Relevant bibliographies by topics / Alzheimer's disease; Amyloid precursor protein

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Alzheimer's disease; Amyloid precursor protein'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Alzheimer's disease; Amyloid precursor protein"

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Nalbantoglu, Josephine. "β-Amyloid Protein in Alzheimer's Disease." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 18, S3 (August 1991): 424–27. http://dx.doi.org/10.1017/s0317167100032595.

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ABSTRACT:β-amyloid protein, a 42-43 amino acid polypeptide, accumulates abnormally in senile plaques and the cerebral vasculature in Alzheimer's disease. This polypeptide is derived from a membrane-associated precursor which has several isoforms expressed in many tissues. The precursor protein is processed constitutively within the P-amyloid domain, leading to the release of the large β-terminal portion into the extracellular medium, β-amyloid protein may be toxic to certain neuronal cell types and its early deposition may be an important event in the pathogenesis of Alzheimer's disease.
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Multhaup, G. "Amyloid precursor protein, copper and Alzheimer's disease." Biomedicine & Pharmacotherapy 51, no. 3 (January 1997): 105–11. http://dx.doi.org/10.1016/s0753-3322(97)86907-7.

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O'Brien, Richard J., and Philip C. Wong. "Amyloid Precursor Protein Processing and Alzheimer's Disease." Annual Review of Neuroscience 34, no. 1 (July 21, 2011): 185–204. http://dx.doi.org/10.1146/annurev-neuro-061010-113613.

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Harrison, Paul J., Wendy H. Wighton-Benn, Josephine M. Heffernan, Maurice W. Sanders, and R. Carl A. Pearson. "Amyloid Precursor Protein mRNAs in Alzheimer's Disease." Neurodegeneration 5, no. 4 (December 1996): 409–15. http://dx.doi.org/10.1006/neur.1996.0055.

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Nunan, Janelle, and David H. Small. "Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease." Essays in Biochemistry 38 (October 1, 2002): 37–49. http://dx.doi.org/10.1042/bse0380037.

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The proteolytic processing of the amyloid-beta protein precursor plays a key role in the development of Alzheimer's disease. Cleavage of the amyloid-beta protein precursor may occur via two pathways, both of which involve the action of proteases called secretases. One pathway, involving beta- and gamma-secretase, liberates amyloid-beta protein, a protein associated with the neurodegeneration seen in Alzheimer's disease. The alternative pathway, involving alpha-secretase, precludes amyloid-beta protein formation. In this review, we describe the progress that has been made in identifying the secretases and their potential as therapeutic targets in the treatment or prevention of Alzheimer's disease.
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ROSSOR, M. N., S. NEWMAN, R. S. J. FRACKOWIAK, P. LANTOS, and A. M. KENNEDY. "Alzheimer's Disease Families with Amyloid Precursor Protein Mutationsa." Annals of the New York Academy of Sciences 695, no. 1 (September 1993): 198–202. http://dx.doi.org/10.1111/j.1749-6632.1993.tb23052.x.

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Ayala-Grosso, Carlos, Gordon Ng, Sophie Roy, and George S. Robertson. "Caspase-cleaved Amyloid Precursor Protein in Alzheimer's Disease." Brain Pathology 12, no. 4 (April 5, 2006): 430–41. http://dx.doi.org/10.1111/j.1750-3639.2002.tb00460.x.

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Ahmad, Syed S., Shahzad Khan, Mohammad A. Kamal, and Umam Wasi. "The Structure and Function of α, β and γ-Secretase as Therapeutic Target Enzymes in the Development of Alzheimer’s Disease: A Review." CNS & Neurological Disorders - Drug Targets 18, no. 9 (January 15, 2020): 657–67. http://dx.doi.org/10.2174/1871527318666191011145941.

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: Alzheimer's disease is a progressive neurodegenerative disorder that affects the central nervous system. There are several factors that cause AD, like, intracellular hyperphosphorylated Tau tangles, collection of extracellular Amyloid-β42 and generation of reactive oxygen species due to mitochondrial dysfunction. This review analyses the most active target of AD and both types of AD-like early-onset AD and late-onset AD. BACE1 is a β-secretase involved in the cleavage of amyloid precursor protein and the pathogenesis of Alzheimer's disease. The presenilin proteins play a critical role in the pathogenesis of Alzheimer malady by intervening the intramembranous cleavage of amyloid precursor protein and the generation of amyloid β. The two homologous proteins PS1 and PS2 speak to the reactant subunits of particular γ-secretase edifices that intercede an assortment of cellular processes. Natural products are common molecular platforms in drug development in AD. Many natural products are being tested in various animal model systems for their role as a potential therapeutic target in AD. Presently, there are a few theories clarifying the early mechanisms of AD pathogenesis. Recently, research advancements in the field of nanotechnology, which utilize macromolecular strategies to make drugs in nanoscale measurements, offer nanotechnology-based diagnostic tools and drug carriers which are highly sensitive for effective drug targeting in the treatment of Alzheimer’s disease.
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Pluta, Ryszard, Liang Ouyang, Sławomir Januszewski, Yang Li, and Stanisław J. Czuczwar. "Participation of Amyloid and Tau Protein in Post-Ischemic Neurodegeneration of the Hippocampus of a Nature Identical to Alzheimer's Disease." International Journal of Molecular Sciences 22, no. 5 (February 28, 2021): 2460. http://dx.doi.org/10.3390/ijms22052460.

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Recent evidence suggests that amyloid and tau protein are of vital importance in post-ischemic death of CA1 pyramidal neurons of the hippocampus. In this review, we summarize protein alterations associated with Alzheimer's disease and their gene expression (amyloid protein precursor and tau protein) after cerebral ischemia, as well as their roles in post-ischemic hippocampus neurodegeneration. In recent years, multiple studies aimed to elucidate the post-ischemic processes in the development of hippocampus neurodegeneration. Their findings have revealed the dysregulation of genes for amyloid protein precursor, β-secretase, presenilin 1 and 2, tau protein, autophagy, mitophagy, and apoptosis identical in nature to Alzheimer's disease. Herein, we present the latest data showing that amyloid and tau protein associated with Alzheimer's disease and their genes play a key role in post-ischemic neurodegeneration of the hippocampus with subsequent development of dementia. Therefore, understanding the underlying process for the development of post-ischemic CA1 area neurodegeneration in the hippocampus in conjunction with Alzheimer's disease-related proteins and genes will provide the most important therapeutic development goals to date.
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Parent, Angèle T., and Gopal Thinakaran. "Modeling Presenilin-Dependent Familial Alzheimer's Disease: Emphasis on Presenilin Substrate-Mediated Signaling and Synaptic Function." International Journal of Alzheimer's Disease 2010 (2010): 1–11. http://dx.doi.org/10.4061/2010/825918.

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Mutations inPSENgenes, which encode presenilin proteins, cause familial early-onset Alzheimer's disease (AD). Transgenic mouse models based on coexpression of familial AD-associated presenilin and amyloid precursor protein variants successfully mimic characteristic pathological features of AD, including plaque formation, synaptic dysfunction, and loss of memory. Presenilins function as the catalytic subunit ofγ-secretase, the enzyme that catalyzes intramembraneous proteolysis of amyloid precursor protein to releaseβ-amyloid peptides. Familial AD-associated mutations in presenilins alter the site ofγ-secretase cleavage in a manner that increases the generation of longer and highly fibrillogenicβ-amyloid peptides. In addition to amyloid precursor protein,γ-secretase catalyzes intramembrane proteolysis of many other substrates known to be important for synaptic function. This paper focuses on how various animal models have enabled us to elucidate the physiological importance of diverseγ-secretase substrates, including amyloid precursor protein and discusses their roles in the context of cellular signaling and synaptic function.
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Dissertations / Theses on the topic "Alzheimer's disease; Amyloid precursor protein"

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Dunbar, Charlotte Emily. "Fe65-amyloid precursor protein signalling and Alzheimer's disease." Thesis, King's College London (University of London), 2017. https://kclpure.kcl.ac.uk/portal/en/theses/fe65amyloid-precursor-protein-signalling-and-alzheimers-disease(7a7a8605-20a7-4a78-9048-c47b3cb324ce).html.

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Deposition of Aβ in amyloid plaques and accumulation of hyperphosphorylated tau in neurofibrillary tangles are hallmark pathologies of Alzheimer’s disease. Changes in APP processing alter Aβ generation and are likely to affect APP function, which may also contribute to Alzheimer’s disease. APP binds to adaptor protein Fe65 and one proposed function of this complex is to signal to the nucleus to regulate gene transcription. However, the mechanisms that regulate APP-Fe65 binding and the genes regulated by this pathway are poorly understood. Phosphorylation is a common mechanism for regulating protein-protein interactions and Fe65 is phosphorylated by several kinases, including ERK1/2. The first hypothesis investigated in this thesis is that BDNF signalling, which leads to ERK1/2 activation, stimulates Fe65 phosphorylation to regulate its binding to APP. BDNF was found to induce ERK1/2-dependent phosphorylation of Fe65 and, in a variety of assays including the use of phosphomutants, BDNF-induced phosphorylation of Fe65 was shown to inhibit the binding of Fe65 to APP. Unpublished next generation sequencing of Fe65 knockout mouse brains suggested that Fe65 may affect the wnt signalling pathway, which regulates GSK3β activity. GSK3β is a kinase involved in the hyperphosphorylation of tau in Alzheimer’s disease. The second hypothesis tested in this thesis is that Fe65 regulates genes that are linked to GSK3β activity and tau phosphorylation. RT-qPCR carried out on Fe65 knockout mouse brains and siRNA-treated rat cortical neurons found that expression of wnt receptor Fzd-1 was affected by loss of Fe65. Additionally, loss of Fe65 decreased both GSK3β activity and tau phosphorylation. These results show that Fe65 is involved with APP to function in a key process that can be regulated by BDNF, a treatment previously shown to be neuroprotective in Alzheimer’s disease models. Furthermore, they reaffirm the link between APP and Fe65 and link Fe65 to tau phosphorylation, which may be the first step in understanding the relationship between the two hallmark pathologies of Alzheimer’s disease.
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McLoughlin, D. M. "Identification of proteins interacting with the Alzheimer's disease amyloid precursor protein." Thesis, King's College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.343724.

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Stephens, David John. "Intracellular processing of the Alzheimer's #beta#-amyloid precursor protein." Thesis, St George's, University of London, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.362427.

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Bowes, Simone. "Processing of Alzheimer's amyloid precursor protein in cultured cells." Thesis, Sheffield Hallam University, 1999. http://shura.shu.ac.uk/19377/.

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The deposition in the brain of the 4 kDa beta-amyloid peptide (betaA4), from amyloid precursor protein (APP), is a key pathology in Alzheimer's disease (AD). The single APP gene is spliced to give 3 major isoforms. In the majority of body tissues, the most common APP isoforms are APP[751] and APP[770], which both contain a Kunitz protease inhibitor (KPI) domain, APP[695] is predominant in the brain. APP is processed through several pathways, not all of which lead to betaA4 production. Central nervous system (CNS) neurones in vivo secrete betaA4, which can be detected in the cerebrospinal fluid, though it is unknown why betaA4 is deposited in the brain in AD. NTera2 (NT2) cells derived from a human teratocarcinoma were used as a model of APP processing. Retinoic acid induces these cells to differentiate into a neuronal phenotype (NT2N cells), which has been shown to closely resemble immature human CNS neurones. Both cell types produce high levels of endogenous APP.Intracellular and secreted APP was studied in both cell types by means of western blotting and immunoprecipitation with a panel of antibodies. It was found that NT2 cells predominantly make and secrete KPI containing APP. NT2N cells make and secrete predominantly APP[695] though some KPI containing APP is also present. There is evidence that neurones in the AD brain are in a state of stress, which could increase levels of APP due to a heat shock promotor region in its gene. To investigate this, NT2 cells were subjected to a heat shock, which resulted in increased levels of heat shock protein (HSP) and APP. KPI containing APP predominated, but there was no corresponding increase in secreted APP. Both cell types were also serum deprived, which resulted in little effect on protein production in NT2 stem cells. However, the neuronal cells showed a small increase in intracellular, KPI-containing APP and in HSP. A reduction in overall APP secretion, and cessation of KPI secretion accompanied this. To further investigate the effects of shock on APP production, mRNA levels in control and serum deprived NT2 and NT2N cells were studied using in situ hybridisation. Control NT2 cells contain low levels of APP751, APP695 and HSP mRNA, with higher levels of APP[770] mRNA. After serum deprivation HSP, APP[751] and APP[770] mRNA levels all rose significantly, while APP[695] mRNA levels were unchanged. Control NT2N cells contained high levels of APP695 mRNA, lower levels of APP[751] mRNA, and very low levels of APP[770] and HSP mRNA. Serum deprivation resulted in unchanged levels of APP[695] and APP[770] mRNA, while APP[751] and HSP levels were increased. These findings indicate that cellular stress can result in increased levels of APP, specifically APP[751], in both neuronal and non-neuronal cells. Increased levels of this isoform have also been reported in AD. Hence cellular stress leads to an increase in an APP isoform implicated in AD, and could also provide an explanation for the increased levels of betaA4 in the disease.
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Prager, Kai. "Investigation of #alpha#-secretase cleavage of amyloid precursor protein." Thesis, Queen's University Belfast, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300994.

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Webster, Marie-Therese. "Studies on the amyloid precursor protein : implication for Alzheimer's disease." Thesis, University College London (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338835.

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Boyce, Susan Gillian. "Amyloid precursor protein subtypes and secretases implicated in Alzheimer's disease." Thesis, Sheffield Hallam University, 2011. http://shura.shu.ac.uk/19378/.

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To date there is no definite understanding to suggest a clear causative route in the events which lead to the neurodegenerative disorder Alzheimer disease (AD) however several proteins have been implicated. Eight proteins that have been implicated in AD have been mapped across seven regions of non-human primate brain tissue from a Macaca fascicularis in this study: APP[770]; APP[751]; APP[695]; ADAM 9, 10 and 17 as alpha-secretases; BACE 1 as beta-secretase and PS1 as gamma-secretase. The APP[695] isoform was found to have the highest levels in the frontal and temporal regions. However, the APP[751] isoform was found to be at the highest level, with very low levels of APP[695] in the soluble fractions of the hippocampus and hypothalamus. Membrane associated levels of alpha-secretases were found to be highest in frontal, temporal, cerebellar, hypothalamus, basal ganglia and hippocampus. The distribution of BACE 1 was found to be low in the frontal and temporal regions in comparison to all the other regions sampled where levels exceeded the levels in the frontal region by over three times. The distribution of gamma-secretase across the regions showed an even distribution with the exception of the hippocampus which had an almost double level in comparison to the other areas sampled. With a relatively high level of the gamma-secretase and gamma-secretase and a concomitant very high level of the APP[kpi] containing subtype APP[751] this would tend to indicate a different sensitivity in the hippocampus and hypothalamus compared to the other regions sampled. The conclusion that may be drawn from these findings is that since the hippocampus and hypothalamus are two of the earliest regions to be affected in AD altered processing of the subtype APP[751] may indicate a regional sensitivity. The culture of NT2/D1 clonal cells with retinoic acid results in the appearance of post-mitotic human neuronal cells. The APP isoforms and secretases present in the brain regions of the Macaca fascicularis have been observed in the NT2 cells as they have been cultured with retinoic acid to obtain the NT2-N neuron-like cells. NT2 cells cultured without retinoic acid produced the sAPP[kpi] subtype in contrast to the cells cultured in the presence of retinoic acid where APP[695] is the predominant subtype. The three secretases of interest in AD were expressed in the NT2 cells and the NT2-N cells similar to the expression in Macaca fascicularis brain tissue. The most notable difference between the brain tissue and NT2/NT2-N cells was to be seen in the expression of BACE 1 as beta-secretase. In the NT2/NT2-N cells BACE 1 appears to be expressed as a stable and high molecular weight form not seen in the Macaca fascicularis brain tissue. The gamma-secretase expression in NT2/NT2-N cells represented by immuno-blotting with an antibody raised against Presenilinl reflected the position seen in the brain tissue. The secretases and APP subtypes in the NT2-N cells most closely reflect the expression found in the hippocampus and hypothalamus of the Macaca fascicularis brain tissue and therefore are a good cellular model for AD.
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McAllister, Cecilia. "An investigation of the proteolytic processing of amyloid precursor protein." Thesis, Queen's University Belfast, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300614.

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Newton, Jillian Rose Ann. "Strategies for the examination of Alzheimer's disease amyloid precursor protein isoforms." Thesis, Sheffield Hallam University, 2004. http://shura.shu.ac.uk/20769/.

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The principal aim of this research project has been the utilisation of various proteomic techniques in the investigation of the Alzheimer's disease amyloid precursor protein (APP) isoforms, namely APP[695], APP[751] and APP[770]. One of the most noticeable pathological characteristics of Alzheimer's disease is the presence of neuritic plaques in brain tissue. The chief protein constituent of neuritic plaques is the beta amyloid peptide. This peptide is proteolytically cleaved from APP, as such the interest in APP isoforms is great and a rapid detection method for the presence of each isoform would be a huge advantage to the research effort with regards to the determination and concentration in both diseased and non-diseased states. Two-dimensional gel electrophoresis and peptide mass fingerprinting are two of the most important techniques in the proteomics arena and both are investigated fully in this work. Retinoic acid induced Ntera 2 cells, derived from a human teratocarcinoma cell line, were the in vitro source of APP. Initial isolation of APP was performed by immunoprecipitation, using a monoclonal antibody raised to amino acids 1-17 of the beta-amyloid peptide sequence, which is present in all three alpha secretase cleaved isoforms of interest. The next step was to separate whole APP into its isoform components by two-dimensional gel electrophoresis. The resulting protein spots were then subjected to peptide mass fingerprinting employing the different digest reagents, trypsin, endoproteinase Asp-N and formic acid. Initial distinction between the APP isoforms could be seen upon examination of theoretical in silica digests using the various digest reagents mentioned. The in silica digests revealed peptides unique to each isoform that in theory could be used as indicators of isoform presence.
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Golde, Todd Eliot. "Analysis of the beta amyloid precursor protein mRNAs in Alzheimer's disease." Case Western Reserve University School of Graduate Studies / OhioLINK, 1991. http://rave.ohiolink.edu/etdc/view?acc_num=case1056572599.

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Books on the topic "Alzheimer's disease; Amyloid precursor protein"

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Masters, C. L., K. Beyreuther, M. Trillet, and Y. Christen, eds. Amyloid Protein Precursor in Development, Aging and Alzheimer’s Disease. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-01135-5.

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The structure and function of Alzheimer's amyloid beta proteins. Austin: R.G. Landes, 1994.

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1924-, Kameyama Masakuni, ed. [Beta]-amyloid precursor proteins and neurotransmitter function: Proeedings of the eighth Workshop on Neurotransmitters and Diseases, Tokyo, June 1, 1991. Amsterdam, The Netherlands: Excerpta Medica, 1991.

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Page, Deaglan. Spatial learning deficits in rats carrying the Swedish mutation for amyloid precursor protein overexpression as a model for Alzheimer's disease. (s.l: The Author), 2001.

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Dowler, Brynn C. Endocytosis: Structural components, functions, and pathways. New York: Nova Biomedical Books, 2010.

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Tanzi, Rudolph E. Decoding darkness: The search for the genetic causes of Alzheimer's disease. Cambridge, Mass: Perseus Publishing, 2000.

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Tanzi, Rudolph E. Decoding darkness: The search for the genetic causes of Alzheimer's disease. Cambridge, Mass: Perseus Pub., 2000.

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B, Parson Ann, ed. Decoding darkness: The search for the genetic causes of Alzheimer's disease. Cambridge, Mass: Perseus Publ., 2000.

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L, Masters Colin, and Colloque médecine et recherche (9th : 1993 : Lyon, France), eds. Amyloid protein precursor in development, aging, and Alzheimer's disease. Berlin: Springer-Verlag, 1994.

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Sekoulidis, Joannis. Transgenic analysis of the Alzheimer's disease amyloid precursor protein (APP). 2004.

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Book chapters on the topic "Alzheimer's disease; Amyloid precursor protein"

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Sisodia, S. S., G. Thinakaran, B. T. Lamb, H. H. Slunt, C. S. Koch, S. D. Ginsberg, A. C. Y. Lo, et al. "In Vivo Biology of Amyloid Precursor Protein/Amyloid Precursor-like Proteins and Transgenic Animal Models of Alzheimer’s Disease." In Alzheimer’s Disease, 61–76. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-03248-0_4.

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Huber, Gerda S., Jean-Luc Moreau, James R. Martin, Yannick Bailly, Jean Mariani, and Bernard Brugg. "ß-Amyloid Precursor Protein — Role in Cognitive Brain Function?" In Alzheimer Disease, 87–90. Boston, MA: Birkhäuser Boston, 1997. http://dx.doi.org/10.1007/978-1-4612-4116-4_14.

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Hendriks, Lydia, Chris De Jonghe, Patrick Cras, Jean-Jacques Martin, and Christine Van Broeckhoven. "β-Amyloid Precursor Protein and Early-Onset Alzheimer's Disease." In Novartis Foundation Symposia, 170–80. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514924.ch11.

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Masters, C. L., G. Multhaup, J. M. Salbaum, A. Weidemann, T. Dyrks, C. Hilbich, P. Fischer, et al. "Precursor of Alzheimer’s Disease (PAD) A4 Amyloid Protein." In Genetics and Alzheimer’s Disease, 134–41. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73647-6_14.

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Haass, C. "Molecular Processing Pathways of β-Amyloid Precursor Protein: Therapeutic Implications." In Alzheimer’s Disease, 77–92. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-03248-0_5.

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Golde, T. E., X. D. Cai, T. T. Cheung, M. Shoji, and S. G. Younkin. "Production of Amyloid β Protein from Normal and Mutated Amyloid β Protein Precursors." In Amyloid Protein Precursor in Development, Aging and Alzheimer’s Disease, 36–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-01135-5_4.

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Price, D. L., B. T. Lamb, J. D. Gearhart, L. J. Martin, L. C. Walker, E. H. Koo, D. R. Borchelt, and S. S. Sisodia. "Amyloid in Alzheimer’s Disease and Animal Models." In Amyloid Protein Precursor in Development, Aging and Alzheimer’s Disease, 156–68. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-01135-5_15.

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Hardy, J., M. Mullan, F. Crawford, K. Duff, R. Crook, P. Diaz, C. Bennett, et al. "Genetic Variability and Alzheimer’s Disease." In Amyloid Protein Precursor in Development, Aging and Alzheimer’s Disease, 190–98. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-01135-5_18.

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Allinquant, B., P. Hantraye, C. Bouillot, K. L. Moya, and A. Prochiantz. "Implication of the Amyloid Precursor Protein in Neurite Outgrowth." In Alzheimer’s Disease: Lessons from Cell Biology, 66–69. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79423-0_6.

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Selkoe, D. J. "Protein Chemical and Molecular Biological Studies of Amyloid Precursor Proteins in Alzheimer’s Disease." In Immunology and Alzheimer’s Disease, 76–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-46634-2_8.

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Conference papers on the topic "Alzheimer's disease; Amyloid precursor protein"

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MÜLLER-SPAHN, F., W. NASER, U. KLAGES, S. MODELL, I. BARTKE, and C. HOCK. "ELISA QUANTIFICATION OF THE AMYLOID A4 PRECURSOR PROTEIN IN CEREBROSPHINAL FLUID OF PATIENTS WITH ALZHEIMER'S DISEASE." In IX World Congress of Psychiatry. WORLD SCIENTIFIC, 1994. http://dx.doi.org/10.1142/9789814440912_0010.

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RajaRajeswari, P., S. Viswanadha Raju, Amira S. Ashour, Nilanjan Dey, and Valentina E. Balas. "Active site cavities identification of amyloid beta precursor protein: Alzheimer disease study." In 2016 IEEE 20th Jubilee International Conference on Intelligent Engineering Systems (INES). IEEE, 2016. http://dx.doi.org/10.1109/ines.2016.7555143.

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ZAMBRANO, NICOLA, RAFFAELLA FARAONIO, ROSARIO MOSCA, OLIMPIA LONGO, PAOLO ARCARI, and TOMMASO RUSSO. "INTERACTION OF THE AMYLOID PRECURSOR PROTEIN WITH PTB DOMAIN-CONTAINING ADAPTORS AND THEIR POTENTIAL INVOLVEMENT IN ALZHEIMER'S DISEASE." In Proceedings of the International School of Biocybernetics. WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776563_0037.

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McCarthy, Thomas, Jin Yu, Salim El-Amouri, Sebastiano Gattoni-Celli, Steve Richieri, Luis De Taboada, Jackson Streeter, and Mark S. Kindy. "Transcranial laser therapy alters amyloid precursor protein processing and improves mitochondrial function in a mouse model of Alzheimer's disease." In SPIE BiOS, edited by Michael R. Hamblin, Ronald W. Waynant, and Juanita Anders. SPIE, 2011. http://dx.doi.org/10.1117/12.877028.

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Noda, Minoru, Takeshi Asai, Kaoru Yamashita, Toshinori Shimanouchi, Hiroshi Umakoshi, Masanori Okuyama, and Ryouichi Kuboi. "A bio-thermochemical sensor of microbolometer immobilized liposome for detection of causative protein of Alzheimer's disease, amyloid beta." In 2009 IEEE Sensors. IEEE, 2009. http://dx.doi.org/10.1109/icsens.2009.5398264.

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