Oxidation behavior of graphene-coated copper at intrinsic graphene defects of different origins

The development of ultrathin barrier films is vital to the advanced semiconductor industry. Graphene appears to hold promise as a protective coating; however, the polycrystalline and defective nature of engineered graphene hinders its practical applications. Here, we investigate the oxidation behavior of graphene-coated Cu foils at intrinsic graphene defects of different origins. Macro-scale information regarding the spatial distribution and oxidation resistance of various graphene defects is readily obtained using optical and electron microscopies after the hot-plate annealing. The controlled oxidation experiments reveal that the degree of structural deficiency is strongly dependent on the origins of the structural defects, the crystallographic orientations of the underlying Cu grains, the growth conditions of graphene, and the kinetics of the graphene growth. The obtained experimental and theoretical results show that oxygen radicals, decomposed from water molecules in ambient air, are effectively inverted at Stone-Wales defects into the graphene/Cu interface with the assistance of facilitators

C. elegans Agrin Is Expressed in Pharynx, IL1 Neurons and Distal Tip Cells and Does Not Genetically Interact with Genes Involved in Synaptogenesis or Muscle Function

Agrin is a basement membrane protein crucial for development and maintenance of the neuromuscular junction in vertebrates. The C. elegans genome harbors a putative agrin gene agr-1. We have cloned the corresponding cDNA to determine the primary structure of the protein and expressed its recombinant fragments to raise specific antibodies. The domain organization of AGR-1 is very similar to the vertebrate orthologues. C. elegans agrin contains a signal sequence for secretion, seven follistatin domains, three EGF-like repeats and two laminin G domains. AGR-1 loss of function mutants did not exhibit any overt phenotypes and did not acquire resistance to the acetylcholine receptor agonist levamisole. Furthermore, crossing them with various mutants for components of the dystrophin-glycoprotein complex with impaired muscle function did not lead to an aggravation of the phenotypes. Promoter-GFP translational fusion as well as immunostaining of worms revealed expression of agrin in buccal epithelium and the protein deposition in the basal lamina of the pharynx. Furthermore, dorsal and ventral IL1 head neurons and distal tip cells of the gonad arms are sources of agrin production, but no expression was detectable in body muscles or in the motoneurons innervating them. Recombinant worm AGR-1 fragment is able to cluster vertebrate dystroglycan in cultured cells, implying a conservation of this interaction, but since neither of these proteins is expressed in muscle of C. elegans, this interaction may be required in different tissues. The connections between muscle cells and the basement membrane, as well as neuromuscular junctions, are structurally distinct between vertebrates and nematodes