IntroductionThis paper examines the process of developing a Research for Impact Tool in the contexts of general fiscal constraint, increased competition for funding, perennial concerns about the over-researching of Aboriginal and Torres Strait Islander issues without demonstrable benefits as well as conceptual and methodological difficulties of evaluating research impact. The aim is to highlight the challenges and opportunities involved in evaluating research impact to serve as resource for potential users of the research for impact tool and others interested in assessing the impact of research.Materials and methodsA combination of literature reviews, workshops with researchers, and reflections by project team members and partners using participatory snowball techniques.ResultsAssessing research impact is perceived to be difficult, akin to the so-called “wicked problem,” but not impossible. Heuristic and collaborative approach to research that takes the expectations of research users, research participants and the funders of research offers a pragmatic solution to evaluating research impact. The logic of the proposed Research for Impact Tool is based on the understanding that the value of research is to create evidence and/or products to support smarter decisions so as to improve the human condition. Research is, therefore, of limited value unless the evidence created is used to make smarter decisions for the betterment of society. A practical way of approaching research impact is, therefore, to start with the decisions confronting decision makers whether they are government policymakers, industry, professional practitioners, or households and the extent to which the research supports them to make smarter policy and practice decisions and the knock-on consequences of doing so. Embedded at each step in the impact planning and tracking process is the need for appropriate mix of expertise, capacity enhancement, and collaborative participatory learning-by-doing approaches.DiscussionThe tool was developed in the context of Aboriginal and Torres Strait Islander research but the basic idea that the way to assess research impact is to start upfront with the information needs of decisions makers is equally applicable to research in other settings, both applied (horizontal) and basic (vertical) research. The tool will be further tested and evaluated with researchers over the next 2 years (2016/17). The decision by the Australian Government to include ‘industry engagement’ and ‘impact’ as additions to the Excellence in Research for Australia (ERA) quality measures from 2018 makes the Research for Impact Tool a timely development. The wider challenge is to engage with major Australian research funding agencies to ensure consistent alignment and approaches across research users, communities, and funders in evaluating impact.
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Cyclosporine (CsA) is widely used in organ transplant patients to help prevent the patient's body from rejecting the organ. CsA has been shown to be a safe and highly effective immunosuppressive drug that binds with the protein Cyclophilin A (CypA) at active sites. However, the exact mechanism of this binding at the molecular level remains unknown. In this project, we elucidate the binding of CsA to CypA at the molecular level by computing their electron structures and revealing their interactions. We employ a novel technique called electron Computer-Aided Drug Design (eCADD) on the protein's full electron structure along with its hydrophobic pocket and the perturbation theory of the interaction between two wave functions. We have identified the wave function of CypA, the biological active residues and active atoms of CypA and CsA, the interaction site between CypA and CsA, and the hydrogen bonds in the ligand CsA binding site. All these calculated active residues, active atoms, and hydrogen bonds are in good agreement with recorded laboratory experiments and provide guidelines for designing new ligands of CypA. We believe that our eCADD framework can provide researchers with a cost-efficient new method of drug design based on the full electron structure of proteins.
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