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Updated: Jun 28, 2025

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14-3-3τ作为早期α-Synuclein多元化和粉样蛋白形成的调节器

Gobert Heesink1, Maxime C M van den Oetelaar2, Slav A Semerdzhiev1

  • 1Nanobiophysics, Faculty of Science and Technology, MESA + Institute for Nanotechnology and Technical Medical Centre, University of Twente, Enschede 7500 AE, The Netherlands.

ACS chemical neuroscience
|April 18, 2024
PubMed
概括

蛋白14-3-3τ延迟了α-synuclein聚合,这是帕金森病的一个关键因素. 它形成混合的多分子,防止有毒的粉样蛋白的形成,并为帕金森病提供新的治疗点.

关键词:
14-3-3的陪伴者是一个伴侣.在IDP的多元化过程中.多元化的调制.蛋白质共冷凝的共冷凝过程蛋白质与蛋白质的相互作用在α-synuclein聚合过程中.

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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