Thesis (Ph.D.) -- University of Adelaide, Dept. of Pathology, 1999. / Appendum pasted into front end-papers. Bibliography: leaves xiii-xliii.

Appendum pasted into front end-papers. / Bibliography: leaves xiii-xliii. / xi, 195, xliii leaves : ill. (chiefly col.) ; 30 cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Traumatic brain injury (TBI) effects neuronal cell bodies (NCBs), axons and dendrites in a complex fashion, producing a spectrum of damage dependent on the initial injury and secondary effects. Accumulation of amyloid precursor (APP) in NSBs and axons is a feature of TBI. This accumulation may be due to impairment of the axonal transport of APP and/or upregulation of APP mRNA synthesis. This thesis hypothesizes that mechanical deformation, which is not severe enough to cause immediate cell death, results in increased APP mRNA and antigen expression as an acute phase response to injury. / Thesis (Ph.D.)--University of Adelaide, Dept. of Pathology, 1999

Thesis (Ph. D.)--University of Washington, 2007. / Vita. Includes bibliographical references (leaves 100-123).

Leung Man-hin. / Thesis submitted in: August 2004. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2005. / Includes bibliographical references (leaves 119-133). / Abstracts in English and Chinese. / Abstract --- p.ii / Acknowledgement --- p.iv / Abbreviations --- p.v / Figure List --- p.vii / Chapter Chapter 1: --- General introduction / Chapter 1.1 --- Introduction --- p.1 / Chapter 1.2 --- Pathogenesis of Alzheimer's disease / Chapter 1.2.1 --- Amyloid cascade hypothesis --- p.2 / Chapter 1.2.2 --- Tauopathy --- p.5 / Chapter 1.3 --- The amyloid precursor proteins / Chapter 1.3.1 --- Structure of amyloid precursor proteins and related peptides --- p.5 / Chapter 1.3.2 --- Amyloid precursor protein mutations --- p.6 / Chapter 1.3.3 --- Amyloid precursor protein processing --- p.10 / Chapter 1.3.4 --- Physiological roles of APP --- p.12 / Chapter 1.3.5 --- The pathophysiological role of Ap --- p.17 / Chapter 1.3.6 --- The pathophysiological role of APP-CTF --- p.20 / Chapter 1.4 --- The role of proteases in amyloid precursor protein processing / Chapter 1.4.1 --- α-secretase and p-secretase --- p.22 / Chapter 1.4.2 --- γ-secretase complex --- p.30 / Chapter 1.4.3 --- Caspases --- p.36 / Chapter 1.4.4 --- Kallikrein-like proteases --- p.37 / Chapter 1.5 --- Objective of the present study --- p.40 / Chapter Chapter 2: --- Materials and methods / Chapter 2.1 --- Experimental procedure / Chapter 2.1.1 --- Plasmid construction --- p.42 / Chapter 2.1.2 --- "DNA purification, ligation and restriction enzyme digestion" --- p.44 / Chapter 2.1.3 --- Competent cell preparation --- p.47 / Chapter 2.1.4 --- Transformation --- p.47 / Chapter 2.1.5 --- Plasmid miniprep --- p.48 / Chapter 2.1.6 --- Prokaryotic expression of neurosin --- p.49 / Chapter 2.1.7 --- SDS-PAGE --- p.51 / Chapter 2.1.8 --- Protein sample preparation --- p.51 / Chapter 2.1.9 --- Western Blot --- p.52 / Chapter 2.1.10 --- Immobilized metal affinity chromatography --- p.54 / Chapter 2.1.11 --- Enzyme assay --- p.55 / Chapter 2.1.12 --- Cell culture and transfection --- p.56 / Chapter 2.1.13 --- Live cell imaging --- p.57 / Chapter 2.2 --- Materials --- p.59 / Chapter Chapter 3 : --- Results / Chapter 3.1 --- Recombinant expression and characterization of neurosin / Chapter 3.1.1 --- Construction of neurosin prokaryotic expression vectors --- p.62 / Chapter 3.1.2 --- Prokaryotic expression of neurosin --- p.64 / Chapter 3.1.3 --- Neurosin was expressed as inclusion bodies --- p.68 / Chapter 3.1.4 --- Co-expression of molecular chaperones with neurosin --- p.70 / Chapter 3.1.5 --- Purification of recombinant neurosin by IMAC --- p.76 / Chapter 3.1.6 --- Enzyme assay --- p.81 / Chapter 3.2 --- Effect of neurosin on APP processing in neuronal cells / Chapter 3.2.1 --- Generation of APP constructs --- p.84 / Chapter 3.2.2 --- Expression of APP in mammalian cultures --- p.89 / Chapter 3.2.3 --- Cellular localization of APP and its processing products --- p.96 / Chapter 3.2.4 --- The role of over-expression of neurosin on APP processing in B103 cells --- p.101 / Chapter Chapter 4: --- Discussion / Chapter 4.1 --- Discussion of neurosin expression --- p.103 / Chapter 4.2 --- Discussion of APP cell model --- p.109 / Chapter 4.3 --- Conclusion --- p.119 / References --- p.121 / Appendix / Chapter A. --- Tables on primers used --- p.138 / Chapter B. --- Plasmid maps --- p.139 / Chapter C. --- Raw data on the DNA sequencing --- p.141

Diss. (sammanfattning) Stockholm : Karol. inst., 2004. / Härtill 5 uppsatser.

Thesis (M.Sc.) - Carleton University, 2006. / Includes bibliographical references (p. 106-118). Also available in electronic format on the Internet.

Dissertation (Ph.D.) -- University of Texas Southwestern Medical Center at Dallas, 2008. / Vita. Bibliography: p. 97-121.

Thesis (Ph.D.) -- University of Rhode Island, 2008. / Typescript. Includes bibliographical references (leaves 141-159).

Thesis (M.Sc.). / Written for the Dept. of Neurology and Neurosurgery. Title from title page of PDF (viewed 2009/08/07). Includes bibliographical references.

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