Relevant bibliographies by topics / Amyloid beta (1-40)

Academic literature on the topic 'Amyloid beta (1-40)'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Amyloid beta (1-40)"

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Zheng, Weihua, Min-Yeh Tsai, and Peter G. Wolynes. "Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1–42) and Amyloid Beta(1–40)." Journal of the American Chemical Society 139, no. 46 (November 7, 2017): 16666–76. http://dx.doi.org/10.1021/jacs.7b08089.

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Chrambach, Adam, Andreas Chrambach, and Sheryl K. Brining. "Gel electrophoretic distinction between Congo Red nonreactive beta-amyloid (1—42) and beta-amyloid (1—40)." Electrophoresis 21, no. 4 (March 1, 2000): 760–61. http://dx.doi.org/10.1002/(sici)1522-2683(20000301)21:4<760::aid-elps760>3.0.co;2-5.

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Usui, Kenji, Shin-ichiro Yokota, Kazuya Iwata, and Yoshio Hamada. "Novel Purification Process for Amyloid Beta Peptide(1-40)." Processes 8, no. 4 (April 15, 2020): 464. http://dx.doi.org/10.3390/pr8040464.

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Amyloid beta peptide (Aβ)-related studies require an adequate supply of purified Aβ peptide. However, Aβ peptides are “difficult sequences” to synthesize chemically, and low yields are common due to aggregation during purification. Here, we demonstrate an easier synthesis, deprotection, reduction, cleavage, and purification process for Aβ(1-40) using standard 9-fluorenylmethyloxycarbonyl (Fmoc)-protected amino acids and solid-phase peptide synthesis (SPPS) resin [HMBA (4-hydroxymethyl benzamide) resin] that provides higher yields of Aβ(1-40) than previous standard protocols. Furthermore, purification requires a similar amount of time as conventional purification processes, although the peptide must be cleaved from the resin immediately prior to purification. The method described herein is not limited to the production of Aβ(1-40), and can be used to synthesize other easily-oxidized and aggregating sequences. Our proposed methodology will contribute to various fields using “difficult sequence” peptides, such as pharmaceutical and materials science, as well as research for the diagnosis and treatment of protein/peptide misfolding diseases.
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Belitzky, Alik, Naomi Melamed-Book, Aryeh Weiss, and Uri Raviv. "The dynamic nature of amyloid beta (1–40) aggregation." Physical Chemistry Chemical Physics 13, no. 30 (2011): 13809. http://dx.doi.org/10.1039/c1cp20832b.

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Stamatelopoulos, Kimon, Christine J. Pol, Colby Ayers, Georgios Georgiopoulos, Aikaterini Gatsiou, Emmanouil S. Brilakis, Amit Khera, Konstantinos Drosatos, James A. de Lemos, and Konstantinos Stellos. "Amyloid-Beta (1-40) Peptide and Subclinical Cardiovascular Disease." Journal of the American College of Cardiology 72, no. 9 (August 2018): 1060–61. http://dx.doi.org/10.1016/j.jacc.2018.06.027.

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Cleary, James, Jodie M. Hittner, Michael Semotuk, Patrick Mantyh, and Eugene O'Hare. "Beta-amyloid(1–40) effects on behavior and memory." Brain Research 682, no. 1-2 (June 1995): 69–74. http://dx.doi.org/10.1016/0006-8993(95)00323-i.

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Pérez, Virginia, Noelia Fandos, Pedro Pesini, and Manuel Sarasa. "P1-244: Validation of beta-amyloid test as a reliable tool for quantifying beta-amyloid 1-40 and beta-amyloid 1-42 in blood." Alzheimer's & Dementia 9 (July 2013): P241. http://dx.doi.org/10.1016/j.jalz.2013.05.468.

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Cerofolini, Linda, Enrico Ravera, Sara Bologna, Thomas Wiglenda, Annett Böddrich, Bettina Purfürst, Iryna Benilova, et al. "Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils." Chemical Communications 56, no. 62 (2020): 8830–33. http://dx.doi.org/10.1039/d0cc02463e.

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KLEIN, AUTUMN M., NEIL W. KOWALL, and ROBERT J. FERRANTE. "Neurotoxicity and Oxidative Damage of Beta Amyloid 1-42 versus Beta Amyloid 1-40 in the Mouse Cerebral Cortex." Annals of the New York Academy of Sciences 893, no. 1 OXIDATIVE/ENE (November 1999): 314–20. http://dx.doi.org/10.1111/j.1749-6632.1999.tb07845.x.

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Maltseva, Elena, and Gerald Brezesinski. "Adsorption of Amyloid Beta (1-40) Peptide to Phosphatidylethanolamine Monolayers." ChemPhysChem 5, no. 8 (August 20, 2004): 1185–90. http://dx.doi.org/10.1002/cphc.200400045.

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Dissertations / Theses on the topic "Amyloid beta (1-40)"

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Shivji, Arif P. "Investigation of #beta#-amyloid (1-40) peptide fibrilization by scanning probe microscopy." Thesis, University of Nottingham, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338493.

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Nag, Subodh. "An investigation of the behavioral and neurochemical changes following the administration of ibotenic acid, 192IgG-saporin or B-amyloid (1-40) into the rat brain possible animal models for Alfheimer's disease /." Hong Kong : University of Hong Kong, 2001. http://sunzi.lib.hku.hk/hkuto/record.jsp?B23426196.

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Nag, Subodh. "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 disease." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2001. http://hub.hku.hk/bib/B31242200.

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Helm, Jeffrey. "Cellular signaling of human microglia in response to [beta]-amyloid 1-40." Thesis, 2001. http://hdl.handle.net/2429/11750.

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Microglia are resident immune cells of the brain that are activated in response to trauma and inflammation. Activated microglia exhibit characteristics similar to peripheral macrophages, such as the expression of irnmunomolecules, secretion of proinflammatory substances and phagocytic activity. Like macrophages, microglia exhibit these characteristics in order to defend the brain from infection and aid in the repair of damaged tissue. However, in Alzheimer's Disease (AD) microglia can become overactivated resulting in the release of substances that escalate Marnmation and ultimately cause neuronal death. A protein implicated in the progression of AD is β-amyloid (Aβ). Aβ production is increased in AD and deposits of Aβ form throughout the brain, which are correlated to the activation of microglia and neuronal death. Studies have shown that Aβ can activate microglia and cause changes in the cellular functions of these cells. For example, in microglia Aβ has been shown to cause increases in the production of pro-inflarnrnatory cytokines and reactive oxygen species. The objective of this work was to characterize the actions of Aβ 40, a commonly expressed form of Aβ, on the mobilization of intracellular calcium ([Ca²⁺]0 in human microglia. The rational was that subsequent pharmacological modulation of the calcium signals induced by Aβ 40 could then be used to alter the cellular functions of microglia, such as the secretion of neurotoxic factors. The first study used calcium sensitive microfluorescence to examine Aβ 40 actions on [Ca²], mediated signaling pathways. Aβ 40 application (4 and 10 μM) to microglia caused a rise in [Ca²j to a plateau level which was sustained following the removal of the peptide. Calcium-free external solution (Ca- free PSS) was used to show that the primary contribution to the [Ca²]; rise came from the influx of extracellular calcium. A small amount of intracellular calcium release is also possible since Ca-free PSS did not totally inhibit the Aβ 40-induced [Ca²][sub i] response. The Aβ 40 mediated calcium influx was sensitive to depolarization since low chloride solution applied extracellularly inhibited the influx of calcium. Additional experiments suggested that a store-operated channel (SOC) did not mediate the Aβ 40-induced calcium influx since an inhibitor of this pathway, SKF96365, had no effect on the [Ca²][sub i] rise. At present, a specific modifier of the Aβ 40-induced influx pathway has not been identified. The next study examined the actions of Aβ 40 on COX-2 expression. COX-2 is an enzyme responsible for prostaglandin synthesis and free radical formation that is overexpressed in AD . Microglia cultures were treated with Aβ 40 for 24 hrs and the expression of COX-2 was determined through RT-PCR analysis. The results show that Aβ 40 significantly increased COX-2 expression. However, it is not know if the enhancement of COX-2 is linked to the Aβ 40-induced increase in [Ca²][sub i]. The third study examined the potential of Aβ 40 to induce the production of neurotoxic substances by human microglia. Neuroblastoma cells were treated with supernatant from microglia exposed to Aβ 40 and the neurotoxic effects were evaluated by assessing cell viability. The results indicate that supernatant from Aβ 40 treated microglia decreased neuroblastoma viability, however the decrease was not significantly different from Aβ 40 applied directly to neuroblastoma cells. This result suggests that a larger number of human microglia are required to record the effects of neurotoxic substances in the cell viability assays used.
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Ko, Chien-Hsien, and 柯建賢. "Electrochemical impedance spectroscopy detection of amyloid beta peptide 1-40 and 1-42 in plasma." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/84598145191007982075.

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碩士
國立中興大學
機械工程學系所
102
Alzheimer’s Disease (AD) is a common dementia disease. A patient who suffers this kind of disease, his/her brain will deposit amyloid plaques and neurofibrillary tangles. The amyloid plaques are generated by β and γ secretase which cleaved Amyloid Precursor Protein (APP). Then they will produce Aβ1-40 and Aβ1-42 proteins which accumulated and aggregated in human’s brain. These proteins can be detected in 5 to 10pg/ml plasma or cerebrospinal fluid. There are two methods to detect those proteins which called ELISA and Western Blot. However, these methods have to be operated by professional trainer which needs high cost and days to accomplish the whole processes. The functions of Western Blot in this study are to examine the specificity and molecular weight of protein and to check self-assembly monolayer and contact angle on chips by using ESCA technique. there are two kinds of experiments that will be discussed in this study. The first one is serum with Aβ1-40 and the second one is serum with Aβ1-42 which measured by using electrochemical impedance spectroscopy. Afterwards, the physical meaning will be explained by using equivalent circuit model. This research is accomplished by using hot embossing method which produced a 3D-nanostructure on specimen. Then the self-assembly monolayer, antibody and antigen will be coated on the specimen. In order to obtain serum without Aβ1-40 and Aβ1-42, we have to use the affinity chromatography method which removed volunteer’s serum Aβ1-40 and Aβ1-42 and then serves as a diluted base. Then Aβ1-40 and Aβ1-42 are added to the serum creating a standard curve between impedance and concentration. The dependent level of serum with Aβ1-40 is measured by EIS concentration measurement which resulted a linear equation of Y = 19526.91 X + 33023 with error R2 = 0.97785 in impedance change versus concentration. The linear equation of serum with Aβ1-42 is given by Y = 31450.3 X + 45775.8 with error R2 = 0.96569. The range of linear detection is occurred from 1 ng/ml to 1 pg/ml in serum with Aβ1-40 and serum with Aβ1-42.
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Zimmermann, Rüdiger. "Der Stellenwert der beta-Amyloid-Quotienten A-beta-x-42/A-beta-x-40 und A-beta-1-42/A-beta-x-40 für die neurochemische Demenzdiagnostik /." 2008. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=016803396&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Tran, Denise Phuong. "Biological and structure characterisation of eukaryotic prefoldin." Thesis, 2018. http://hdl.handle.net/2440/115168.

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Prefoldin is a hexameric protein complex ubiquitously expressed and found to influence the conformation of amyloidogenic peptides. Relatively high degrees of sequence identity and conservation across evolutionary lineages are observed, however differences in binding abilities have been noted between the homologs. This thesis describes work examining the structure of eukaryotic prefoldin and its biological activities with respect to interaction with amyloid β. The structure and biological activities of prefoldin’s individual subunits are also explored. Although many studies have investigated the structure of prokaryotic prefoldin, there is limited information available for eukaryotic prefoldin. Two-dimensional ¹H-¹H and ¹H-¹³C nuclear magnetic resonance (NMR) spectroscopy was utilised to probe the structure of both α and β human prefoldin subunits. The data revealed the highly alpha helical secondary structure of the subunits, which was further verified through far-UV circular dichroism. Further thermal aggregation assays utilising this technique have demonstrated the stability of the prefoldin subunits. The biological effect of prefoldin on the amyloid fibril formation of the Alzheimer’s disease related amyloid β peptide was investigated using a combination of dye-binding assays and cytotoxicity assays. The presence and absence of fibrils was confirmed by transmission electron microscopy. In terms of fibril formation, prefoldin and its subunits prevented in vitro conversion of the amyloid β peptide to amyloid fibrils. In some cases, total inhibition of fibril formation occurred and a 3-(4,5- dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay was conducted on the resultant products. The product was incubated with healthy PC-12 cells and induced cellular death, therefore establishing the cytotoxicity of the resultant oligomeric amyloid β form. Previous investigations into the binding capabilities of prokaryotic prefoldin identified the distal tips as an important structural aspect, interacting with the amyloidogenic peptide. The binding interface of prefoldin subunits 5 and 6 with amyloid β was probed using chemical cross-linking (CXL) experiments. Traditional methods to identify cross-linked peptides are challenging and the results are often ambiguous. In this study, CXL products were analysed by liquid chromatography-ion mobility-mass spectrometry (LC-IM-MS) to investigate the utility of IM in enhancing the CXL analytical workflow. The orthogonal separation of ion mobility enabled the identification of the cross-linked amino acids. The distal end of prefoldin subunit 5 was found to interact with the Nterminus of the amyloid peptide, whereas prefoldin subunit 6 was identified to interact with the peptide in the middle of its sequence. Ion mobility-mass spectrometry (IM-MS) analysis of the eukaryotic prefoldin complex identified the collisional cross section of the intact hexamer. Solution disruption experiments of the intact complex revealed the disengaging sub-complexes, and information on the intersubunit contacts and relative interfacial strengths were obtained. A capillary temperature controller (CTC) was developed to observe the thermal dissociation of the complex using nano-electrospray IM-MS. The combination of these results confirmed a structural aspect common to both mammalian prefoldin and prokaryotic prefoldin, despite the primary sequence differences. The biological assays revealed the ability of prefoldin to prevent the aggregation and amyloid fibril formation of amyloid β, and low resolution MS techniques were able to postulate the arrangement of the subunits and the possible interface interactions of the hexameric complex with the amyloidogenic peptide. This thesis has therefore provided an in-depth investigation of the structural characteristics of eukaryotic prefoldin and its chaperoning capability, therefore implicating a potential role for prefoldin in modulating protein misfolding and aggregation.
Thesis (Ph.D.) -- University of Adelaide, School of Physical Sciences, 2018
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Gloeckner, Sara Friederike. "Transthyretin-, Aß 1-40- und Aß 1-42- und Tau-Protein-Konzentrationen im Liquor cerebrospinalis bei demenziellen Erkrankungen." Doctoral thesis, 2010. http://hdl.handle.net/11858/00-1735-0000-0006-AFE5-D.

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Book chapters on the topic "Amyloid beta (1-40)"

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Alper, Benjamin J., and Walter K. Schmidt. "Evaluating Amyloid Beta (Aβ) 1-40 Degradation by Capillary Electrophoresis." In Capillary Electrophoresis of Biomolecules, 263–73. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-296-4_19.

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Durieux, J. P., F. Dick, M. Schwaller, G. Haas, U. Wixmerten, S. Mundwiler, and R. Nyfeler. "Synthesis of beta amyloid protein [1-40] scope and limitations of convergent solid phase synthesis." In Peptides, 34–36. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_4.

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Attems, J., F. Lintner, and K. A. Jellinger. "Distribution of Amyloid Peptide Beta 1-40 and 1-42 in Cerebral Amyloid Angiopathy and Correlation with Alzheimer Disease Pathology." In Amyloid and Amyloidosis, 393–95. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494-140.

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Attems, J., K. Jellinger, and F. Lintner. "Distribution of Amyloid Peptide Beta 1-40 and 1-42 in Cerebral Amyloid Angiopathy and Correlation with Alzheimer Disease Pathology." In Amyloid and Amyloidosis, 393–95. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494.ch135.

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Conference papers on the topic "Amyloid beta (1-40)"

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Mendonça, Pedro Henrique Carvalho Furtado de, Fernanda Rabello Detoni, Letícia Silva Brandão dos Santos, Talita Cardoso Gomes, and Ivan Magalhães Viana. "Monoclonal antibodies in the treatment of Alzheimer’s disease: a literature review." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.597.

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Background: Alzheimer’s disease (AD) is a neurodegenerative disorder, whose treatment is limited to drugs that offer comfort to the patient. Immunotherapy with monoclonal antibodies (mAbs) has been the subject of a study with the promise of reversing cognitive deficits. In this scenario, we conducted a systematic review to elucidate aspects about the effectiveness of such treatment. Objectives: Analyze the prognostic of patients with AD through immunotherapy using anti-amilody mAbs. Methods: It was used the PubMed database using the descriptors: “Amyloid beta-Peptides AND Alzheimer disease AND Immunotherapy”. Filters: clinical trial, randomized controlled trial. 6 articles from 2015 to 2021 were selected. Inclusion criteria: (1) mAbs as treatment for AD; (2) Analyze the prognostic. Results: The immunotherapy with bapineuzumab and solanezumab didn’t showed no statistically significant difference between the groups of bapineuzumab 0,5 mg / kg (p = 0,979) and placebo (p = 0,973) and a change of 6.65 in the solanezumab group and 7.44 in the placebo group (difference, −0.80; P = 0 , 10). However, subcutaneous treatment of bapineuzumab exhibited fewer abnormalities of images related to amyloid with edema or effusion (AIRA), so, better tolerated compared to intravenous treatment. In the study with the ABvac40 vaccine, about 92% of the individuals in the test group developed specific anti-Aβ 40 antibodies. Conclusion: Bapineuzumab and solanezumab didn’t achieve significant results in the reduction of cognitive decline, however bapineuzumab enabled the prevention of Aβ aggregation. However, the use of mAbs can trigger collateral effects, requiring an individual analysis.
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