18 research outputs found

    Shone-Anomalie: Fallbericht und Hintergrund

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    Zusammenfassung: Die Shone-Anomalie wurde 1963 erstmals beschrieben und stellt eine seltene kongenitale kardiovaskulĂ€re Missbildung mit verschiedenen linkskardialen stenotischen LĂ€sionen dar. Die klassische Form besteht aus einem fibrösen supravalvulĂ€ren Mitralring, einer fallschirmartigen Deformation der Mitralklappe mit nur einem Papillarmuskel ("parachute mitral valve"), einer subvalvulĂ€ren Aortenstenose und einer Aortenisthmusstenose. Es gibt nur vereinzelte perioperative Fallberichte von erwachsenen Patienten mit dieser kardiovaskulĂ€ren Missbildung. Allerdings können Patienten mit einer undiagnostizierten, inkompletten Form der Shone-Anomalie auch im Erwachsenenalter fĂŒr nichtherzchirurgische Operationen vorgesehen sein. In dem vorliegenden Fallbericht wird das anĂ€sthesiologische Management einer Patientin, die fĂŒr eine abdominale Hysterektomie vorgesehen war und an einer bisher nichtdiagnostizierten Shone-Anomalie litt, beschriebe

    Limits to sustained energy intake XXIV : impact of suckling behaviour on the body temperatures of lactating female mice

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    We would like to thank the animal house staff and all members of the Energetics group for their invaluable help at various stages throughout the project. This work was supported by Natural Environment Research Council grant (NERC, NE/C004159/1). YG was supported by a scholarship from the rotary foundation. LV was supported by a Rubicon grant from the Netherlands Scientific Organisation (NWO).Peer reviewedPublisher PD

    Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex

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    Nuclear pore complexes (NPCs) are ∌100 MDa transport channels assembled from multiple copies of ∌30 nucleoporins (Nups). One-third of these Nups contain phenylalanine-glycine (FG)-rich repeats, forming a diffusion barrier, which is selectively permeable for nuclear transport receptors that interact with these repeats. Here, we identify an additional function of FG repeats in the structure and biogenesis of the yeast NPC. We demonstrate that GLFG-containing FG repeats directly bind to multiple scaffold Nups in vitro and act as NPC-targeting determinants in vivo. Furthermore, we show that the GLFG repeats of Nup116 function in a redundant manner with Nup188, a nonessential scaffold Nup, to stabilize critical interactions within the NPC scaffold needed for late steps of NPC assembly. Our results reveal a previously unanticipated structural role for natively unfolded GLFG repeats as Velcro to link NPC subcomplexes and thus add a new layer of connections to current models of the NPC architecture. In addition to forming the permeability barrier, FG repeats in nucleoporins contribute structurally to nuclear pore biogenesis and function. Keywords: Nuclear pore complex; Nuclear pore biogenesis; Nuclear pore structure; Intrinsically disordered domains; FG repeats; Nuclear envelope; Protein interactionsNational Institutes of Health (U.S.) (Grant R01GM077537
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