The amyloid state of proteins in human diseases.

The amyloid state of proteins in human diseases.
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DOI:
10.1016/j.cell.2012.02.022
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发表时间:
2012-03-16
期刊:
影响因子:
64.5
通讯作者:
Jucker M
Jucker M
中科院分区:
生物学1区
文献类型:
--
作者:
Eisenberg D;Jucker M

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淀粉样纤维和寡聚体与包括阿尔茨海默病和朊病毒病症在内的多种人类疾病相关。在这里,我们试图将淀粉样蛋白质分子特性的最新发现与病理组织和疾病状态的观察联系起来。我们总结了淀粉样蛋白的结构和成核的研究,并将其与淀粉样蛋白多态性、朊病毒株、组织中致病蛋白的共聚集以及毒性和传播性机制的观察结果联系起来。分子研究也导致了许多针对淀粉样疾病的生物和化学干预策略。
Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer’s disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, co-aggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases.
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