963 resultados para Railroad worms
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Cover title.
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1910-1922 have title: General Manager's Report
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Mode of access: Internet.
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Mode of access: Internet.
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Mode of access: Internet.
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Title Varies: Investigation In the Matter of Making Accident Investigation Reports; Report In the Matter of Making Accident Investigation Reports
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-May 1900 Have Title: Proceedings
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von Adolph Becker
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D-Zug dritter Klasse, the second novel Irmgard Keun published in exile from Nazi Germany, describes seven passengers on a Berlin-Paris express in 1937. Although it begins like a wide-ranging narrative of persecution and emigration, many of the passengers' stories develop in non-political, inconsequential, and downright farcical directions, a shift which scholars have struggled to explain. This article suggests that D-Zug is a novel of emigration in a personal and literary sense, interpreting the narrative's erratic trajectory as a conscious expression of Keun's fear that her continuing exile could stifle her political effectiveness and professional abilities as an antifascist author.
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While our understanding of lipid microdomains has advanced in recent years, many aspects of their formation and dynamics are still unclear. In particular, the molecular determinants that facilitate the partitioning of integral membrane proteins into lipid raft domains are yet to be clarified. This review focuses on a family of raft-associated integral membrane proteins, termed flotillins, which belongs to a larger class of integral membrane proteins that carry an evolutionarily conserved domain called the prohibitin homology (PHB) domain. A number of studies now suggest that eucaryotic proteins carrying this domain have affinity for lipid raft domains. The PHB domain is carried by a diverse array of proteins including stomatin, podocin, the archetypal PHB protein, prohibitin, lower eucaryotic proteins such as the Dictyostelium discoideum proteins vacuolin A and vacuolin B and the Caenorhabditis elegans proteins unc-1, unc-24 and mec-2. The presence of this domain in some procaryotic proteins suggests that the PHB domain may constitute a primordial lipid recognition motif. Recent work has provided new insights into the trafficking and targeting of flotillin and other PHB domain proteins. While the function of this large family of proteins remains unclear, studies of the C. elegans PHB proteins suggest possible links to a class of volatile anaesthetics raising the possibility that these lipophilic agents could influence lipid raft domains. This review will discuss recent insights into the cell biology of flotillins and the large family of evolutionarily conserved PHB domain proteins.