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Simultaneous IR-Spectroscopic Observation of α-Synuclein, Lipids, and Solvent Reveals an Alternative Membrane-Induced Oligomerization Pathway
ChemBioChem ( IF 2.6 ) Pub Date : 2017-11-02 02:35:53 , DOI: 10.1002/cbic.201700355
Mohammad A. Fallah 1 , Hanne R. Gerding 2 , Christian Scheibe 1 , Malte Drescher 1 , Christiaan Karreman 2 , Stefan Schildknecht 2 , Marcel Leist 2 , Karin Hauser 1
Affiliation  

Aggregation of Parkinson's-associated proteins: The presence of a membrane changes the oligomerization pathway of Parkinson's-associated intrinsically disordered protein (IDP) α-synuclein from that observed in solution. Membrane remodeling and disruption are caused not by the final aggregates, but by specific membrane–aggregate interaction.

中文翻译:

α-突触核蛋白,脂质和溶剂的同时红外光谱观察揭示了一种膜诱导的低聚途径。

帕金森氏相关蛋白的聚集:膜的存在改变了溶液中观察到的帕金森氏相关内在无序蛋白(IDP)α-突触核蛋白的寡聚途径。膜的重塑和破坏不是由最终的聚集体引起的,而是由特定的膜-聚集体相互作用引起的。
更新日期:2017-11-02
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