209 research outputs found

    Misty, Spellbound and the lost Gothic of British girls’ comics.

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    This article is a case study of the 1970s British girls’ comics Spellbound (DC Thomson, 1976–1977) and Misty (IPC, 1978–1980). These mystery anthology comics followed the more famous American horror comics from publishers like EC Comics - but were aimed at pre-teen girls. The article situates these comics with respect to Gothic critical theory and within the wider landscape of British girls’ comics. Firstly, it closely considers and compares the structure and content of their stories with respect to theories of the terror and horror Gothic. It discovers that both comics offer similar fare, with a subversive streak that undercuts established horror archetypes. The article then looks closely at both titles’ aesthetics and their use of the page to draw comparisons. It uses comics theory and Gothic cinematic theory to demonstrate that the appearance of Misty is more strongly Gothic than the aesthetic of Spellbound. Finally, it considers a selection of stories from both comics and analyses their common themes using Gothic critical theory. It argues that both comics rework Gothic themes into new forms that are relevant to their pre-teen and teenage readers. It concludes by summarising the study’s findings and suggesting that these comics offer a “Gothic for Girls” that is part cautionary tale and part bildungsroman. This article is published as part of a collection on Gothic and horror

    Direct Visualization of Laser-Driven Electron Multiple Scattering and Tunneling Distance in Strong-Field Ionization

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    Using a simple model of strong-field ionization of atoms that generalizes the well-known 3-step model from 1D to 3D, we show that the experimental photoelectron angular distributions resulting from laser ionization of xenon and argon display prominent structures that correspond to electrons that pass by their parent ion more than once before strongly scattering. The shape of these structures can be associated with the specific number of times the electron is driven past its parent ion in the laser field before scattering. Furthermore, a careful analysis of the cutoff energy of the structures allows us to experimentally measure the distance between the electron and ion at the moment of tunnel ionization. This work provides new physical insight into how atoms ionize in strong laser fields and has implications for further efforts to extract atomic and molecular dynamics from strong-field physics

    Organ donation, ethnicity and the negotiation of death: ethnographic insights from the UK

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    The introduction of end-of-life care criteria in the UK aims at standardising the processes of care at the end of life, including how medical decisions on death are communicated to the families of dying and (brain) dead patients. In the setting of the intensive care unit, these activities are routinely complicated by the imperative to secure donor organs for transplantation: where recent changes to donation services have seen the accommodation of organ donation procedures into end-of-life care routines. This has ramifications for understanding how medical decisions around death and dying are brokered with the families of potential organ donors. Drawing on an ethnographic study in England, this paper will document how communications around death get turned into a particular matter of concern for the practice of requesting organ donation from minority ethnic families. It shows how attempts to resolve differences of opinion between health professionals and families about a diagnosis of brain stem death or dying are mediated by sets of brokering practices: specifically, those termed technological, authoritative and religious brokering. These practices, we argue, not only facilitate a family’s acceptance of their relative’s death, but also serve to make possible a decision on organ donation

    Direct Evidence for Packaging Signal-Mediated Assembly of Bacteriophage MS2

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    Using cross-linking coupled to matrix-assisted laser desorption/ionization mass spectrometry and CLIP-Seq sequencing, we determined the peptide and oligonucleotide sequences at the interfaces between the capsid proteins and the genomic RNA of bacteriophage MS2. The results suggest that the same coat protein (CP)-RNA and maturation protein (MP)-RNA interfaces are used in every viral particle. The portions of the viral RNA in contact with CP subunits span the genome, consistent with a large number of discrete and similar contacts within each particle. Many of these sites match previous predictions of the locations of multiple, dispersed and degenerate RNA sites with cognate CP affinity termed packaging signals (PSs). Chemical RNA footprinting was used to compare the secondary structures of protein-free genomic fragments and the RNA in the virion. Some PSs are partially present in protein-free RNA but others would need to refold from their dominant solution conformations to form the contacts identified in the virion. The RNA-binding peptides within the MP map to two sections of the N-terminal half of the protein. Comparison of MP sequences from related phages suggests a similar arrangement of RNA-binding sites, although these N-terminal regions have only limited sequence conservation. In contrast, the sequences of the C-termini are highly conserved, consistent with them encompassing pilin-binding domains required for initial contact with host cells. These results provide independent and unambiguous support for the assembly of MS2 virions via a PS-mediated mechanism involving a series of induced-fit viral protein interactions with RNA

    Insights into Minor Group Rhinovirus Uncoating: The X-ray Structure of the HRV2 Empty Capsid

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    Upon attachment to their respective receptor, human rhinoviruses (HRVs) are internalized into the host cell via different pathways but undergo similar structural changes. This ultimately results in the delivery of the viral RNA into the cytoplasm for replication. To improve our understanding of the conformational modifications associated with the release of the viral genome, we have determined the X-ray structure at 3.0 Å resolution of the end-stage of HRV2 uncoating, the empty capsid. The structure shows important conformational changes in the capsid protomer. In particular, a hinge movement around the hydrophobic pocket of VP1 allows a coordinated shift of VP2 and VP3. This overall displacement forces a reorganization of the inter-protomer interfaces, resulting in a particle expansion and in the opening of new channels in the capsid core. These new breaches in the capsid, opening one at the base of the canyon and the second at the particle two-fold axes, might act as gates for the externalization of the VP1 N-terminus and the extrusion of the viral RNA, respectively. The structural comparison between native and empty HRV2 particles unveils a number of pH-sensitive amino acid residues, conserved in rhinoviruses, which participate in the structural rearrangements involved in the uncoating process

    The Enterovirus 71 A-particle Forms a Gateway to Allow Genome Release: A CryoEM Study of Picornavirus Uncoating

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    Since its discovery in 1969, enterovirus 71 (EV71) has emerged as a serious worldwide health threat. This human pathogen of the picornavirus family causes hand, foot, and mouth disease, and also has the capacity to invade the central nervous system to cause severe disease and death. Upon binding to a host receptor on the cell surface, the virus begins a two-step uncoating process, first forming an expanded, altered "A-particle", which is primed for genome release. In a second step after endocytosis, an unknown trigger leads to RNA expulsion, generating an intact, empty capsid. Cryo-electron microscopy reconstructions of these two capsid states provide insight into the mechanics of genome release. The EV71 A-particle capsid interacts with the genome near the icosahedral two-fold axis of symmetry, which opens to the external environment via a channel ~10 Å in diameter that is lined with patches of negatively charged residues. After the EV71 genome has been released, the two-fold channel shrinks, though the overall capsid dimensions are conserved. These structural characteristics identify the two-fold channel as the site where a gateway forms and regulates the process of genome release. © 2013 Shingler et al
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