Mennonites
Mostrando 1-4 de 4 artigos, teses e dissertações.
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1. Religious Nationalism in an Age of Globalization: The Case of Paraguay's "Mennonite State"
Abstract: This article uses the example of Mennonite nation-building in Paraguay during the 1920s and 1930s to argue that state formation is not inherently modernist. Tracing nineteenth and early twentieth-century discourses of Mennonite colonies in Imperial Russia, Canada, and elsewhere as a "state within a state," the essay advocates a reevaluation of theo
Almanack. Publicado em: 2016-12
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2. Vitalidade linguística do Plautdietsch em contato com variedades Standard faladas em comunidades menonitas no Brasil
O presente estudo analisa o contato linguístico alemão-português em três comunidades menonitas no sul do Brasil, bem como também o contato linguístico alemão-português-inglês em uma comunidade menonita localizada no estado de Goiás. Todos esses grupos são de origem anabatista (1525). Caracterizam-se, por isso, como étnico-religiosos. Mesmo com o
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 2011
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3. Analysis of the CCR5 gene coding region diversity in five South American populations reveals two new non-synonymous alleles in Amerindians and high CCR5*D32 frequency in Euro-Brazilians
The CC chemokine receptor 5 (CCR5) molecule is an important co-receptor for HIV. The effect of the CCR5*D32 allele in susceptibility to HIV infection and AIDS disease is well known. Other alleles than CCR5*D32 have not been analysed before, neither in Amerindians nor in the majority of the populations all over the world. We investigated the distribution of t
Genetics and Molecular Biology. Publicado em: 16/01/2009
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4. Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1 alpha impedes assembly of the E1 component of branched-chain alpha-keto acid dehydrogenase complex.
Maple Syrup Urine Disease (MSUD) in Mennonites is associated with homozygosity for a T to A transversion in the E1 alpha gene of the branched-chain alpha-keto acid dehydrogenase complex. This causes a tyrosine to asparagine substitution at position 393 (Y393N). To assess the functional significance of this missense mutation, we have carried out transfection