Thioredoxin from Escherichia coli as a Role Model of Molecular Recognition, Folding, Dynamics and Function
Author:
Publisher
Bentham Science Publishers Ltd.
Subject
Biochemistry,General Medicine,Structural Biology
Cited by 9 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Remodelling the surface of thioredoxin from Escherichia coli by grafting an iron-binding site from the CyaY protein family;Dalton Transactions;2022
2. The trans-to-cis proline isomerization in E. coli Trx folding is accelerated by trans prolines;Biophysical Journal;2021-12
3. Exploring the conformational transition between the fully folded and locally unfolded substates of Escherichia coli thiol peroxidase;Physical Chemistry Chemical Physics;2020
4. Exploring the Conformational Transition Between the Fully Folded and Locally Unfolded Substates of the Escherichia coli thiol peroxidase;2019-12-28
5. Functional analyses of ancestral thioredoxins provide insights into their evolutionary history;Journal of Biological Chemistry;2019-09
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