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一种用于大脑尺度上淀粉样蛋白动态变化及阿尔茨海默病治疗的网络聚合模型。

A network aggregation model for amyloid- dynamics and treatment of Alzheimer's diseases at the brain scale.

作者信息

Brennan Georgia S, Goriely Alain

机构信息

Mathematical Institute, University of Oxford, Andrew Wiles Building, Woodstock Rd, Oxford, OX2 6GG, UK.

出版信息

J Math Biol. 2025 Feb 1;90(2):22. doi: 10.1007/s00285-024-02179-5.

DOI:10.1007/s00285-024-02179-5
PMID:39891738
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11787187/
Abstract

Neurodegenerative diseases are associated with the assembly of specific proteins into oligomers and fibrillar aggregates. At the brain scale, these protein assemblies can diffuse through the brain and seed other regions, creating an autocatalytic protein progression. The growth and transport of these assemblies depend on various mechanisms that can be targeted therapeutically. Here, we use spatially-extended nucleation-aggregation-fragmentation models for the dynamics of prion-like neurodegenerative protein-spreading in the brain to study the effect of different drugs on whole-brain Alzheimer's disease progression.

摘要

神经退行性疾病与特定蛋白质组装成寡聚体和纤维状聚集体有关。在大脑层面，这些蛋白质聚集体可在大脑中扩散并播种到其他区域，形成自催化的蛋白质进展。这些聚集体的生长和运输取决于多种可用于治疗靶向的机制。在这里，我们使用空间扩展的成核 - 聚集 - 碎片化模型来研究大脑中朊病毒样神经退行性蛋白质传播的动力学，以探讨不同药物对全脑阿尔茨海默病进展的影响。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/7217547e2f82/285_2024_2179_Fig17_HTML.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/a902e3c78deb/285_2024_2179_Fig1_HTML.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/59b5abf941c1/285_2024_2179_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/fb3385e47c8f/285_2024_2179_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/8f6aaefc63c0/285_2024_2179_Fig10_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/7a09ab6ba97f/285_2024_2179_Fig11_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/270c82002315/285_2024_2179_Fig12_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/e21d1133aa92/285_2024_2179_Fig13_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/4ea91ce95ef6/285_2024_2179_Fig14_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/4b3574231b99/285_2024_2179_Fig15_HTML.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4829/11787187/7217547e2f82/285_2024_2179_Fig17_HTML.jpg

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Alzheimers Dement. 2023 Jun;19(6):2287-2297. doi: 10.1002/alz.12877. Epub 2022 Dec 1.
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Lecanemab, Aducanumab, and Gantenerumab - Binding Profiles to Different Forms of Amyloid-Beta Might Explain Efficacy and Side Effects in Clinical Trials for Alzheimer's Disease.仑卡奈单抗、阿杜卡玛单抗和加内替单抗——对不同形式的淀粉样蛋白-β的结合谱可能解释了阿尔茨海默病临床试验中的疗效和副作用。
Neurotherapeutics. 2023 Jan;20(1):195-206. doi: 10.1007/s13311-022-01308-6. Epub 2022 Oct 17.
3
Amyloid-Related Imaging Abnormalities With Anti-amyloid Antibodies for the Treatment of Dementia Due to Alzheimer's Disease.
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Front Neurol. 2022 Mar 23;13:862369. doi: 10.3389/fneur.2022.862369. eCollection 2022.
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The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics.阿尔茨海默病中的淀粉样蛋白假说：新疗法的新见解。
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