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Meng-Rong Ma

Showing results (1-10 of 4) with videos related to

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Scientific Reports|November 18, 2016
Phosphorylation induces distinct alpha-synuclein strain formationMeng-Rong Ma, Zhi-Wen Hu, Yu-Fen Zhao, et al.
The Journal of Biological Chemistry|May 28, 2017
Phosphorylation at Ser<sup>8</sup> as an intrinsic regulatory switch to regulate the morphologies and structures of Alzheimer's 40-residue β-amyloid (Aβ40) fibrilsZhi-Wen Hu, Meng-Rong Ma, Yong-Xiang Chen, et al.
The Journal of Biological Chemistry|December 30, 2016
Phosphorylation at Ser<sup>8</sup> as an Intrinsic Regulatory Switch to Regulate the Morphologies and Structures of Alzheimer's 40-residue β-Amyloid (Aβ40) FibrilsZhi-Wen Hu, Meng-Rong Ma, Yong-Xiang Chen, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 26, 2021
Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's diseaseShengnan Zhang, Yu-Qing Liu, Chunyu Jia, et al.
Pageof 1

Showing results (1-10 of 4) with videos related to

Sort By:
Pageof 1
Scientific Reports|November 18, 2016
Phosphorylation induces distinct alpha-synuclein strain formationMeng-Rong Ma, Zhi-Wen Hu, Yu-Fen Zhao, et al.
The Journal of Biological Chemistry|May 28, 2017
Phosphorylation at Ser<sup>8</sup> as an intrinsic regulatory switch to regulate the morphologies and structures of Alzheimer's 40-residue β-amyloid (Aβ40) fibrilsZhi-Wen Hu, Meng-Rong Ma, Yong-Xiang Chen, et al.
The Journal of Biological Chemistry|December 30, 2016
Phosphorylation at Ser<sup>8</sup> as an Intrinsic Regulatory Switch to Regulate the Morphologies and Structures of Alzheimer's 40-residue β-Amyloid (Aβ40) FibrilsZhi-Wen Hu, Meng-Rong Ma, Yong-Xiang Chen, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 26, 2021
Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's diseaseShengnan Zhang, Yu-Qing Liu, Chunyu Jia, et al.
Pageof 1