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  • 1
    Book
    Book
    2017
    ISBN: 1474297692  ISBN: 9781474297691 
    Language: English
    Description: The philosophy of Ayn Rand has had a role equal or greater than that of Milton Friedman or F.A. Hayek in shaping the contemporary neo-liberal consensus. Its impact was powerful on architects of Reaganomics such as Alan Greenspan, former Director of the World Bank, and the new breed of American industrialists who developed revolutionary information technologies in Silicon Valley. But what do we really know of Rand's philosophy? Is her gospel of selfishness really nothing more than a reiteration of a quintessentially American "rugged individualism?? This book argues that Rand's philosophy can in fact be traced back to a moment, before World War I, when the work of a now-forgotten German philosopher called Max Stirner possessed an extraordinary appeal for writers and artists across Europe. The influence of Stirnerian Egoism upon that phase of intense creative innovation we now call Modernism was seminal.The implications for our understanding of Modernism are profound - so too for our grasp of the "cultural logic of late capitalism?. This book presents the reader with a fresh perspective on the Modernist classics, as well as introducing less familiar art and writing that is only now beginning to attract interest in the West. It arrives at a fresh and compelling re-evaluation of Modernism: revealing its selfish streak.
    Subject(s): Autarchy ; Miscellanea ; Objectivism (Philosophy) ; Philosophy ; Selfishness
    ISBN: 1474297692
    ISBN: 9781474297691
    Source: Bloomsbury Collections: All Titles
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  • 2
    Book
    Book
    2013
    ISBN: 9781846318016  ISBN: 9781846318597  ISBN: 1846318599  ISBN: 9781781387085  ISBN: 1846318017  ISBN: 1781387087 
    Language: English
    Description: In London Underground: A Cultural Geography, David Ashford sets out to chart one of the strangest, as well as the most familiar, spaces in London. This book provides a theoretical account of the evolution of an archetypal modern environment. The first to complete that slow process of estrangement from the natural topography initiated by the Industrial Revolution, the London Underground is shown to be what French anthropologist Marc Augé has termed non-lieu - a non-place, like motorway, supermarket or airport lounge, compelled to interpret its relationship to the invisible landscape it traverses through the medium of signs and maps. Surveying an unusually wide variety of material, ranging from the Victorian triple-decker novel, to Modernist art and architecture, to Pop music and graffiti, this cultural geography suggests that the tube-network is a transitional form, linking the alienated spaces of Victorian England to the virtual spaces of our contemporary consumer-capitalism. Recounting the history of the production of this new space, and of the struggles it has generated, London Underground is nothing less than the story of how people have attempted to make a home in the psychopathological spaces of the modern world.
    Subject(s): Civilization ; Cultural geography ; England ; English, Irish, Scottish, Welsh ; European ; History ; Language & Literature ; Literary Criticism ; London ; London (England) ; London Underground Limited ; Subways
    ISBN: 9781846318016
    ISBN: 9781846318597
    ISBN: 1846318599
    ISBN: 9781781387085
    ISBN: 1846318017
    ISBN: 1781387087
    Source: Ebook Central - Academic Complete
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  • 3
    Article
    Article
    2014
    ISSN: 1071-6068  ISSN: 1080-6601 
    Language: English
    In: Modernism/modernity (Baltimore, Md.), 2014-11, Vol.21 (4), p.977-995
    Subject(s): 1800-1899 ; 1806-1856 ; 1900-1999 ; American literature ; Analysis ; Authors ; Ayn Rand ; capitalism ; Criticism and interpretation ; Der Einzige und sein Eigentum ; Egoism ; Egoism/Egotism ; Egotism ; English Literature ; German literature ; Influence ; Literature ; Max Stirner ; Modernism ; novel ; Novelists ; Objectivism ; Philosophy ; prose ; Rand, Ayn ; Russian American writers ; Stirner, Max ; the individual ; Twentieth Century
    ISSN: 1071-6068
    ISSN: 1080-6601
    E-ISSN: 1080-6601
    Source: Project MUSE - Premium Collection
    Source: MLA International Bibliography with Full Text
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  • 4
    Language: English
    In: Science (American Association for the Advancement of Science), 2015-07-17, Vol.349 (6245), p.309-312
    Description: Morphinan alkaloids from the opium poppy are used for pain relief. The direction of metabolites to morphinan biosynthesis requires isomerization of (S)- to (R)-reticuline. Characterization of high-reticuline poppy mutants revealed a genetic locus, designated STORR [(S)- to (R)-reticuline] that encodes both cytochrome P450 and oxidoreductase modules, the latter belonging to the aldo-keto reductase family. Metabolite analysis of mutant alleles and heterologous expression demonstrate that the P450 module is responsible for the conversion of (S)-reticuline to 1,2-dehydroreticuline, whereas the oxidoreductase module converts 1,2-dehydroreticuline to (R)-reticuline rather than functioning as a P450 redox partner. Proteomic analysis confirmed that these two modules are contained on a single polypeptide in vivo. This modular assembly implies a selection pressure favoring substrate channeling. The fusion protein STORR may enable microbial-based morphinan production.
    Subject(s): REPORTS
    ISSN: 0036-8075
    E-ISSN: 1095-9203
    Source: JSTOR Life Sciences
    Source: Single Journals
    Source: Academic Search Ultimate
    Source: Alma/SFX Local Collection
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  • 5
    Language: English
    In: The New phytologist, 2012-08-01, Vol.195 (3), p.585-595
    Description: The genome includes seven family 34 glycosyltransferase (GT34) encoding genes and have previously been shown to encode XyG α-1,6-xylosyltransferases, while knockout mutants of a third, , exhibit decreased XyG content, suggesting a similar activity. Here, we extend the study to the rest of the Arabidopsis GT34 genes in terms of biochemical activity and their roles in XyG biosynthesis. The enzyme activity of XXTs was investigated using recombinant protein expressed in . XyG analysis of single and double T-DNA insertion knockouts, together with over-expression of GT34s in selected mutant lines, provided detailed function of each gene. We reveal the activity of the third member of the GT34 gene family (XXT4) that exhibits xylosyltransferase activity. Double mutants for either or had a large impact on XyG content, structure and size distribution. Overexpression of the remaining member, , was able to restore XyG epitopes in and double knockouts, suggesting that it also encodes a protein with XXT activity. Our work demonstrates that five of the seven GT34 genes encode XXT enzymes.
    Subject(s): Antibodies ; Arabidopsis ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Biosynthesis ; Cell Wall - metabolism ; cell wall biosynthesis ; Cell walls ; Chromatography, Gel ; Embryos ; Enzyme Activation ; Enzymes ; Epitopes - metabolism ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Full papers ; galactomannan ; Gene Expression Regulation, Enzymologic ; Gene Expression Regulation, Plant ; Genes, Plant ; Genetic Complementation Test ; Glucans - metabolism ; glycosyltransferase ; Immunohistochemistry ; Multigene Family ; Oligosaccharides ; Pentosyltransferases - genetics ; Pentosyltransferases - metabolism ; plant cell walls ; Plant cells ; Plants ; Proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Reverse transcriptase polymerase chain reaction ; Xylans - metabolism ; xyloglucan
    ISSN: 0028-646X
    E-ISSN: 1469-8137
    Source: JSTOR Life Sciences
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
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  • 6
    Language: English
    In: FEMS microbiology letters, 2015-08-01, Vol.362 (16)
    Description: The production of malodour by humans is mediated by bacterial transformation of naturally secreted, non-odorous molecules. Specifically in the underarm (axilla), malodour arises due to biotransformation by the microbiota of dipeptide-conjugated thioalcohols, particularly S-[1-(2-hydroxyethyl)-1-methylbutyl]-(l)-cysteinylglycine (Cys-Gly-3M3SH). This molecule, secreted by the axilla, has a well-established role in malodour when metabolized to free thioalcohol by bacteria. We present Cys-Gly-3M3SH biotransformation data from a library of skin-isolated corynebacteria and staphylococci and report a significant variation in thioalcohol generation across individual bacterial species. Staphylococcus hominis, Staphylococcus haemolyticus and Staphylococcus lugdunensis were particularly efficient Cys-Gly-3M3SH transformers. In contrast, Staphylococcus epidermidis and Corynebacterium tuberculostearicum, both highly prevalent axillary commensals, are low producers of 3M3SH. We also identify significant differences between the ability of several isolates to biotransform Cys-Gly-3M3SH compared to S-benzyl-l-Cys-Gly, a dipeptide-linked version of a commonly used malodour precursor substrate. Finally, using traditional biochemical assays we subsequently establish that Cys-Gly-3M3SH is actively transported into S. hominis, rather than passively diffusing across the membrane. This work significantly enhances our knowledge of Cys-Gly-3M3SH biotransformation by physiologically important bacteria in the axillary microbiota. Differences in body odour generation by members of the underarm microbiota.
    Subject(s): Alcohols - metabolism ; Axilla - microbiology ; Biotransformation ; Corynebacterium - classification ; Corynebacterium - isolation & purification ; Corynebacterium - metabolism ; Hexanols - metabolism ; Humans ; Microbiota - physiology ; Odorants - analysis ; Skin - metabolism ; Skin - microbiology ; Staphylococcus - classification ; Staphylococcus - isolation & purification ; Staphylococcus - metabolism ; Staphylococcus epidermidis - metabolism ; Staphylococcus hominis - metabolism ; Sulfanilic Acids - metabolism ; Symbiosis
    E-ISSN: 1574-6968
    Source: Oxford Journals 2016 Current and Archive A-Z Collection
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  • 7
    Language: English
    In: Nature (London), 2015-06-04, Vol.522 (7554), p.81-84
    Description: No large group of recently extinct placental mammals remains as evolutionarily cryptic as the approximately 280 genera grouped as 'South American native ungulates'. To Charles Darwin, who first collected their remains, they included perhaps the 'strangest animal[s] ever discovered'. Today, much like 180 years ago, it is no clearer whether they had one origin or several, arose before or after the Cretaceous/Palaeogene transition 66.2 million years ago, or are more likely to belong with the elephants and sirenians of superorder Afrotheria than with the euungulates (cattle, horses, and allies) of superorder Laurasiatheria. Morphology-based analyses have proved unconvincing because convergences are pervasive among unrelated ungulate-like placentals. Approaches using ancient DNA have also been unsuccessful, probably because of rapid DNA degradation in semitropical and temperate deposits. Here we apply proteomic analysis to screen bone samples of the Late Quaternary South American native ungulate taxa Toxodon (Notoungulata) and Macrauchenia (Litopterna) for phylogenetically informative protein sequences. For each ungulate, we obtain approximately 90% direct sequence coverage of type I collagen α1- and α2-chains, representing approximately 900 of 1,140 amino-acid residues for each subunit. A phylogeny is estimated from an alignment of these fossil sequences with collagen (I) gene transcripts from available mammalian genomes or mass spectrometrically derived sequence data obtained for this study. The resulting consensus tree agrees well with recent higher-level mammalian phylogenies. Toxodon and Macrauchenia form a monophyletic group whose sister taxon is not Afrotheria or any of its constituent clades as recently claimed, but instead crown Perissodactyla (horses, tapirs, and rhinoceroses). These results are consistent with the origin of at least some South American native ungulates from 'condylarths', a paraphyletic assembly of archaic placentals. With ongoing improvements in instrumentation and analytical procedures, proteomics may produce a revolution in systematics such as that achieved by genomics, but with the possibility of reaching much further back in time.
    Subject(s): Amino Acid Sequence ; Animals ; Bone and Bones - chemistry ; Cattle ; Collagen Type I - chemistry ; Collagen Type I - genetics ; Female ; Fossils ; Mammals - classification ; Perissodactyla - classification ; Phylogeny ; Placenta ; Pregnancy ; Proteomics ; South America
    ISSN: 0028-0836
    E-ISSN: 1476-4687
    Source: Academic Search Ultimate
    Source: Alma/SFX Local Collection
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  • 8
    Language: English
    In: Nature chemistry, 2010-12, Vol.2 (12), p.1084-1088
    Description: The minerals involved in the formation of metazoan skeletons principally comprise glassy silica, calcium phosphate or carbonate. Because of their ancient heritage, glass sponges (Hexactinellida) may shed light on fundamental questions such as molecular evolution, the unique chemistry and formation of the first skeletal silica-based structures, and the origin of multicellular animals. We have studied anchoring spicules from the metre-long stalk of the glass rope sponge (Hyalonema sieboldi; Porifera, Class Hexactinellida), which are remarkable for their size, durability, flexibility and optical properties. Using slow-alkali etching of biosilica, we isolated the organic fraction, which was revealed to be dominated by a hydroxylated fibrillar collagen that contains an unusual [Gly-3Hyp-4Hyp] motif. We speculate that this motif is predisposed for silica precipitation, and provides a novel template for biosilicification in nature.
    Subject(s): Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Collagen - chemistry ; Evolution, Molecular ; Hydroxylation ; Nanoparticles - chemistry ; Nanoparticles - ultrastructure ; Porifera - chemistry ; Silicon Dioxide - chemistry
    ISSN: 1755-4330
    E-ISSN: 1755-4349
    Source: Academic Search Ultimate
    Source: Alma/SFX Local Collection
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  • 9
    Language: English
    In: Emerging infectious diseases, 2003-06, Vol.9 (6), p.702-707
    Description: Adventure travel is becoming more popular, increasing the likelihood of contact with unusual pathogens. We investigated an outbreak of leptospirosis in "Eco-Challenge" multisport race athletes to determine illness etiology and implement public health measures. Of 304 athletes, we contacted 189 (62%) from the United States and 26 other countries. Eighty (42%) athletes met our case definition. Twenty-nine (36%) case-patients were hospitalized; none died. Logistic regression showed swimming in the Segama River (relative risk [RR]=2.0; 95% confidence interval [CI]=1.3 to 3.1) to be an independent risk factor. Twenty-six (68%) of 38 case-patients tested positive for leptospiral antibodies. Taking doxycycline before or during the race was protective (RR=0.4, 95% CI=0.2 to 1.2) for the 20 athletes who reported using it. Increased adventure travel may lead to more frequent exposure to leptospires, and preexposure chemoprophylaxis for leptospirosis (200 mg oral doxycycline/week) may decrease illness risk. Efforts are needed to inform adventure travel participants of unique infections such as leptospirosis.
    Subject(s): Adult ; adventure travel immunoassay ; Borneo ; Case studies ; Disease Outbreaks ; DNA, Bacterial - analysis ; doxycycline ; febrile illness ; Female ; Fever - epidemiology ; Fever - microbiology ; Fresh Water - microbiology ; Humans ; Leptospira - genetics ; Leptospira - isolation & purification ; Leptospirosis ; Leptospirosis - diagnosis ; Leptospirosis - epidemiology ; Malaysia ; Malaysia - epidemiology ; Male ; Middle Aged ; Research ; Risk Factors ; Sports ; Travel ; Water Microbiology
    ISSN: 1080-6040
    E-ISSN: 1080-6059
    Source: Academic Search Ultimate
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 10
    Language: English
    In: Journal of Parkinson's disease, 2017-08-08, Vol.7 (3), p.523-531
    ISSN: 1877-7171
    E-ISSN: 1877-718X
    Source: Academic Search Ultimate
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