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A biophysical study of amyloid-β aggregation and toxicity determinantsBolognesi, Benedetta Maria January 2011 (has links)
No description available.
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Single molecule studies of amyloid-β aggregationNarayan, Priyanka January 2012 (has links)
No description available.
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Development of a coarse-grained protein model and molecular dynamics studies of amyloid-[beta] peptide aggregation /Han, Wei. January 2007 (has links)
Thesis (Ph.D.)--Hong Kong University of Science and Technology, 2007. / Includes bibliographical references. Also available in electronic version.
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Studies on the mechanisms of A[beta] aggregation and toxicity in DrosophilaSperetta, Elena January 2011 (has links)
No description available.
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The effects of partial denaturation on in vitro fibril formation /Vernaglia, Brian Anthony. January 2004 (has links)
Thesis (Ph.D.)--Tufts University, 2004. / Adviser: Eliana De Bernardez Clark. Submitted to the Dept. of Chemical Engineering. Includes bibliographical references (leaves 173-181). Access restricted to members of the Tufts University community. Also available via the World Wide Web;
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Studies on upregulation of amyloid precursor protein in response to traumatic brain injury /Heuvel, Corinna van den. January 1999 (has links) (PDF)
Thesis (Ph.D.) -- University of Adelaide, Dept. of Pathology, 1999. / Appendum pasted into front end-papers. Bibliography: leaves xiii-xliii.
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Studies on mechanism and intervention of alzheimer's beta-amyloid fibrillogenesis /Wong, Ka-Man. January 2002 (has links)
Thesis (M. Phil.)--Hong Kong University of Science and Technology, 2002. / Includes bibliographical references (leaves 113-125). Also available in electronic version. Access restricted to campus users.
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Spectroscopic investigations of the beta-amyloid peptideSchmidt, Emily Ann. January 2008 (has links)
Thesis (M.S.)--University of Missouri-Columbia, 2008. / The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file (viewed on August 14, 2009) Includes bibliographical references.
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An investigation of the behavioral and neurochemical changes followingthe administration of ibotenic acid, 192IgG-saporin or B-amyloid (1-40) into the rat brain: possible animalmodels for Alfheimer's diseaseNag, Subodh. January 2001 (has links)
published_or_final_version / Physiology / Doctoral / Doctor of Philosophy
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Probing the role of the 37kDa/67kDa laminin receptor in amyloid beta mediated pathogenesis in alzheimer's diseaseDias, Bianca Da Costa 23 September 2014 (has links)
A thesis submitted to the Faculty of Science, University of the Witwatersrand, Johannesburg, in fulfilment of the requirements for the degree of Doctor of Philosophy. Johannesburg, 2014. / Alzheimer’s Disease (AD) is characterized by neurofibrillary tangles, senile plaques and
neuronal loss. Although the mechanisms underlying Amyloid beta 42 (Aβ42) neurotoxicity
have not been firmly established, it is proposed that the neuronal loss is elicited through
associations with cell surface receptors. The cellular prion protein (PrPc) has been identified
as an Aβ42 receptor and as a regulator of the amyloidogenic cleavage pathway. As Aβ42
shares common binding partners with the 37kDa/67kDa laminin receptor (LRP/LR),
including PrPc, we investigated whether these proteins interact and assessed the pathological
significance of this association. LRP/LR was found to co-localize with Aβ on the cell surface.
The occurrence of FRET suggested that an interaction between LRP/LR and Aβ indeed exists
at the cell surface. Furthermore, pull down assays and Aβ-specific ELISAs demonstrated that
LRP/LR forms a physical association with endogenously shed Aβ, thereby verifying the
physiological relevance of this association. Antibody blockade by IgG1-iS18 and shRNAmediated
downregulation of LRP/LR significantly enhanced cell viability and proliferation
and decreased apoptosis in cells co-treated with Aβ42 when compared to cells incubated with
Aβ42 alone. In addition, antibody blockade and shRNA-mediated downregulation of LRP/LR
significantly impeded Aβ42 internalization. These results suggest that LRP/LR acts as an
internalization receptor for Aβ42 and may thereby contribute to the cytotoxicity of the
neuropeptide by facilitating intracellular Aβ42 accumulation and aggregation - which has
consequences for cell proliferation and may promote apoptosis. These findings recommend
anti-LRP/LR specific antibodies and shRNAs as potential therapeutic tools for Alzheimer’s
Disease treatment.
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