Protein Allostery Study in Cells Using NMR Spectroscopy-Reference-Cited by-同舟云学术

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Protein Allostery Study in Cells Using NMR Spectroscopy

Published:2024-04-23 Issue:18 Volume:96 Page:7065-7072
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Chen Xiaoxu¹²³,Zhang Xueying¹²³⁴,Qin Mingming¹²³,Chen Jingfei¹²³,Wang Mengting¹²³,Liu Zhijun⁵,An Liaoyuan¹²³,Song Xiangfei¹²³,Yao Lishan¹²³^ORCID

Affiliation:

1. Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, China

2. Shandong Energy Institute, Qingdao 266101, China

3. Qingdao New Energy Shandong Laboratory, Qingdao 266101, China

4. University of Chinese Academy of Sciences, Beijing 100049, China

5. National Facility for Protein Science, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China

Funder

National Key Research and Development Program of China

Youth Innovation Promotion Association of the Chinese Academy of Sciences

Taishan Scholar Project of Shandong Province

National Natural Science Foundation of China

Natural Science Foundation of Shandong Province

Shandong Energy Institute, Chinese Academy of Sciences

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.4c00360

Reference78 articles.

1. Principles of Allosteric Interactions in Cell Signaling

2. Advances in NMR Methods To Map Allosteric Sites: From Models to Translation

3. The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery

4. Allosteric switch regulates protein–protein binding through collective motion

5. Substrate-binding domain conformational dynamics mediate Hsp70 allostery

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