10 research outputs found

    What Drives Downsizing of Protected Areas?: A Case Study of Amazon National Park

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    Researchers, NGOs, and the Brazilin government have paid significant attention to the preservation of Brazil’s natural landscapes. As a result, more than 25 million ha have been added to the system of protected areas in the region. However, the size and legal status of many protected areas throughout the Brazilian Amazon are being eroded. Understanding the drivers and outcomes of these reductions to protected areas is essential for the long-term management and preservation of ecosystem services. The objective of this article is to understand the social, political, and institutional factors behind a 2012 reduction to Amazon National Park (ANP), the first one created in Brazil’s Amazonia. Regional, national, and international demands for cattle and gold spurred an influx of migrants to the region, which increased the demand for land in and around ANP. In addition, the park’s semi-circled boundary created confusion on the ground over its exact limits. Institutional conflicts among environmental and colonization federal agencies further compounded the problem. Lastly, national energy shortages motivated the federal government to seek a site for hydropower generation that overlapped park boundaries. The coalescence of these drivers resulted in the encroachment and eventual downsizing of ANP by 47,080 hectares, and in the modification of 43 percent of the pre-2012 perimeter of the park

    Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO\u27s activity

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    AML1/ETO results from the t(8;21) associated with 12%–15% of acute myeloid leukemia. The AML1/ETO MYND domain mediates interactions with the corepressors SMRT and N-CoR and contributes to AML1/ETO\u27s ability to repress proliferation and differentiation of primary bone marrow cells as well as to enhance their self renewal in vitro. We solved the solution structure of the MYND domain and show it to be structurally homologous to the PHD and RING finger families of proteins. We also determined the solution structure of an MYND-SMRT peptide complex. We demonstrated that a single amino acid substitution that disrupts the interaction between the MYND domain and the SMRT peptide attenuated AML1/ETO\u27s effects on proliferation, differentiation, and gene expression

    Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers

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    There are four closely-related dengue virus (DENV) serotypes. Infection with one serotype generates antibodies that may cross-react and enhance infection with other serotypes in a secondary infection. We demonstrated that DENV serotype 2 (DENV2)–specific human monoclonal antibody (HMAb) 2D22 is therapeutic in a mouse model of antibody-enhanced severe dengue disease. We determined the cryo–electron microscopy (cryo-EM) structures of HMAb 2D22 complexed with two different DENV2 strains. HMAb 2D22 binds across viral envelope (E) proteins in the dimeric structure, which probably blocks the E protein reorganization required for virus fusion. HMAb 2D22 “locks” two-thirds of or all dimers on the virus surface, depending on the strain, but neutralizes these DENV2 strains with equal potency. The epitope defined by HMAb 2D22 is a potential target for vaccines and therapeutics

    World Congress Integrative Medicine & Health 2017: part two

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    World Congress Integrative Medicine & Health 2017: part two

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