Your browser doesn't support javascript.
loading
Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme.
Chen, Yao; Xu, Weiya; Yu, Shuwei; Ni, Kang; She, Guangbiao; Ye, Xiaodong; Xing, Qiong; Zhao, Jian; Huang, Chengdong.
Affiliation
  • Chen Y; Ministry of Education Key Laboratory for Membrane-less Organelles & Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
  • Xu W; Ministry of Education Key Laboratory for Membrane-less Organelles & Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
  • Yu S; State Key Laboratory of Tea Plant Biology and Utilization, College of Tea and Food Science and Technology, Anhui Agricultural University, Hefei, China.
  • Ni K; Hefei National Laboratory for Physical Sciences at the Microscale, Department of Chemical Physics, University of Science and Technology of China, Hefei, China.
  • She G; State Key Laboratory of Tea Plant Biology and Utilization, College of Tea and Food Science and Technology, Anhui Agricultural University, Hefei, China.
  • Ye X; Hefei National Laboratory for Physical Sciences at the Microscale, Department of Chemical Physics, University of Science and Technology of China, Hefei, China.
  • Xing Q; State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan, China.
  • Zhao J; State Key Laboratory of Tea Plant Biology and Utilization, College of Tea and Food Science and Technology, Anhui Agricultural University, Hefei, China.
  • Huang C; Ministry of Education Key Laboratory for Membrane-less Organelles & Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China.
Elife ; 102021 12 13.
Article in En | MEDLINE | ID: mdl-34898426
Subject(s)
Key words
Fulltext
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Escherichia coli / Glutamate-Ammonia Ligase Type of study: Prognostic_studies Language: En Journal: Elife Year: 2021 Type: Article Affiliation country: China
Fulltext
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Escherichia coli / Glutamate-Ammonia Ligase Type of study: Prognostic_studies Language: En Journal: Elife Year: 2021 Type: Article Affiliation country: China