Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein

To better understand the specific cascade of protein interactions that lead to the pathological aggregation of α-synuclein (wild-type and mutant forms), Leitão et al. present a method to measure interactions of monomeric, oligomeric, and fibrillar forms of α-syn with 65 proteins that were previously...

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Autores principales: André D. G. Leitão, Paulina Rudolffi-Soto, Alexandre Chappard, Akshay Bhumkar, Derrick Lau, Dominic J. B. Hunter, Yann Gambin, Emma Sierecki
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/aca601966a214f07a960669aebb2ca79
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Sumario:To better understand the specific cascade of protein interactions that lead to the pathological aggregation of α-synuclein (wild-type and mutant forms), Leitão et al. present a method to measure interactions of monomeric, oligomeric, and fibrillar forms of α-syn with 65 proteins that were previously shown to be components of Lewy bodies. This approach is useful to understand the sequence of protein-binding events that lead to α-syn aggregation.