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 10 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. Trx4, a novel thioredoxin protein, is important for Toxoplasma gondii fitness;Parasites & Vectors;2024-04-04
2. Remodelling the surface of thioredoxin from Escherichia coli by grafting an iron-binding site from the CyaY protein family;Dalton Transactions;2022
3. The trans-to-cis proline isomerization in E. coli Trx folding is accelerated by trans prolines;Biophysical Journal;2021-12
4. Exploring the conformational transition between the fully folded and locally unfolded substates of Escherichia coli thiol peroxidase;Physical Chemistry Chemical Physics;2020
5. Exploring the Conformational Transition Between the Fully Folded and Locally Unfolded Substates of the Escherichia coli thiol peroxidase;2019-12-28
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