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Your search keyword '"Mu-Yun Xie"' showing total 3 results
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3 results on '"Mu-Yun Xie"'

1. Peptide diffusion and self-assembly in ambient water nanofilm on mica surface

Author

Hai Li, Feng Zhang, Yi Zhang, Ming Ye, Bo Zhou, Yu-Zhao Tang, Hai-Jun Yang, Mu-Yun Xie, Sheng-Fu Chen, Jian-Hua He, Hai-Ping Fang, and Jun Hu

Subjects
Atomic force microscopy -- Usage, Diffusion processes -- Analysis, Peptides -- Chemical properties, Schists -- Structure, Schists -- Chemical properties, Chemicals, plastics and rubber industries
Published
2009

2. Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion

Author

Jian Zhao, Lei Lei Jiang, Mei Xia Che, Jianhua He, Hong-Yu Hu, Chen Jie Zhou, Hai Yin Li, and Mu Yun Xie

Subjects
Amyloid, Cytoplasmic inclusion, Peptide, Helix-turn-helix, Biology, medicine.disease_cause, Biochemistry, DNA-binding protein, Inclusion bodies, Ubiquitin, mental disorders, medicine, Animals, Humans, Caenorhabditis elegans, Molecular Biology, Helix-Turn-Helix Motifs, chemistry.chemical_classification, Inclusion Bodies, Mutation, nutritional and metabolic diseases, Molecular Bases of Disease, Cell Biology, Cell biology, nervous system diseases, Protein Structure, Tertiary, DNA-Binding Proteins, chemistry, Drug Design, TDP-43 Proteinopathies, biology.protein, Hydrophobic and Hydrophilic Interactions, HeLa Cells
Abstract

TDP-43 (TAR DNA-binding protein of 43 kDa) is a major deposited protein in amyotrophic lateral sclerosis and frontotemporal dementia with ubiquitin. A great number of genetic mutations identified in the flexible C-terminal region are associated with disease pathologies. We investigated the molecular determinants of TDP-43 aggregation and its underlying mechanisms. We identified a hydrophobic patch (residues 318–343) as the amyloidogenic core essential for TDP-43 aggregation. Biophysical studies demonstrated that the homologous peptide formed a helix-turn-helix structure in solution, whereas it underwent structural transformation from an α-helix to a β-sheet during aggregation. Mutation or deletion of this core region significantly reduced the aggregation and cytoplasmic inclusions of full-length TDP-43 (or TDP-35 fragment) in cells. Thus, structural transformation of the amyloidogenic core initiates the aggregation and cytoplasmic inclusion formation of TDP-43. This particular core region provides a potential therapeutic target to design small-molecule compounds for mitigating TDP-43 proteinopathies.

Published
2013

3. Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion.

Author

Lei-Lei Jiang, Mei-Xia Che, Jian Zhao, Chen-Jie Zhou, Mu-Yun Xie, Hai-Yin Li, Jian-Hua He, and Hong-Yu Hu

Subjects
*DNA-binding proteins, *AMYOTROPHIC lateral sclerosis, *GENETIC mutation, *C-terminal binding proteins, *HELICAL structure, *BIOLOGICAL aggregation
Abstract

TDP-43 (TAR DNA-binding protein of 43 kDa) is a major deposited protein in amyotrophic lateral sclerosis and frontotemporal dementia with ubiquitin. A great number of genetic mutations identified in the flexible C-terminal region are associated with disease pathologies. We investigated the molecular determinants of TDP-43 aggregation and its underlying mechanisms. We identified a hydrophobic patch (residues 318-343) as the amyloidogenic core essential for TDP-43 aggregation. Biophysical studies demonstrated that the homologous peptide formed a helix-turn-helix structure in solution, whereas it underwent structural transformation from an α-helix to a β-sheet during aggregation. Mutation or deletion of this core region significantly reduced the aggregation and cytoplasmic inclusions of full-length TDP-43 (or TDP-35 fragment) in cells. Thus, structural transformation of the amyloidogenic core initiates the aggregation and cytoplasmic inclusion formation of TDP-43. This particular core region provides a potential therapeutic target to design small-molecule compounds for mitigating TDP-43 proteinopathies. [ABSTRACT FROM AUTHOR]

Published
2013
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