Browsing by Subject "Venus"
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Item Open Access Naked and Unashamed: A Study of the Aphrodite Anadyomene in the Greco-Roman World(2010) Wardle, Marianne EileenThis dissertation presents a study of the Aphrodite Anadyomene type in its cultural and physical contexts. Like many other naked Aphrodites, the Anadyomene was not posed to conceal the body, but with arms raised, naked and unashamed, exposing the goddess' body to the gaze. Depictions of the Aphrodite Anadyomene present the female body as an object to be desired. The Anadyomene offers none of the complicated games of peek-a-boo which pudica Venuses play by shielding their bodies from view. Instead, the goddess offers her body to the viewer's gaze and there is no doubt that we, as viewers, are meant to look, and that our looking should produce desire. As a type, the Anadyomene glorifies the process of the feminine toilette and adornment and as the goddess stands, naked and unashamed, she presents an achievable ideal for the female viewer.
The roots of the iconography of the Anaydyomene can be found in archaic Greek texts such as Hesiod's Theogony and Homeric Hymn from the eighth century B.C.E, as well as in paintings of women bathing on red figure vases from the fifth century B.C.E. The Anadyomene type provides a helpful case study to consider the ways that representations of Aphrodite were utilized. Consulting archaeological reports and detailed studies of display contexts make it possible to reconstruct and imagine the original settings for these kinds of works. The known findspots for representations of the Anadyomene can be grouped into four contexts: Graves, Sanctuaries, Baths and Fountains, and Houses. Small objects might have been seen, handled, and used daily that carried connotations and meanings which these ancient viewers would have brought to other more elite or public works.
Item Open Access Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent Proteins.(J Bacteriol, 2017-01-01) Moore, Desmond A; Whatley, Zakiya N; Joshi, Chandra P; Osawa, Masaki; Erickson, Harold PFtsZ, a bacterial tubulin homologue, is a cytoskeletal protein that assembles into protofilaments that are one subunit thick. These protofilaments assemble further to form a "Z ring" at the center of prokaryotic cells. The Z ring generates a constriction force on the inner membrane and also serves as a scaffold to recruit cell wall remodeling proteins for complete cell division in vivo One model of the Z ring proposes that protofilaments associate via lateral bonds to form ribbons; however, lateral bonds are still only hypothetical. To explore potential lateral bonding sites, we probed the surface of Escherichia coli FtsZ by inserting either small peptides or whole fluorescent proteins (FPs). Among the four lateral surfaces on FtsZ protofilaments, we obtained inserts on the front and back surfaces that were functional for cell division. We concluded that these faces are not sites of essential interactions. Inserts at two sites, G124 and R174, located on the left and right surfaces, completely blocked function, and these sites were identified as possible sites for essential lateral interactions. However, the insert at R174 did not interfere with association of protofilaments into sheets and bundles in vitro Another goal was to find a location within FtsZ that supported insertion of FP reporter proteins while allowing the FtsZ-FPs to function as the sole source of FtsZ. We discovered one internal site, G55-Q56, where several different FPs could be inserted without impairing function. These FtsZ-FPs may provide advances for imaging Z-ring structure by superresolution techniques. IMPORTANCE: One model for the Z-ring structure proposes that protofilaments are assembled into ribbons by lateral bonds between FtsZ subunits. Our study excluded the involvement of the front and back faces of the protofilament in essential interactions in vivo but pointed to two potential lateral bond sites, on the right and left sides. We also identified an FtsZ loop where various fluorescent proteins could be inserted without blocking function; these FtsZ-FPs functioned as the sole source of FtsZ. This advance provides improved tools for all fluorescence imaging of the Z ring and may be especially important for superresolution imaging.