The pragmatic-semiotic construction of male identities in contemporary advertising of male grooming products

[EN] This article aims to unveil how male identities are constructed in a corpus of male toiletry TV ads through a pragmatic and multimodal analysis of a set of implicit assumptions conveyed about the male participants in the ads. The validity of these assumptions is first empirically tested with a group of 10 male informants and then those implied meanings are bundled into thematic cores for their qualitative and quantitative description. Findings reveal that these ads still rely on stereotypical constructs and traditional discourses of what it takes to be a man. For example, men are invited to consume grooming products but reminded to do it the men's way. Men are also reminded of their sexual power to seduce and attract women with the aid of the product. Likewise, by portraying male ad personae in traditional manly activities while emphasizing their toughness and body strength, or their resourcefulness when faced with challenging situations, the ads portray a rather skewed view of contemporary men, which fails to take into account the myriad roles a modern man can play in contemporary societies.I am really grateful to the reviewers for their insightful comments and also to the editor of the journal.Saz Rubio, MMD. (2019). The pragmatic-semiotic construction of male identities in contemporary advertising of male grooming products. Discourse & Communication. 13(2):192-227. https://doi.org/10.1177/1750481318817621S192227132Alexander, S. M. (2003). Stylish Hard Bodies: Branded Masculinity in Men’s Health Magazine. Sociological Perspectives, 46(4), 535-554. doi:10.1525/sop.2003.46.4.535Attwood, F. (2005). ‘Tits and ass and porn and fighting’. International Journal of Cultural Studies, 8(1), 83-100. doi:10.1177/1367877905050165Rubio, M. D. 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Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions

Crystal structures reveal how distinct sites on the cysteine desulfurase IscS bind two different sulfur-acceptor proteins, IscU and TusA, to transfer sulfur atoms for iron-sulfur cluster biosynthesis and tRNA thiolation

New Structural and Functional Contexts of the Dx[DN]xDG Linear Motif: Insights into Evolution of Calcium-Binding Proteins

Binding of calcium ions (Ca2+) to proteins can have profound effects on their structure and function. Common roles of calcium binding include structure stabilization and regulation of activity. It is known that diverse families – EF-hands being one of at least twelve – use a Dx[DN]xDG linear motif to bind calcium in near-identical fashion. Here, four novel structural contexts for the motif are described. Existing experimental data for one of them, a thermophilic archaeal subtilisin, demonstrate for the first time a role for Dx[DN]xDG-bound calcium in protein folding. An integrin-like embedding of the motif in the blade of a β-propeller fold – here named the calcium blade – is discovered in structures of bacterial and fungal proteins. Furthermore, sensitive database searches suggest a common origin for the calcium blade in β-propeller structures of different sizes and a pan-kingdom distribution of these proteins. Factors favouring the multiple convergent evolution of the motif appear to include its general Asp-richness, the regular spacing of the Asp residues and the fact that change of Asp into Gly and vice versa can occur though a single nucleotide change. Among the known structural contexts for the Dx[DN]xDG motif, only the calcium blade and the EF-hand are currently found intracellularly in large numbers, perhaps because the higher extracellular concentration of Ca2+ allows for easier fixing of newly evolved motifs that have acquired useful functions. The analysis presented here will inform ongoing efforts toward prediction of similar calcium-binding motifs from sequence information alone

Genome-wide association mapping identifies a new arsenate reductase enzyme critical for limiting arsenic accumulation in plants

Inorganic arsenic is a carcinogen, and its ingestion through foods such as rice presents a significant risk to human health. Plants chemically reduce arsenate to arsenite. Using genome-wide association (GWA) mapping of loci controlling natural variation in arsenic accumulation in Arabidopsis thaliana allowed us to identify the arsenate reductase required for this reduction, which we named High Arsenic Content 1 (HAC1). Complementation verified the identity of HAC1, and expression in Escherichia coli lacking a functional arsenate reductase confirmed the arsenate reductase activity of HAC1. The HAC1 protein accumulates in the epidermis, the outer cell layer of the root, and also in the pericycle cells surrounding the central vascular tissue. Plants lacking HAC1 lose their ability to efflux arsenite from roots, leading to both increased transport of arsenic into the central vascular tissue and on into the shoot. HAC1 therefore functions to reduce arsenate to arsenite in the outer cell layer of the root, facilitating efflux of arsenic as arsenite back into the soil to limit both its accumulation in the root and transport to the shoot. Arsenate reduction by HAC1 in the pericycle may play a role in limiting arsenic loading into the xylem. Loss of HAC1-encoded arsenic reduction leads to a significant increase in arsenic accumulation in shoots, causing an increased sensitivity to arsenate toxicity. We also confirmed the previous observation that the ACR2 arsenate reductase in A. thaliana plays no detectable role in arsenic metabolism. Furthermore, ACR2 does not interact epistatically with HAC1, since arsenic metabolism in the acr2 hac1 double mutant is disrupted in an identical manner to that described for the hac1 single mutant. Our identification of HAC1 and its associated natural variation provides an important new resource for the development of low arsenic-containing food such as rice

Deinococcus geothermalis: The Pool of Extreme Radiation Resistance Genes Shrinks

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Robust image analysis with sparse representation on quantized visual features

10.1109/TIP.2012.2219543IEEE Transactions on Image Processing223860-871IIPR