Legal but lethal: functional protein aggregation at the verge of toxicity.
Legal but lethal: functional protein aggregation at the verge of toxicity.
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DOI：
10.3389/fncel.2015.00045
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发表时间：
2015
影响因子：
5.3
通讯作者：
Falsone SF
中科院分区：
文献类型：
--
作者：
Falsone A;Falsone SF
许多神经退行性疾病与不可逆的蛋白质聚集有关，这一过程通常伴随着毒性和严重的细胞损伤。然而，蛋白质聚集也可以用于生理目的，正如朊病毒所显示的那样。虽然该蛋白家族的聚集最初被认为只对哺乳动物有害，但现在几乎可以清楚地看到，许多其他蛋白质采用类似朊病毒的属性，合理地聚合成具有有组织生理作用的高阶复合物。这意味着细胞至少可以在某种程度上容忍固有危险的蛋白质聚集体的积累，以获得功能性利益。这篇综述总结了目前已知的生物采取的策略，以保持有益的聚集，并防止有毒聚集体的灾难性积累，经常伴随神经变性。
Many neurodegenerative disorders are linked to irreversible protein aggregation, a process that usually comes along with toxicity and serious cellular damage. However, it is emerging that protein aggregation can also serve for physiological purposes, as impressively shown for prions. While the aggregation of this protein family was initially considered exclusively toxic in mammalians organisms, it is now almost clear that many other proteins adopt prion-like attributes to rationally polymerize into higher order complexes with organized physiologic roles. This implies that cells can tolerate at least in some measure the accumulation of inherently dangerous protein aggregates for functional profit. This review summarizes currently known strategies that living organisms adopt to preserve beneficial aggregation, and to prevent the catastrophic accumulation of toxic aggregates that frequently accompany neurodegeneration.
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影响因子：
3.7
作者：
Acosta JR;Goldsbury C;Winnick C;Badrock AP;Fraser ST;Laird AS;Hall TE;Don EK;Fifita JA;Blair IP;Nicholson GA;Cole NJ
通讯作者：
Cole NJ
影响因子：
7.5
作者：
Dundr, Miroslav
通讯作者：
Dundr, Miroslav
影响因子：
15.1
作者：
Baron DM;Kaushansky LJ;Ward CL;Sama RR;Chian RJ;Boggio KJ;Quaresma AJ;Nickerson JA;Bosco DA
通讯作者：
Bosco DA
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5.6
作者：
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通讯作者：
Jackson, Sophie E.
内源性TDP-43而不是FUS，通过G3BP导致应力颗粒组件。
影响因子：
15.1
作者：
Aulas A;Stabile S;Vande Velde C
通讯作者：
Vande Velde C