50,645 research outputs found

    Critical Realism and Empirical Research Methods in Education

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    In the light of recent writings of Richard Pring, and in relation to the application of empirical research methods in education, this paper offers a corrective to a neo-realist viewpoint and develops a critical realist perspective. The argument is made that the deployment of empirical research methods needs to be underpinned by a meta-theory embracing epistemological and ontological elements; that this meta-theory does not commit one to the view that absolute knowledge of the social world is possible; and that critical realism is the most appropriate meta-theory to underpin the use of empirical research methods. Further to this, unhelpful dualisms between quantitative and qualitative methodologies, and between structure and agency, are discussed in relation to neo-realist and critical realist perspectives

    Resolving the Quantitative-Qualitative Dilemma: A Critical Realist Approach

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    The philosophical issues underpinning the quantitative–qualitative divide in educational research are examined. Three types of argument which support a resolution are considered: pragmatism, false duality and warranty through triangulation. In addition a number of proposed strategies—alignment, sequencing, translation and triangulation—are critically assessed. The article concludes by suggesting that many of these ways of reconciling quantitative and qualitative methods and approaches are still deficient in relation to the development of an overarching and correct view of ontological and epistemological matters, and that critical realism offers a more coherent solution, where the reconciliation occurs at the ontological level

    Book Review: Risking Christ for Christ\u27s Sake

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    A review of Risking Christ for Christ\u27s Sake: Towards an Ecumenical Theology of Pluralism by M.M. Thomas

    Book Review: River of Compassion: A Christian Commentary on the Bhagavad Gita

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    A review of River of Compassion: A Christian Commentary on the Bhagavad Gita by Bede Griffiths

    Book Review: Inter-Faith Dialogue and World Community

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    A review of Inter-Faith Dialogue and World Community edited by Ch. Sreenivasa Rao

    Purification of TrkA intracellular domain and the characterization of novel intracellular proteins : a thesis presented in partial fulfilment of the requirements for the degree of Masters of Science in Molecular Biology at Massey University

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    Nerve growth factor (NGF) binds to its receptor, TrkA, at the tips of nerve cell axons to inhibit apoptosis, causing survival and differentiation. Some factors within this process are largely unknown, such as the role of the p75 receptor and the molecular mechanisms that occur within the cell. NGF binding causes dimerization of TrkA, which activates the intracellular kinase domain. Autophosphorylation on tyrosine residues stimulates binding to the receptor of several intracellular proteins that mediate the NGF response. This receptor complex has been demonstrated to be retrogradely transported to the cell body. Retrograde transport is hypothesized to occur in small vesicles that have been isolated in our lab using a cell fractionation protocol using in vitro reactions with an ATP regenerating system. Discovering the initial molecular interactions that occur upon NGF binding could further our knowledge of NGF's inhibition of apoptosis, providing us with a possible tool for treatment of diseases that occur when the regulation of apoptosis no longer exists. Novel proteins that were not previously identified were associated with TrkA in small vesicles after NGF activation. To isolate these proteins for further characterization, TrkA's intracellular domain (TrkAID) was expressed in E. Coli. This protein was found to be constitutively tyrosine-phosphorylated and therefore presumably active. In E.Coli, TrkAID protein was localized to the soluble fraction but smaller amounts were detected in the insoluble fraction. TrkAID was partially purified from the soluble fraction using a combination of salt disruption and denaturing techniques. The unpurified TrkAID was immunoprecipitated from the bacterial soluble fraction with an antibody to the C-terminus of TrkA, and some results suggest that immunoprecipitated TrkAID was able to stimulate ERK activation in untreated PC12 cells, but unfortunately this was not reproducible. If the protein could be purified with a combination of techniques, then it would provide a useful tool for studying the initial events in NGF stimulation, that is, the recruitment of several intracellular proteins to the tyrosine-phosphorylated intracellular domain of TrkA
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