

Chloride ions are known to bind and alter the absorption spectra of some but not all visual pigments. In this report, the human red and green color vision pigments are shown to bind Cl- and to undergo a large red shift in their absorption maxima. Mutation of 18 different positively charged amino acids in these pigments identified two residues, His197 and Lys200, in the Cl(-)-binding site. His197 and Lys200 are strictly conserved in all long-wavelength cone pigments but are absent in all rhodopsins and short-wavelength cone pigments. This fact suggests that the evolutionary branch of the long-wavelength pigments was established when an ancestral pigment acquired the ability to bind Cl- and, as a result, shift the absorption maximum to longer wavelengths.