14 research outputs found

    From Choc En Retour To Nomadisme En Fleche

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    This thesis seeks to analyze and expound upon Aimé Césaire’s theory of history, choc en retour from Discours sur le colonialisme and situate William Faulkner’s Absalom! Absalom! and André Schwarz-Bart’s La Mulatresse Solitude (and to a lesser extent Le Dernier des Justes and Go Down, Moses) within this theoretical framework; which presents the Holocaust as the culmination (“retrun shock”) of four centuries of colonial violence – from the seventeenth to twentieth centuries – perpetrated by Western powers such as France and the United States. While Césaire’s application to Schwarz- Bart’s texts is more standard – with his two novels explicitly linking Antillean slavery to the Holocaust – the connections between American antebellum slavery, the Civil War and consequent decades of racially motivated discrimination and terror in the United States – as presented by Faulkner – have rarely been viewed through choc en retour. This stems from a dearth of research seeking to build upon Aimé Césaire’s historical connections, and link concentric histories of violence and exploitation to one another. Thus, this thesis takes a genealogical approach, which also employs Glissant’s theorization of nomadisme en flèche. This notion casts imperialism as a perpetually wanton extraction of goods and resources, in which bourgeois states constantly seek out new markets and labor pools in service of metropolitan prosperity; as they engage in increasingly amoral practices (i.e. slavery). Understanding choc en retour in tandem with nomadisme en flèche allows for linkages between seemingly divergent timelines. As a result, this thesis argues that Faulkner and Schwarz-Bart use their novels to show how both France and the United States’ domination of various peoples cast as “the Other” and perpetuation of violent exploitative processes through nomadisme en flèche carries the constant threat of “un veritable choc en retour” – leading to Antillean slave rebellions, the Civil, the Holocaust and today’s perpetually violent neoliberal world

    A Novel Conserved Isoform of the Ubiquitin Ligase UFD2a/UBE4B Is Expressed Exclusively in Mature Striated Muscle Cells

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    Yeast Ufd2p was the first identified E4 multiubiquitin chain assembly factor. Its vertebrate homologues later referred to as UFD2a, UBE4B or E4B were also shown to have E3 ubiquitin ligase activity. UFD2a function in the brain has been well established in vivo, and in vitro studies have shown that its activity is essential for proper condensation and segregation of chromosomes during mitosis. Here we show that 2 alternative splice forms of UFD2a, UFD2a-7 and -7/7a, are expressed sequentially during myoblast differentiation of C2C12 cell cultures and during cardiotoxin-induced regeneration of skeletal muscle in mice. UFD2a-7 contains an alternate exon 7, and UFD2a-7/7a, the larger of the 2 isoforms, contains an additional novel exon 7a. Analysis of protein or mRNA expression in mice and zebrafish revealed that a similar pattern of isoform switching occurs during developmental myogenesis of cardiac and skeletal muscle. In vertebrates (humans, rodents, zebrafish), UFD2a-7/7a is expressed only in mature striated muscle. This unique tissue specificity is further validated by the conserved presence of 2 muscle-specific splicing regulatory motifs located in the 3′ introns of exons 7 and 7a. UFD2a interacts with VCP/p97, an AAA-type ATPase implicated in processes whose functions appear to be regulated, in part, through their interaction with one or more of 15 previously identified cofactors. UFD2a-7/7a did not interact with VCP/p97 in yeast 2-hybrid experiments, which may allow the ATPase to bind cofactors that facilitate its muscle-specific functions. We conclude that the regulated expression of these UFD2a isoforms most likely imparts divergent functions that are important for myogenisis

    Superluminal to subluminal transition in the pulse propagation in a resonantly absorbing medium

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    The Iceland Palaeomagnetism Database (ICEPMAG)

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