Domain Structure and Denaturation of a Dimeric Mip-like Peptidyl-Prolyl cis–trans Isomerase from Escherichia coli
Author:
Affiliation:
1. Department of Biochemistry, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata 700054, West Bengal, India
2. Department of Biotechnology, Haldia Institute of Technology, PO-HIT, Dt-Purba Medinipur, Pin 721657, West Bengal, India
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi2015037
Reference52 articles.
1. Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
2. Isolation and Amino Acid Sequence of a New 22-kDa FKBP-like Peptidyl-prolyl cis/trans-Isomerase of Escherichia coli
3. DNA sequence of mip, a Legionella pneumophila gene associated with macrophage infectivity
4. Chlamydia trachomatis Mip-like protein has peptidylprolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection
5. Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase involved in cell infection.
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