中国神经再生研究(英文版) ›› 2019, Vol. 14 ›› Issue (11): 1897-1898.doi: 10.4103/1673-5374.259608

• 观点:退行性病与再生 • 上一篇    下一篇

诱导α-突触核蛋白压缩:一种抑制α-突触核蛋白聚集的新策略?

  

  • 出版日期:2019-11-15 发布日期:2019-11-15

Inducing α-synuclein compaction: a new strategy for inhibiting α-synuclein aggregation?

Francisca Pinheiro 1, 2, Salvador Ventura 1, 2   

  1. 1 Institut de Biotecnologia i Biomedicina, Universitat Autonoma de Barcelona, Bellaterra, Spain;
    2 Departament de Bioquimica i Biologia Molecular, Universitat Autonoma de Barcelona, Bellaterra, Spain
  • Online:2019-11-15 Published:2019-11-15
  • Contact: Salvador Ventura, PhD, salvador.ventura@uab.es.

摘要:

orcid: 0000-0002-9652-6351 (Salvador Ventura)

Abstract:

Proteins might misfold during translation and folding or even once they are in their native states, due to stochastic fluctuations, destabilizing mutations or cellular stress. Aberrant protein species are usually detected and either refolded or cleared by the protein quality control machinery . When misfolded protein conformers cannot be degraded, they tend to self-assemble to form aggregates, a characteristic of many neurodegenerative diseases.