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Relevant bibliographies by topics / Amyloid-beta peptide (A-beta)

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Academic literature on the topic 'Amyloid-beta peptide (A-beta)'

Author: Grafiati

Published: 9 March 2023

Last updated: 19 July 2025

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Journal articles on the topic "Amyloid-beta peptide (A-beta)"

1

Muhammad, Jehangir, Wang Xiaohui, Zhao Ye, Ali Umar, kasmiri Kashif, and cheng Wang. "Inhibition of amyloid beta oligomer, fibrils, and peptide using nanoparticles to disrupt Alzheimer's pathogenesis." World Journal of Advanced Research and Reviews 23, no. 2 (2024): 343–57. https://doi.org/10.5281/zenodo.14836935.

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The Aβ peptide, which is connected to the development of Alzheimer's disease, forms highly neurotoxic prefibrillar oligomeric aggregates, which are challenging to study due to their fleeting, low prevalence, and diverse nature. These aggregates are considered to play a role in the pathogenesis of numerous neurodegenerative diseases. The potential approach of blocking or disrupting the buildup of amyloid peptides, particularly amyloid-β (AβOs), by using nanoparticles that specifically bind or prevent their aggregation to develop new medications and treatments for Alzheimer's dise

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Buneeva, O. A., O. V. Gnedenko, M. V. Medvedeva, A. S. Ivanov, and A. E. Medvedev. "The effect of neuroprotector isatin on binding of some model proteins with beta-amyloid peptide: a biosensor study." Biomeditsinskaya Khimiya 62, no. 6 (2016): 720–24. http://dx.doi.org/10.18097/pbmc20166206720.

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The amyloid-beta peptide 1-42 formed during proteolytic processing of the amyloid precursor protein (APP) plays a key role in the development or progression of Alzheimer's disease (AD) and other pathologies associated with formation of protein aggregates in the central nervous system. Recent proteomic profiling of mouse and rat brain preparations by means of beta-amyloid peptide immobilized on Affigel-10 revealed a large group of amyloid-binding proteins (n>80). Many (about 25%) of these proteins were previously identified as isatin-binding proteins. The aim of this study was to validate di

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Aloufi, Bandar. "Molecular dynamics simulation analysis of the beta amyloid peptide with docked inhibitors." Bioinformation 18, no. 7 (2022): 622–29. http://dx.doi.org/10.6026/97320630018622.

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Beta amyloid peptide is widely studied due to its association with Alzheimer disease (AD). Various study reported that the accumulation of beta amyloid in brain cells leads to Alzheimer disease. Hence, Beta amyloid peptide could be a potential target of anti-AD therapy. Hence, it is of interest to develop potent inhibitors for Beta amyloid peptide in the context of Alzheimer disease (AD). We report the binding features of Ascorbic acid, Cysteine, Dithioerythriol, Dithiothreitol, Malic acid and α-Tocopherol with beta amyloid having binding energy values of -6.7, -6.5, -6.0, -6.5, -6.7 and - 7.0

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Uéda, K., H. Fukushima, E. Masliah, et al. "Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease." Proceedings of the National Academy of Sciences 90, no. 23 (1993): 11282–86. http://dx.doi.org/10.1073/pnas.90.23.11282.

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A neuropathological hallmark of Alzheimer disease (AD) is a widespread amyloid deposition. We analyzed the entire amino acid sequences in an amyloid preparation and found, in addition to the major beta/A4-protein (A beta) fragment, two unknown peptides. We raised antibodies against synthetic peptides using subsequences of these peptides. These antibodies immunostained amyloid in neuritic and diffuse plaques as well as vascular amyloid. Electron microscopic analysis demonstrated that the immunostaining was localized on amyloid fibrils. We have isolated an apparently full-length cDNA encoding a

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Jiang, H., D. Burdick, C. G. Glabe, C. W. Cotman, and A. J. Tenner. "beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain." Journal of Immunology 152, no. 10 (1994): 5050–59. http://dx.doi.org/10.4049/jimmunol.152.10.5050.

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Abstract beta-amyloid peptides that accumulate within the brain of individuals with Alzheimer's disease bind to C1q and activate the classical C pathway via a specific interaction with a site within the collagen-like domain of C1q (C1q-CLF). Synthetic analogues of beta-amyloid peptides, beta 1-42 and beta 1-40, bound to C1q and were strong activators of C as assessed by both total C consumption and C4 consumption. beta 1-42 was significantly more effective than beta 1-40 in binding to C1q and triggering C activation, whereas beta 1-28 demonstrated little or no binding or C activation. This C-a

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6

Muhammad Jehangir, Xiaohui Wang, Ye Zhao, Umar Ali, Kashif kasmiri, and Wang cheng. "Inhibition of amyloid beta oligomer, fibrils, and peptide using nanoparticles to disrupt Alzheimer's pathogenesis." World Journal of Advanced Research and Reviews 23, no. 2 (2024): 343–57. http://dx.doi.org/10.30574/wjarr.2024.23.2.2349.

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The Aβ peptide, which is connected to the development of Alzheimer's disease, forms highly neurotoxic prefibrillar oligomeric aggregates, which are challenging to study due to their fleeting, low prevalence, and diverse nature. These aggregates are considered to play a role in the pathogenesis of numerous neurodegenerative diseases. The potential approach of blocking or disrupting the buildup of amyloid peptides, particularly amyloid-β (AβOs), by using nanoparticles that specifically bind or prevent their aggregation to develop new medications and treatments for Alzheimer's disease (AD) could

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7

Klunk, W. E., J. W. Pettegrew, and D. J. Abraham. "Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation." Journal of Histochemistry & Cytochemistry 37, no. 8 (1989): 1273–81. http://dx.doi.org/10.1177/37.8.2666510.

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The binding of Congo red to several purified amyloid-like peptides having a beta-pleated sheet conformation was quantitatively examined. Congo red binds preferentially to the beta-pleated sheet conformation of both insulin fibrils and poly-L-lysine. Congo red does not bind nearly so well to poly-L-serine or polyglycine, despite the fact that these peptides also have a beta-pleated sheet conformation. Binding to insulin fibrils was saturable with an apparent Bmax of 2 moles of Congo red per mole of insulin fibrils and an apparent KD of 1.75 x 10(-7) M. Binding to beta-poly-L-lysine was similar

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Agaeva, G., and G. Najafova. "ELECTRONIC PARAMETERS OF CONFORMATIONAL STATES OF ABETA-AMYLOID PEPTIDE (25-35)." Russian Journal of Biological Physics and Chemisrty 8, no. 1 (2024): 21–26. http://dx.doi.org/10.29039/rusjbpc.2023.0583.

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The electronic characteristics of stable conformational states of beta-amyloid peptide (25-35) have been studied by molecular modeling methods. Beta-amyloid peptide (Aβ) is the main component of senile plaques found in the brains of patients with Alzheimer's disease. Aβ (25-35) fragment of a molecule with the amino acid sequence Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met. It has been shown that the conformational features of a molecule are largely determined by its environment; therefore, the aim of this work was to study the differences in the conformations of amyloid beta-peptide (25-35) in

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Jensen, P. H., E. S. Sørensen, T. E. Petersen, J. Gliemann та L. K. Rasmussen. "Residues in the synuclein consensus motif of the α-synuclein fragment, NAC, participate in transglutaminase-catalysed cross-linking to Alzheimer-disease amyloid βA4 peptide". Biochemical Journal 310, № 1 (1995): 91–94. http://dx.doi.org/10.1042/bj3100091.

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The widespread deposition of amyloid plaques is one of the hallmarks of Alzheimer disease (AD). A recently described component of amyloid plaques is the 35-residue peptide, non-A beta component of AD amyloid, which is derived from a larger intracellular neuronal constituent, alpha-synuclein. We demonstrate that transglutaminase catalyses the formation of the covalent non-A beta component of AD amyloid polymers in vitro as well as polymers with beta-amyloid peptide, the major constituent of AD plaques. The transglutaminase-reactive amino acid residues in the non-A beta component of AD amyloid w

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Ghiso, J., E. Matsubara, A. Koudinov та ін. "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 (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 peptide (A-beta)"

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Han, Wei. "Development of a coarse-grained protein model and molecular dynamics studies of amyloid-[beta] peptide aggregation /." View abstract or full-text, 2007. http://library.ust.hk/cgi/db/thesis.pl?CHEM%202007%20HAN.

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Han, Fang. "AMYLOID A-BETA PEPTIDE: IN-CELL STUDIES AND MECHANISM OF POLYPHENOL-BASED INHIBITION TO AGGREGATION." Case Western Reserve University School of Graduate Studies / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=case1404771350.

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Shirwany, Najeeb A. "Neurotoxicity induced by A[beta] 40 and A[beta] 42 in transgenic mouse models of Alzheimer's disease." Oklahoma City : [s.n.], 2009.

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Gulisano, Walter. "A renewed vision for Amyloid beta and tau in Alzheimer s disease pathophysiology." Doctoral thesis, Università di Catania, 2018. http://hdl.handle.net/10761/4152.

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The aim of this thesis was to study the pathogenetic mechanisms underlying Alzheimer s disease (AD), a neurodegenerative disorder affecting the elderly and characterized by memory loss, personality changes and cognitive dysfunction leading to dementia. I will discuss the main projects in which I participated aimed at understanding the role of the main molecular interactors involved in AD pathogenesis, i.e. Amyloid-beta peptide and tau protein, on hippocampal synaptic plasticity and memory in animal models. After reviewing the pathophysiological models that have been developed so far, our gener

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Beckett, Christina. "VARIANCE OF THE AMYLOID BETA PEPTIDE AS A METRIC FOR THE DIAGNOSIS OF ALZHEIMER'S DISEASE." UKnowledge, 2016. http://uknowledge.uky.edu/medsci_etds/6.

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Alzheimer’s disease (AD) is the most prevalent neurodegenerative disorder associated with aging. AD is by far the best understood and most studied neurodegenerative disease. Substantial advances have been made over the last decade, however it is debatable how much closer we are to a clinically useful therapy. A long standing goal in the AD field has been to improve the accuracy of early detection, with the assumption that the ability to intervene earlier in the disease process will lead to a better clinical outcome. Major facets of this effort have been the continued development and improvemen

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Luheshi, Leila Mohamed. "Mutational analysis of the aggregation and toxicity of the amyloid beta peptide in a Drosophila model of Alzheimer's Disease." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612965.

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Hilt, Silvia. "Spin Labeled Fluorene Compounds are a Versatile Sword in the Fight Against Amyloid Beta Peptide of Alzheimer's Disease." Thesis, University of California, Davis, 2016. http://pqdtopen.proquest.com/#viewpdf?dispub=10182862.

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<p> Amyloid-β (Aβ) peptide is generated after sequential cleavage of the constitutively expressed amyloid precursor protein (APP) by γ and β secretases, and is recognized as the primary causative agent underlying the neuropathogenesis of Alzheimer’sDisease (AD). Once generated, monomeric Aβ demonstrates a high propensity to aggregate into toxic Aβ oligomers (AβO) of various sizes, which eventually accumulate in the brain in the form of amyloid plaques. Mutations in either the gene for APP or one or both of its processing genes, presenilin-1 (PS1) and p

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Jana, A. K. "Modulation of the intrinsic properties of alzheimer’s amyloid beta peptide with nanosurfaces and chemical modifications: a computational approach." Thesis(Ph.D.), CSIR-National Chemical Laboratory, Pune, 2016. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/2083.

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Ameen, Muhammad T., and Patrick C. Bradshaw. "VITAMIN B2 REDUCES AMYLOID-BETA PROTEOTOXICITY AND IMPROVES HEALTH IN A CAENORHABDITIS ELEGANS ALZHEIMER’S DISEASE MODEL." Digital Commons @ East Tennessee State University, 2018. https://dc.etsu.edu/asrf/2018/schedule/24.

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Alzheimer’s disease (AD) is a neurodegenerative disease and the most common form of dementia associated with amyloid-beta peptide deposition and loss of mitochondrial function and regulation. Currently, there is no cure for AD, thus, there is a need to continuously develop therapeutic strategies that could address the complex multifactorial causes of AD development. Due to this necessity, this study has investigated the role of vitamin B2 as a disease modifying drug for AD by employingamyloid-beta and mitochondrial based AD therapeutic strategies. Using a transgenic C. elegans AD worm model ex

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Ameen, Muhammad Tukur. "A Role of Vitamin B2 in Reducing Amyloid-beta Toxicity in a Caenorhabditis elegans Alzheimer’s Disease Model." Digital Commons @ East Tennessee State University, 2018. https://dc.etsu.edu/etd/3398.

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Alzheimer’s disease (AD) is associated with amyloid-beta peptide deposition and loss of mitochondrial function. Using a transgenic C. elegans AD worm model expressing amyloid-beta in body wall muscle, we determined that supplementation with either of the forms of vitamin B2, flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) protected against amyloid-beta mediated paralysis. FMN and FAD were then assayed to determine effects on ATP, oxygen consumption, and reactive oxygen species (ROS) with these compounds not significantly improving any of these mitochondrial bioenergetic functi

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Books on the topic "Amyloid-beta peptide (A-beta)"

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Alzheimer amyloid-[beta] peptide aggregation: A potential in vivo model of ealry aggregate formation. National Library of Canada, 2002.

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2

Abeta Peptide and Alzheimer's Disease: Celebrating a Century of Research. Springer, 2006.

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Saido, Takaomi. A-Beta Metabolism and Alzheimer's Disease. Landes Bioscience, 2003.

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4

Safar, Jiri G. Prion Paradigm of Human Neurodegenerative Diseases Caused by Protein Misfolding. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0005.

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Data accumulated from different laboratories argue that a growing number of proteins causing neurodegeneration share certain characteristics with prions. Prion-like particles were produced from synthetic amyloid beta (Aβ‎) peptides of Alzheimer’s disease (AD), from recombinant α‎-synuclein linked to Parkinson’s disease (PD), and from recombinant tau associated with frontotemporal dementias (FTD). Evidence from human prions reveals that variable disease phenotypes, rates of propagation, and targeting of different brain structures are determined by distinct conformers (strains) of pathogenic pri

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Book chapters on the topic "Amyloid-beta peptide (A-beta)"

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Lin, Meng-chin, Tajib Mirzabekov, and Bruce Kagan. "Channel Formation by a Neurotoxic Beta Amyloid Peptide, Aβ25–35." In Neurodegenerative Diseases. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-0209-2_39.

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Behl, Christian. "Getting to the Bottom of It: Amyloid Beta Peptide Is Derived from a Larger Precursor." In Alzheimer’s Disease Research. Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-31570-1_8.

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Lahiri, Debomoy K., and Martin R. Farlow. "Tacrine Reduces the Secretion of Soluble Amyloid Beta-Peptides in a Neuroblastoma Cell Line." In Advances in Behavioral Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5337-3_80.

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Kondela, Tomáš, Pavol Hrubovčák, Dmitry Soloviov, et al. "Approaches for a Closer Look at Problems of Liquid Membranes with Amyloid-Beta Peptides." In Springer Proceedings in Physics. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-80924-9_10.

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Anand, Abhinav, Neha Sharma, Monica Gulati, and Navneet Khurana. "Amyloid Beta." In Research Anthology on Diagnosing and Treating Neurocognitive Disorders. 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. 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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Puzzo Daniela and Arancio Ottavio. "Amyloid-β Peptide: Dr. Jekyll or Mr. Hyde?" In Advances in Alzheimer’s Disease. IOS Press, 2013. https://doi.org/10.3233/978-1-61499-154-0-111.

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Amyloid-&beta; peptide (A&beta;) is considered a key protein in the pathogenesis of Alzheimer's disease (AD) because of its neurotoxicity and capacity to form characteristic insoluble deposits known as senile plaques. A&beta; derives from amyloid-&beta; protein precursor (A&beta;PP), whose proteolytic processing generates several fragments including A&beta; peptides of various lengths. The normal function of A&beta;PP and its fragments remains poorly understood. While some fragments have been suggested to have a function in normal physiological cellular processes, A&beta; has been widely considered as a &ldquo;garbage&rdquo; fragment that becomes toxic when it accumulates in the brain, resulting in impaired synaptic function and memory. A&beta; is produced and released physiologically in the healthy brain during neuronal activity. In the last 10 years, we have been investigating whether A&beta; plays a physiological role in the brain. We first demonstrated that picomolar concentrations of a human A&beta;42preparation enhanced synaptic plasticity and memory in mice. Next, we investigated the role of endogenous A&beta; in healthy murine brains and found that treatment with a specific antirodent A&beta; antibody and an siRNA against murine A&beta;PP impaired synaptic plasticity and memory. The concurrent addition of human A&beta;42rescued these deficits, suggesting that in the healthy brain, physiological A&beta; concentrations are necessary for normal synaptic plasticity and memory to occur. Furthermore, the effect of both exogenous and endogenous A&beta; was seen to be mediated by modulation of neurotransmitter release and &alpha;7-nicotinic receptors. These findings need to be taken into consideration when designing novel therapeutic strategies for AD.

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Prasanthi R.P. Jaya, Marwarha Gurdeep, and Ghribi Othman. "The Cholesterol-Fed Rabbit as a Model System for Cholesterol-Alzheimer's Disease Studies." In Advances in Alzheimer’s Disease. IOS Press, 2011. https://doi.org/10.3233/978-1-60750-733-8-163.

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Epidemiological, animal, and cellular studies suggest that abnormalities in cholesterol metabolism are a risk factor for Alzheimer's disease (AD), potentially by increasing amyloid-&beta; (A&beta;) peptide levels. Accumulation of A&beta; in the brain is suggested to play a key role in the neurodegenerative processes by triggering the hyperphosphorylation of tau and the neuronal death that develop in the course of AD. However, the mechanisms by which cholesterol increases A&beta; levels are still ill-defined. Work from our laboratory using the cholesterol-fed rabbit model system indicates that hypercholesterolemia increases A&beta; through multiple mechanisms that affect production, degradation and clearance of this peptide. We also have found that the oxidized cholesterol metabolite, 27-hydroxycholesterol, also increases A&beta; levels in organotypic slices from rabbit hippocampus. Our results suggest that multiple signaling pathways are involved in hypercholesterolemia-induced AD pathology and suggest 27-hydroxycholesterol as the link between circulating cholesterol and AD-like pathology in the brain.

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Nguyen Phuong H., del Castillo-Frias Maria P., Berthoumieux Olivia, Faller Peter, Doig Andrew J., and Derreumaux Philippe. "Amyloid-β/Drug Interactions from Computer Simulations and Cell-Based Assays." In Advances in Alzheimer’s Disease. IOS Press, 2018. https://doi.org/10.3233/978-1-61499-876-1-657.

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Targeting the early oligomers formed by the amyloid-&beta; (A&beta;) peptide of 40 and 42 amino acids is considered one promising therapeutic approach for Alzheimer's disease (AD). In vitro experiments and computer simulations are often used in synergy to reveal the modes of interactions of drugs. In this account, we present our contribution to understanding how small molecules bind to A&beta;40/A&beta;42peptides, based either on extensive coarse-grained and all-atom simulations, or a variety of experimental techniques. We conclude by offering several perspectives on the future of this field to design more efficient drugs.

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Wilcock Donna M. and Colton Carol A. "Anti-Amyloid-β Immunotherapy in Alzheimer's Disease: Relevance of Transgenic Mouse Studies to Clinical Trials." In Advances in Alzheimer’s Disease. IOS Press, 2011. https://doi.org/10.3233/978-1-60750-733-8-247.

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Therapeutic approaches to the treatment of Alzheimer's disease are focused primarily on the amyloid-&beta; peptide which aggregates to form amyloid deposits in the brain. The amyloid hypothesis states that amyloid is the precipitating factor that results in the other pathologies of Alzheimer's disease. One such therapy that has attracted significant attention is anti-amyloid-&beta; immunotherapy. First described in 1999, immunotherapy uses anti-amyloid-&beta; antibodies to lower brain amyloid levels. Active and passive immunization were shown to lower brain amyloid levels and improve cognition in multiple transgenic mouse models. Mechanisms of action were studied in these mice and revealed a complex set of mechanisms that depended on the type of antibody used. When active immunization advanced to clinical trials a subset of patients developed meningoencephalitis, an event not predicted in mouse studies. It was suspected that a T-cell response due to the type of adjuvant used was the cause. Passive immunization has also advanced to Phase III clinical trials on the basis of successful transgenic mouse studies. Reports from the active immunization clinical trial indicated that, similarly to effects observed in mouse studies, amyloid levels in brain were reduced.

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Conference papers on the topic "Amyloid-beta peptide (A-beta)"

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Gonçalves, Brenda, Isadora Ribeiro, Thamires Magalhães, et al. "NEUROPSYCHOLOGICAL TESTS AS PREDICTORS OF CONVERSION TO ALZHEIMER’S DISEASE IN BETA-AMYLOID POSITIVE INDIVIDUALS." In XIII Meeting of Researchers on Alzheimer's Disease and Related Disorders. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1980-5764.rpda007.

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Background: amnestic Mild Cognitive Impairment (aMCI) refers to a possibletransitional stage between healthy aging and dementia and has an increased chance of converting to Alzheimer’s disease (AD). Objectives: to assess whether neuropsychological tests can predict the conversion to AD in patients with aMCI and altered CSF amyloid peptide (βA+). Methods: 48 individuals underwent neuropsychological assessment (time 0 and time 1), being 18 healthy controls and 30 aMCI βA+, who performed a single CSF collection (time 0). All subjects with aMCI scored 0.5 in the Memory category of the Clinical Dem

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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

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