A solar steam generation method has been widely investigated as a sustainable method to achieve seawater desalination and sewage treatment. However, oil pollutants are usually emitted in real seawater or wastewaters, which can cause serious fouling problems to disturb the solar evaporation performance. In this work, a mussel-inspired, low-cost, polydopamine-filled cellulose aerogel (PDA-CA) has been rationally designed and fabricated with both superhydrophilicity and underwater superoleophobicity. The resulting PDA-CA device could also achieve a high solar evaporation rate of 1.36 kg m–1 h–1 with an 86% solar energy utilize efficiency under 1 sun illumination. In addition, the PDA-CA not only exhibited promising antifouling capacity for long-term water evaporation but also engaged in the effective adsorption of organic dye contaminants. These promising features of PDA-CA may offer new opportunities for developing multifunctional photothermal devices for solar-driven water remediation.

N-Glycosylation and GPI anchoring of proteins occur in the endoplasmic reticulum (ER). Liu et al. revealed N-glycans participate in quality control and temporal ER retention of GPI-anchored proteins (GPI-APs), ensuring their correct folding and GPI processing before exiting from the ER. Chronic ER stress induced exposure of unprocessed GPI-APs on the cell surface.

Graphene, with its properties of intrinsic flexibility, reliable electrical performance, and high chemical stability, is highly desirable as bioelectrodes for detecting electrophysiological signals. However, its mechanical properties limit its application to a great extentenergy dissipation mechanisms are not provided by the carbon network for external strain and it easily cracks. Herein, inspired by the very structure of the avian nest, we report a durable and nondisposable transparent graphene skin electrode for detecting electrophysiological signals, which was fabricated by semi-embedding highly graphitized electrospun fiber/monolayer graphene (GFG) into soft elastomer. Because of the semi-embedded structure and strong interaction between annealed electrospun fiber and graphene through graphitization, as-fabricated conductive film demonstrated high conductivity and transparency (∼150 Ω/□ at 83% transmittance), as well as a stable electrical performance under mechanical vibrations (strain, peel-off, stir, etc.). It can be used to reliably collect vital biometric signals, such as electrocardiogram (ECG), surface electromyogram (sEMG), and electroencephalogram (EEG). Furthermore, the semi-embedded GFG in the elastomer demonstrated excellent washability (rinsing/stirring in water) and repeatability (∼10 repeats) with high signal-to-noise ratio (up to 30 dB) while detecting sEMG. This is the first report of durable and transparent graphene skin electrode for biometric signals detection, revealing potential opportunities in wearable healthcare applications.

Over 100 kinds of proteins are expressed as glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) on the cell surface in mammalian cells. GPI-APs possess unique properties in terms of their intracellular trafficking and association with lipid rafts. Although it is clear that GPI-APs play critical roles in various biological phenomena, it is poorly understood how the GPI moiety contributes to these mechanisms. More than 30 genes are involved in the correct biosynthesis of GPI-APs. We here constructed a cell library in which 32 genes involved in GPI biosynthesis were knocked out in human embryonic kidney 293 cells. Using the cell library, the surface expression and sensitivity to phosphatidylinositol-specific phospholipase C of GPI-APs were analyzed. Furthermore, we identified structural motifs of GPIs that are recognized by a GPI-binding toxin, aerolysin. The cell-based GPI-knockout library could be applied not only to basic researches, but also to applications and methodologies related to GPI-APs.

Over 100 glycosylphosphatidylinositol‐anchored proteins (GPI‐APs) are encoded in the mammalian genome. It is not well understood how these proteins are targeted and translocated to the endoplasmic reticulum (ER). Here, we reveal that many GPI‐APs, such as CD59, CD55, and CD109, utilize human SND2 (hSND2)‐dependent ER targeting machinery. We also found that signal recognition particle receptors seem to cooperate with hSND2 to target GPI‐APs to the ER. Both the N‐terminal signal sequence and C‐terminal GPI attachment signal of GPI‐APs contribute to ER targeting via the hSND2‐dependent pathway. Particularly, the hydrophobicity of the C‐terminal GPI attachment signal acts as the determinant of hSND2 dependency. Our results explain the route and mechanism of the ER targeting of GPI‐APs in mammalian cells.