A characterization of the scientific impact of Brazilian institutions

In this paper we studied the research activity of Brazilian Institutions for all sciences and also their performance in the area of physics between 1945 and December 2008. All the data come from the Web of Science database for this period. The analysis of the experimental data shows that, within a nonextensive thermostatistical formalism, the Tsallis \emph{q}-exponential distribution $N(c)$ can constitute a new characterization of the research impact for Brazilian Institutions. The data examined in the present survey can be fitted successfully by applying a universal curve namely, $N(c) \propto 1/[1+(q-1) c/T]^{\frac{1}{q-1}}$ with $q\simeq 4/3$ for {\it all} the available citations $c$, $T$ being an "effective temperature". The present analysis ultimately suggests that via the "effective temperature" $T$, we can provide a new performance metric for the impact level of the research activity in Brazil, taking into account the number of the publications and their citations. This new performance metric takes into account the "quantity" (number of publications) and the "quality" (number of citations) for different Brazilian Institutions. In addition we analyzed the research performance of Brazil to show how the scientific research activity changes with time, for instance between 1945 to 1985, then during the period 1986-1990, 1991-1995, and so on until the present. Finally, this work intends to show a new methodology that can be used to analyze and compare institutions within a given country.Comment: 7 pages, 5 figure

Mapas de coeficiente de cultura (kc) da fase do florescimento do milho para o Estado de Minas Gerais.

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation.

A variety of cellular pathways are regulated by protein modifications with ubiquitin-family proteins. SUMO, the Small Ubiquitin-like MOdifier, is covalently attached to lysine on target proteins via a cascade reaction catalyzed by E1, E2, and E3 enzymes. A major barrier to understanding the diverse regulatory roles of SUMO has been a lack of suitable methods to identify protein sumoylation sites. Here we developed a mass-spectrometry (MS) based approach combining chemical and enzymatic modifications to identify sumoylation sites. We applied this method to analyze the auto-sumoylation of the E1 enzyme in vitro and compared it to the GG-remnant method using Smt3-I96R as a substrate. We further examined the effect of smt3-I96R mutation in vivo and performed a proteome-wide analysis of protein sumoylation sites in Saccharomyces cerevisiae. To validate these findings, we confirmed several sumoylation sites of Aos1 and Uba2 in vivo. Together, these results demonstrate that our chemical and enzymatic method for identifying protein sumoylation sites provides a useful tool and that a combination of methods allows a detailed analysis of protein sumoylation sites

Sistema de Controle da Pesca de Mato Grosso do Sul SCPESCA/MS 15 - 2008.

Neste boletim encontram-se as informações sobre a pesca profissional e esportiva coletadas pelo Sistema de Controle da Pesca de Mato Grosso do Sul (SCPESCA/MS) no ano de 2008. Os dados obtidos são provenientes do pescado capturado em toda a Bacia do Alto Paraguai em Mato Grosso do Sul e vistoriado pela Polícia Militar Ambiental/MS.bitstream/item/54560/1/BP107.pd