5 research outputs found

    A portfolio approach to analyzing complex human-environment interactions:Institutions and land change

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    The challenge confronting those seeking to understand the institutional dimensions of global environmental change and patterns of land-use and land-cover change is to find effective methods for analyzing the dynamics of socio-ecological systems. Such systems exhibit a number of characteristics that pose problems for the most commonly used statistical techniques and may require additional and innovative analytic tools. This article explores options available to researchers working in this field and recommends a strategy for achieving scientific progress. Statistical procedures developed in other fields of study are often helpful in addressing challenges arising in research into global change. Accordingly, we start with an assessment of some of the enhanced statistical techniques that are available for the study of socio-ecological systems. By themselves, however, even the most advanced statistical models cannot solve all the problems that arise in efforts to explain institutional effectiveness and patterns of land-use and land-cover change. We therefore proceed to an exploration of additional analytic techniques, including configurational comparisons and meta-analyses; case studies, counterfactuals, and narratives; and systems analysis and simulations. Our goal is to create a portfolio of complementary methods or, in other words, a tool kit for understanding complex human-environment interactions. When the results obtained through the use of two or more techniques converge, confidence in the robustness of key findings rises. Contradictory results, on the other hand, signal a need for additional analysis

    Transforming activity of Fbxo7 is mediated specifically through regulation of cyclin D/cdk6

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    D cyclins (D1, D2 and D3) and their catalytic subunits (cyclin-dependent kinases cdk4 and cdk6) have a facilitating, but nonessential, role in cell cycle entry. Tissue-specific functions for D-type cyclins and cdks have been reported; however, the biochemical properties of these kinases are indistinguishable. We report that an F box protein, Fbxo7, interacted with cellular and viral D cyclins and distinguished among the cdks that bind D-type cyclins, specifically binding cdk6, in vitro and in vivo. Fbxo7 specifically regulated D cyclin/cdk6 complexes: Fbxo7 knockdown decreased cdk6 association with cyclin and its overexpression increased D cyclin/cdk6 activity and E2F activity. Fbxo7 interacted with p27, but its enhancement of cyclin D/cdk6 activity was p21/p27 independent. Fbxo7 overexpression transformed murine fibroblasts, rendering them tumorigenic in athymic nude mice. Transformed phenotypes were dependent on cdk6, as knockdown of cdk6 reversed them. Fbxo7 was highly expressed in epithelial tumors, but not in normal tissues, suggesting that it may have a proto-oncogenic role in human cancers
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