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Your search keyword '"Guo, Da-Chuan"' showing total 24 results
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24 results on '"Guo, Da-Chuan"'

8. Cardiovascular health metrics defined by Life's Essential 8 scores and subsequent macrovascular and microvascular complications in individuals with type 2 diabetes: A prospective cohort study

Author

Huang, Ze‐Gui, primary, Gao, Jing‐Wei, additional, Zhang, Hai‐Feng, additional, You, Si, additional, Xiong, Zhuo‐Chao, additional, Wu, Yu‐Biao, additional, Guo, Da‐Chuan, additional, Wang, Jing‐Feng, additional, Chen, Yang‐Xin, additional, Zhang, Shao‐Ling, additional, and Liu, Pin‐Ming, additional

Published
2024
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12. Glycolysis Inhibition Alleviates Cardiac Fibrosis After Myocardial Infarction by Suppressing Cardiac Fibroblast Activation

Author

Chen, Zhi-Teng, primary, Gao, Qing-Yuan, additional, Wu, Mao-Xiong, additional, Wang, Meng, additional, Sun, Run-Lu, additional, Jiang, Yuan, additional, Guo, Qi, additional, Guo, Da-Chuan, additional, Liu, Chi-Yu, additional, Chen, Si-Xu, additional, Liu, Xiao, additional, Wang, Jing-Feng, additional, Zhang, Hai-Feng, additional, and Chen, Yang-Xin, additional

Published
2021
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13. Protein-RNA Interaction Interface Prediction and Design

Author

华中科技大学物理学院生物分子物理与模建小组, 武汉 ,Biomolecular Physics, Zhao Yun-Jie, Liu Shi-Yong, Huang Yang-Yu, Yang Xiu-Feng, Li Lin, Guo Da-Chuan, LI Hao-Tian, Cheng Hong-Li, and JI Xiao-Feng

Subjects
Crystallography, Conformational change, Computer science, Docking (molecular), RNA, Interaction interface, Computational biology, Physical and Theoretical Chemistry, Experimental methods, Medical research, Macromolecule
Abstract

RNA-protein interactions play key roles in many biological processes. The three dimensional (3D) structure of protein-RNA complexes can be determined experimentally by structural biologists. The recognition between protein and RNA can be understood from the 3D atomic structure. However, the structure determination of protein-RNA complexes by experimental methods is often difficult and costly, and limited to the binding strength. Thus, the prediction and design of protein-RNA complex structures is important in biological medical research. In this review, we will discuss the recent progress in protein-RNA interface prediction and design, which includes the following aspects: (1) protein-RNA docking and the conformational change on binding; (2) the recognition mechanism of protein-RNA binding; (3) the molecular design based on the protein-RNA interface. Improvement of the protein-RNA docking algorithm will help us annotate a large number of proteins and RNA with unknown function, and molecular design based on macromolecular interactions will be useful in drug design.

Published
2012
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17. Protein Structural Ensembles Visualized by Solvent Paramagnetic Relaxation Enhancement.

Author

Gong, Zhou, Gu, Xin-Hua, Guo, Da-Chuan, Wang, Jin, and Tang, Chun

Subjects
PROTEIN structure, PARAMAGNETIC materials, NUCLEAR magnetic resonance spectroscopy, MOLECULAR dynamics, CONFORMATIONAL analysis
Abstract

A protein can be in different conformations when fulfilling its function. Yet depiction of protein structural ensembles remains difficult. Here we show that the accurate measurement of solvent paramagnetic relaxation enhancement (sPRE) in the presence of an inert paramagnetic cosolute allows the assessment of protein dynamics. Demonstrated with two multi-domain proteins, we present a method to characterize protein microsecond-millisecond dynamics based on the analysis of the sPRE. Provided with the known structures of a protein, our method uncovers an ensemble of structures that fully accounts for the observed sPRE. In conjunction with molecular dynamics simulations, our method can identify protein alternative conformation that has only been theorized before. Together, our method expands the application of sPRE beyond structural characterization of rigid proteins and complements the established PRE NMR technique. [ABSTRACT FROM AUTHOR]

Published
2017
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18. Rücktitelbild: Visualizing an Ultra-Weak Protein-Protein Interaction in Phosphorylation Signaling (Angew. Chem. 43/2014)

Author

Xing, Qiong, primary, Huang, Peng, additional, Yang, Ju, additional, Sun, Jian-Qiang, additional, Gong, Zhou, additional, Dong, Xu, additional, Guo, Da-Chuan, additional, Chen, Shao-Min, additional, Yang, Yu-Hong, additional, Wang, Yan, additional, Yang, Ming-Hui, additional, Yi, Ming, additional, Ding, Yi-Ming, additional, Liu, Mai-Li, additional, Zhang, Wei-Ping, additional, and Tang, Chun, additional

Published
2014
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19. Back Cover: Visualizing an Ultra-Weak Protein-Protein Interaction in Phosphorylation Signaling (Angew. Chem. Int. Ed. 43/2014)

Author

Xing, Qiong, primary, Huang, Peng, additional, Yang, Ju, additional, Sun, Jian-Qiang, additional, Gong, Zhou, additional, Dong, Xu, additional, Guo, Da-Chuan, additional, Chen, Shao-Min, additional, Yang, Yu-Hong, additional, Wang, Yan, additional, Yang, Ming-Hui, additional, Yi, Ming, additional, Ding, Yi-Ming, additional, Liu, Mai-Li, additional, Zhang, Wei-Ping, additional, and Tang, Chun, additional

Published
2014
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20. Visualizing an Ultra-Weak Protein-Protein Interaction in Phosphorylation Signaling

Author

Xing, Qiong, primary, Huang, Peng, additional, Yang, Ju, additional, Sun, Jian-Qiang, additional, Gong, Zhou, additional, Dong, Xu, additional, Guo, Da-Chuan, additional, Chen, Shao-Min, additional, Yang, Yu-Hong, additional, Wang, Yan, additional, Yang, Ming-Hui, additional, Yi, Ming, additional, Ding, Yi-Ming, additional, Liu, Mai-Li, additional, Zhang, Wei-Ping, additional, and Tang, Chun, additional

Published
2014
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24. Protein Structural Ensembles Visualized by Solvent Paramagnetic Relaxation Enhancement.

Author

Gong Z, Gu XH, Guo DC, Wang J, and Tang C

Subjects
Protein Conformation, Solvents chemistry, Molecular Dynamics Simulation, Proteins chemistry
Abstract

A protein can be in different conformations when fulfilling its function. Yet depiction of protein structural ensembles remains difficult. Here we show that the accurate measurement of solvent paramagnetic relaxation enhancement (sPRE) in the presence of an inert paramagnetic cosolute allows the assessment of protein dynamics. Demonstrated with two multi-domain proteins, we present a method to characterize protein microsecond-millisecond dynamics based on the analysis of the sPRE. Provided with the known structures of a protein, our method uncovers an ensemble of structures that fully accounts for the observed sPRE. In conjunction with molecular dynamics simulations, our method can identify protein alternative conformation that has only been theorized before. Together, our method expands the application of sPRE beyond structural characterization of rigid proteins and complements the established PRE NMR technique., (© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Published
2017
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