985 resultados para Jose María Tomasi, Beato


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Fecha: s.f. (>1970 copia) / Unidad de instalación: Carpeta 45 - Expediente 2-16 / Nº de pág.: 3 (mecanografiadas)

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Contributed to: "Measuring the Changes": 13th FIG International Symposium on Deformation Measurements and Analysis; 4th IAG Symposium on Geodesy for Geotechnical and Structural Enginering (Lisbon, Portugal, May 12-15, 2008).

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[ES] Información sobre este proyecto ha servido de base a los siguientes artículos:

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O Diario..., como observa Borba de Moraes, "apresenta um roteiro muito resumido, mas muito exato" e, como diz Sacramento Blake, "atendendo ao que é escrito em viagem, e viagem de 648 léguas de terras invias e inexploradas. É, entretanto, trabalho de grande valor para a geografia dos lugares percorridos." O Diario... foi reeditado pelo Instituto Nacional do Livro em 1944.

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Ponencia presentada en I Congreso de Estudios Históricos del Condado de Treviño: 850 aniversario de la fundación de la Villa de Treviño, celebrado los días 1,2 y 3 de junio de 2011 en Treviño (Condado de Treviño)

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v. 1. ano de 1808 a 1811. 1836 -- v. 2. ano de 1812 a 1818 -- v. 3. ano de 1819 a 1822. 1837 -- v. 4 ano de 1823 a 1824. 1838 -- v. 5. ano a 1826. 1838 -- v. 6. ano de 1827 a 1828. 1841 -- v. 7. ano de 1829 a 1831 e índice. 1844.

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Duración (en horas): Más de 50 horas. Destinatario: Estudiante y Docente

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This series will include all those people who, by means of their contributions, great and small, played a part in the consolidation of ichthyology in Argentina. The general plan of this work consists of individual factsheets containing a list of works by each author, along with reference bibliography and, whenever possible, personal pictures and additional material. The datasheets will be published primarily in chronological order, although this is subject to change by the availability of materials for successive editions. This work represents another approach for the recovery and revalorization of those who set the foundations of Argentine ichthyology while in diverse historical circumstances. I expect this to be the beginning of a major work that achieves the description of such a significant part of the history of natural sciences in Argentina.

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8 cartas (mecanografiadas) ; 225x285 mmm. Ubicación: Caja 1 - Carpeta 20

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Background: Sporadic Creutzfeldt-Jakob disease (sCJD) is a rare neurodegenerative disorder in humans included in the group of Transmissible Spongiform Encephalopathies or prion diseases. The vast majority of sCJD cases are molecularly classified according to the abnormal prion protein (PrPSc) conformations along with polymorphism of codon 129 of the PRNP gene. Recently, a novel human disease, termed "protease-sensitive prionopathy", has been described. This disease shows a distinct clinical and neuropathological phenotype and it is associated to an abnormal prion protein more sensitive to protease digestion. Case presentation: We report the case of a 75-year-old-man who developed a clinical course and presented pathologic lesions compatible with sporadic Creutzfeldt-Jakob disease, and biochemical findings reminiscent of "protease-sensitive prionopathy". Neuropathological examinations revealed spongiform change mainly affecting the cerebral cortex, putamen/globus pallidus and thalamus, accompanied by mild astrocytosis and microgliosis, with slight involvement of the cerebellum. Confluent vacuoles were absent. Diffuse synaptic PrP deposits in these regions were largely removed following proteinase treatment. PrP deposition, as revealed with 3F4 and 1E4 antibodies, was markedly sensitive to pre-treatment with proteinase K. Molecular analysis of PrPSc showed an abnormal prion protein more sensitive to proteinase K digestion, with a five-band pattern of 28, 24, 21, 19, and 16 kDa, and three aglycosylated isoforms of 19, 16 and 6 kDa. This PrPSc was estimated to be 80% susceptible to digestion while the pathogenic prion protein associated with classical forms of sporadic Creutzfeldt-Jakob disease were only 2% (type VV2) and 23% (type MM1) susceptible. No mutations in the PRNP gene were found and genotype for codon 129 was heterozygous methionine/valine. Conclusions: A novel form of human disease with abnormal prion protein sensitive to protease and MV at codon 129 was described. Although clinical signs were compatible with sporadic Creutzfeldt-Jakob disease, the molecular subtype with the abnormal prion protein isoforms showing enhanced protease sensitivity was reminiscent of the "protease-sensitive prionopathy". It remains to be established whether the differences found between the latter and this case are due to the polymorphism at codon 129. Different degrees of proteinase K susceptibility were easily determined with the chemical polymer detection system which could help to detect proteinase-susceptible pathologic prion protein in diseases other than the classical ones.

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1 carta (manuscrita) : 275x214mm. Ubicación: Caja 1 - Carpeta 81

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7 cartas (mecanografiadas y manuscritas) ; entre 180x130mm y 214x139mm. Ubicación: Caja 1 - Carpeta 82

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209 p. : il., gráf.

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10 cartas (mecanografiadas); entre 210x255mm y 210x310mm. [La carta fechada el 10-11-1942 esta incompleta, falta la primera hoja]