Relevant bibliographies by topics / Amyloid beta-protein precursor

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  2. Dissertations / Theses
  3. Books
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Academic literature on the topic 'Amyloid beta-protein precursor'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2024

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Journal articles on the topic "Amyloid beta-protein precursor"

1

Koo, E. H., S. L. Squazzo, D. J. Selkoe, and C. H. Koo. "Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody." Journal of Cell Science 109, no. 5 (May 1, 1996): 991–98. http://dx.doi.org/10.1242/jcs.109.5.991.

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Amyloid beta-protein, the principal constituent of amyloid fibrils found in senile plaques and blood vessels in Alzheimer's disease, is constitutively produced and released into medium of cultured cells. Amyloid beta-protein is derived by proteolysis of the beta-amyloid precursor protein by unclear mechanisms. Beta-amyloid precursor protein is a transmembrane protein which can be processed to release a large secretory product or processed in the endosomal/lysosomal pathway without secretion. Previous studies have shown that from the cell surface, beta-amyloid precursor protein may be released
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Naushad, Mehjabeen, Siva Sundara Kumar Durairajan, Amal Kanti Bera, Sanjib Senapati та Min Li. "Natural Compounds with Anti-BACE1 Activity as Promising Therapeutic Drugs for Treating Alzheimerʼs Disease". Planta Medica 85, № 17 (16 жовтня 2019): 1316–25. http://dx.doi.org/10.1055/a-1019-9819.

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AbstractAlzheimerʼs disease is a neurodegenerative disease that leads to irreversible neuronal damage. Senile plaques, composed of amyloid beta peptide, is the principal abnormal characteristic of the disease. Among the factors involved, the secretase enzymes, namely, α secretase, beta-site amyloid precursor protein-cleaving enzyme, β secretase, and γ secretase, hold consequential importance. Beta-site amyloid precursor protein-cleaving enzyme 1 is considered to be the rate-limiting factor in the production of amyloid beta peptide. Research supporting the concept of inhibition of beta-site amy
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Cai, X., T. Golde, and S. Younkin. "Release of excess amyloid beta protein from a mutant amyloid beta protein precursor." Science 259, no. 5094 (January 22, 1993): 514–16. http://dx.doi.org/10.1126/science.8424174.

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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 sec
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Parkin, Edward T., Jessica E. Hammond, Lauren Owens, and Matthew D. Hodges. "The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein." PLOS ONE 17, no. 1 (January 13, 2022): e0255715. http://dx.doi.org/10.1371/journal.pone.0255715.

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The amyloid cascade hypothesis proposes that excessive accumulation of amyloid beta-peptides is the initiating event in Alzheimer’s disease. These neurotoxic peptides are generated from the amyloid precursor protein via sequential cleavage by β- and γ-secretases in the ’amyloidogenic’ proteolytic pathway. Alternatively, the amyloid precursor protein can be processed via the ’non-amyloidogenic’ pathway which, through the action of the α-secretase a disintegrin and metalloproteinase (ADAM) 10, both precludes amyloid beta-peptide formation and has the additional benefit of generating a neuroprote
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Wilquet, Valérie, and Bart De Strooper. "Amyloid-beta precursor protein processing in neurodegeneration." Current Opinion in Neurobiology 14, no. 5 (October 2004): 582–88. http://dx.doi.org/10.1016/j.conb.2004.08.001.

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Schubert, David, Greg Cole, Tsunao Saitoh, and Tilman Oltersdorf. "Amyloid beta protein precursor is a mitogen." Biochemical and Biophysical Research Communications 162, no. 1 (July 1989): 83–88. http://dx.doi.org/10.1016/0006-291x(89)91965-7.

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Ling, Xie, R. N. Martins, M. Racchi, S. Craft, and E. Helmerhorst. "Amyloid beta antagonizes insulin promoted secretion of the amyloid beta protein precursor." Journal of Alzheimer's Disease 4, no. 5 (November 1, 2002): 369–74. http://dx.doi.org/10.3233/jad-2002-4504.

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Ayoubi, Riham, Maryam Fotouhi, Donovan Worrall, Kathleen Southern, and Carl Laflamme. "Identification of high-performing antibodies for amyloid-beta precursor protein for use in Western Blot, immunoprecipitation and immunofluorescence." F1000Research 12 (August 9, 2023): 956. http://dx.doi.org/10.12688/f1000research.139867.1.

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The amyloid-beta precursor protein is a transmembrane protein expressed in many tissues and highly concentrated in the brain. The protein is of significant interest due to its involvement in the generation of amyloidogenic β-amyloid peptides, prone to plaque formation that is characteristic of Alzheimer’s Disease. The scientific community would benefit from the availability of high-quality anti-amyloid-beta precursor protein antibodies to enhance reproducible research on this target. In this study, we characterized eleven amyloid-beta precursor protein commercial antibodies for Western blot, i
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Ghiso, J., E. Matsubara, A. Koudinov, N. H. Choi-Miura, M. Tomita, T. Wisniewski та B. Frangione. "The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex". Biochemical Journal 293, № 1 (1 липня 1993): 27–30. http://dx.doi.org/10.1042/bj2930027.

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The amyloid fibrils deposited in Alzheimer's neuritic plaque cores and cerebral blood vessels are mainly composed of aggregated forms of a unique peptide, 39-42 amino acids long, named amyloid beta (A beta). A similar, although soluble, A beta (‘sA beta’) has been identified in cerebrospinal fluid, plasma and cell supernatants, indicating that it is normally produced by proteolytic processing of its precursor protein, amyloid precursor protein (APP). Using direct binding experiments we have isolated and characterized an 80 kDa circulating protein that specifically interacts with a synthetic pe
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Dissertations / Theses on the topic "Amyloid beta-protein precursor"

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Dooley, Nora P. "Analysis of beta-amyloid precursor protein in Alzheimer's fibroblasts." Thesis, McGill University, 1992. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=56982.

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One of the hallmarks of Alzheimer's disease is the accumulation of beta-amyloid protein in the core of neuritic plaques. This 38-40 amino acid polypeptide is derived from a larger precursor known as beta-amyloid precursor protein (BAPP). In this thesis the expression of this precursor in cultured human fibroblasts obtained from Alzheimer's patients and age-matched controls is examined at the mRNA and protein level. Using the technique of reverse transcriptase-polymerase chain reaction, human fibroblasts were found to express BAPP transcripts encoding 770, 751, 714, and 695 amino acids. In immu
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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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Jung, Sonia Sun-Yung. "Expression and processing of the Alzheimer's beta-amyloid precursor protein." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0031/NQ64584.pdf.

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Jung, Sonia Sun-Yung 1968. "Expression and processing of the Alzheimer's beta-amyloid precursor protein." Thesis, McGill University, 1999. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=36618.

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Alzheimer's disease (AD) is the most common neurodegenerative disease affecting the elderly. One of the main pathological hallmarks of AD is abundant senile plaques found in brain parenchyma and in the meningovasculature. The core of these senile plaques is predominantly composed of the 40--43 amino acid beta-amyloid (Abeta) peptide which arises from proteolytic cleavage of the beta-amyloid precursor protein (betaAPP), a glycoprotein with a predicted structure of a transmembrane protein. Most studies of betaAPP expression and processing have focused on cultured cell systems. Previously, our la
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Kim, Joung-Hun. "Electrophysiological and biochemical studies of #beta#-amyloid precursor protein fragments." Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.394383.

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Sultana, Joynab. "Behavioral Effects of Amyloid Precursor Protein beta Mutation in zebrafish." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-421155.

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Amyloid precursor protein beta (βAPP) plays an important role in the pathogenesis of Alzheimer’s disease. An appb mutant strain of zebrafish has been previously generated and has shown increased boldness. Here we tested boldness by Novel Tank Diving Test and compared the results between the wildtype AB strain controls (WT) (N=16) and appb mutant strain (N=28), as well as between two Swedish testing institutions that use different protocols. Fish were tracked by automated video tracking in Ethovision. Compared with the wild type fish, using both the Uppsala and Gothenburg protocols, the mutant
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Selivanova, Alexandra. "Intracellular dynamics of Alzheimer disease-related proteins /." Stockholm, 2007. http://diss.kib.ki.se/2007/978-91-7357-234-7/.

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Heuvel, Corinna van den. "Studies on upregulation of amyloid precursor protein in response to traumatic brain injury /." Title page, contents and abstract only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phv22723.pdf.

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Ly, Philip T. T. "Glycogen synthase kinase-3 signaling in Alzheimer's disease : regulation of beta-amyloid precursor protein processing and amyloid beta protein production." Thesis, University of British Columbia, 2012. http://hdl.handle.net/2429/42848.

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Glycogen synthase kinase 3 (GSK3) is a serine/threonine kinase that plays a part in a number of physiological processes ranging from glycogen metabolism to gene transcription. Recent studies indicated that GSK3 also involved in the formation of Alzheimer’s disease (AD) pathologies: neurofibrillary tangles and amyloid plaques. Neurofibrillary tangles develop when abnormal tau proteins accumulate inside neurons and form insoluble filaments, and amyloid plaques develop when the amyloid β protein (Aβ) accumulates in increasingly insoluble forms. The Aβ peptide is generated through sequential cleav
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Leutz, Steffen. "Neuronaler Zelltod bei der Alzheimer-Demenz : Einfluss von b-Amyloid [Beta-Amyloid] und Amyloid-precursor-Protein /." Aachen : Shaker, 2002. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=009735379&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Books on the topic "Amyloid beta-protein precursor"

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Weiming, Xia, and Xu Huaxi, eds. Amyloid precursor protein: A practical approach. Boca Raton, Fla: CRC Press, 2005.

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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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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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M, Nitsch Roger, and International Study Group on the Pharmacology of Memory Disorders Associated with Aging. Meeting, eds. Alzheimer's disease: Amyloid precursor proteins, signal transduction, and neuronal transplantation. New York, N.Y: New York Academy of Sciences, 1993.

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Christian, Haass, ed. Molecular biology of Alzheimer's disease: Genes and mechanisms involved in amyloid generation. Amsterdam: Harwood Academic Publishers, 1998.

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1936-, Wurtman Richard J., and New York Academy of Sciences., eds. The neurobiology of Alzheimer's disease: Edited by Richard J. Wurtman ... [et al.]. New York: New York Academy of Sciences, 1996.

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1936-, Wurtman Richard J., and Study Group on the Pharmacology of Memory Disorders Associated with Aging. Meeting, eds. The Neurobiology of Alzheimer's disease. New York, N.Y: New York Academy of Sciences, 1996.

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A, Nixon Ralph, Banner Carl D. B, and New York Academy of Sciences., eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York: NewYork Academy of Sciences, 1992.

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B, Banner Carl D., and Nixon Ralph A, eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York, N.Y: New York Academy of Sciences, 1992.

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M, Hooper N., ed. Alzheimer's disease: Methods and protocols. Totowa, N.J: Humana Press, 2000.

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Book chapters on the topic "Amyloid beta-protein precursor"

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Caporaso, G. L., S. E. Gandy, J. D. Buxbaum, T. Suzuki, C. Nordstedt, K. Iverfeldt, T. V. Ramabhadran, A. J. Czernik, A. C. Nairn, and P. Greengard. "Protein Phosphorylation Regulates the Cellular Trafficking and Processing of the Alzheimer Beta/A4 Amyloid Precursor Protein." In Molecular Mechanisms of Membrane Traffic, 201–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_42.

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Yamada, Takeshi, Ryutaro Izumi, Hiroyuki Sasaki, Hirokazu Furuya, Ikuo Goto, and Yoshiyuki Sasaki. "Structure and Expression of mRNA for the Mouse Homolog of Alzheimer Amyloid Beta Protein Precursor." In Basic, Clinical, and Therapeutic Aspects of Alzheimer’s and Parkinson’s Diseases, 47–50. Boston, MA: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4684-5844-2_9.

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El-Hachem, Nehme, Benjamin Haibe-Kains, Athar Khalil, Firas H. Kobeissy, and Georges Nemer. "AutoDock and AutoDockTools for Protein-Ligand Docking: Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1(BACE1) as a Case Study." In Methods in Molecular Biology, 391–403. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6952-4_20.

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Kosik, K. S., and D. J. Selkoe. "Studies of the Beta-Amyloid Precursor Protein in Brain and the Pathological Transformation of Tau into the Neurofibrillary Tangle." In Genetics and Alzheimer’s Disease, 164–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73647-6_18.

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Anand, Abhinav, Neha Sharma, Monica Gulati, and Navneet Khurana. "Amyloid Beta." In Research Anthology on Diagnosing and Treating Neurocognitive Disorders, 1–17. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-3441-0.ch001.

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Alzheimer's disease (AD), exhibiting accumulation of amyloid beta (Aβ) peptide as a foremost protagonist, is one of the top five causes of deaths. It is a neurodegenerative disorder (ND) that causes a progressive decline in memory and cognitive abilities. It is characterized by deposition of Aβ plaques and neurofibrillary tangles (NFTs) in the neurons, which in turn causes a decline in the brain acetylcholine levels. Aβ hypothesis is the most accepted hypothesis pertaining to the pathogenesis of AD. Amyloid Precursor Protein (APP) is constitutively present in brain and it is cleaved by three proteolytic enzymes (i.e., alpha, beta, and gamma secretases). Beta and gamma secretases cleave APP to form Aβ. Ubiquitin Proteasome System (UPS) is involved in the clearing of Aβ plaques. AD also involves impairment in UPS. The novel disease-modifying approaches involve inhibition of beta and gamma secretases. A number of clinical trials are going on worldwide with moieties targeting beta and gamma secretases. This chapter deals with an overview of APP and its enzymatic cleavage leading to AD.
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Anand, Abhinav, Neha Sharma, Monica Gulati, and Navneet Khurana. "Amyloid Beta." In Advances in Medical Diagnosis, Treatment, and Care, 235–51. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-5282-6.ch011.

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Alzheimer's disease (AD), exhibiting accumulation of amyloid beta (Aβ) peptide as a foremost protagonist, is one of the top five causes of deaths. It is a neurodegenerative disorder (ND) that causes a progressive decline in memory and cognitive abilities. It is characterized by deposition of Aβ plaques and neurofibrillary tangles (NFTs) in the neurons, which in turn causes a decline in the brain acetylcholine levels. Aβ hypothesis is the most accepted hypothesis pertaining to the pathogenesis of AD. Amyloid Precursor Protein (APP) is constitutively present in brain and it is cleaved by three proteolytic enzymes (i.e., alpha, beta, and gamma secretases). Beta and gamma secretases cleave APP to form Aβ. Ubiquitin Proteasome System (UPS) is involved in the clearing of Aβ plaques. AD also involves impairment in UPS. The novel disease-modifying approaches involve inhibition of beta and gamma secretases. A number of clinical trials are going on worldwide with moieties targeting beta and gamma secretases. This chapter deals with an overview of APP and its enzymatic cleavage leading to AD.
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Penke, B., and T. Harkány. "Physiological role of amyloid precursor protein (APP) and beta-amyloid peptides." In Molecular Pathomechanisms and New Trends in Drug Research, 402–10. CRC Press, 2002. http://dx.doi.org/10.1201/9780203219973.ch33.

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Obici, L., G. De Rosa, G. Palladini, S. Marciano, S. Donadei, E. Arbustini, L. Verga, M. Concardi, G. Ferrari, and G. Merlini. "Hereditary Cerebral Amyloid Angiopathy Associated with a Novel Amyloid Beta Precursor Protein Mutation." In Amyloid and Amyloidosis, 396–98. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494-141.

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Palladini, G., L. Obici, G. Merlini, S. Marciano, L. Verga, G. Ferrari, G. De Rosa, E. Arbustini, S. Donadei, and M. Concardi. "Hereditary Cerebral Amyloid Angiopathy Associated with a Novel Amyloid Beta Precursor Protein Mutation." In Amyloid and Amyloidosis, 396–98. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494.ch136.

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"Amyloid Beta (A4) Precursor Protein-Binding, Family B, Member 1 Interacting Protein (APBB1IP)." In Encyclopedia of Signaling Molecules, 312. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_100202.

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Conference papers on the topic "Amyloid beta-protein precursor"

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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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von Arnim, Christine, Michael Wagner, Petra Weber, and Herbert Schneckenburger. "TIRET microscopy: monitoring protein (amyloid precursor protein and beta-secretase) interaction on the surface of living cells." In Biomedical Optics (BiOS) 2007, edited by Daniel L. Farkas, Robert C. Leif, and Dan V. Nicolau. SPIE, 2007. http://dx.doi.org/10.1117/12.699856.

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Shakila, G., C. Meganathan, N. Sundaraganesan, and H. Saleem. "Pharmacophore based virtual screening, molecular docking and density functional theory approaches to discover the potent beta-amyloid precursor protein (B-APP) inhibitor." In 7TH NATIONAL CONFERENCE ON HIERARCHICALLY STRUCTURED MATERIALS (NCHSM-2019). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5114592.

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Reports on the topic "Amyloid beta-protein precursor"

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Elmann, Anat, Orly Lazarov, Joel Kashman, and Rivka Ofir. therapeutic potential of a desert plant and its active compounds for Alzheimer's Disease. United States Department of Agriculture, March 2015. http://dx.doi.org/10.32747/2015.7597913.bard.

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We chose to focus our investigations on the effect of the active forms, TTF and AcA, rather than the whole (crude) extract. 1. To establish cultivation program designed to develop lead cultivar/s (which will be selected from the different Af accessions) with the highest yield of the active compounds TTF and/or achillolide A (AcA). These cultivar/s will be the source for the purification of large amounts of the active compounds when needed in the future for functional foods/drug development. This task was completed. 2. To determine the effect of the Af extract, TTF and AcA on neuronal vulnerabi
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