Engineering a Hyperstable <i>Yersinia pestis</i> Outer Membrane Protein Ail Using Thermodynamic Design-Reference-Cited by-同舟云学术

Engineering a Hyperstable Yersinia pestis Outer Membrane Protein Ail Using Thermodynamic Design

Published:2022-01-21 Issue:4 Volume:144 Page:1545-1555
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

George Anjana¹,Ravi Roshika¹,Tiwari Pankaj Bharat¹,Srivastava Shashank Ranjan¹,Jain Vikas²,Mahalakshmi Radhakrishnan¹^ORCID

Affiliation:

1. Molecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal - 462066, India

2. Microbiology and Molecular Biology Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal - 462066, India

Funder

The Wellcome Trust DBT India Alliance

Science and Engineering Research Board

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.1c05964

Reference68 articles.

1. Parallel independent evolution of pathogenicity within the genus Yersinia

2. Bacterial resistance to complement killing mediated by the Ail protein of Yersinia enterocolitica.

3. The Yersiniae — a model genus to study the rapid evolution of bacterial pathogens

4. Resistance of Yersinia pestis to Complement-Dependent Killing Is Mediated by the Ail Outer Membrane Protein

5. Structure of human Vitronectin C-terminal domain and interaction with Yersinia pestis outer membrane protein Ail

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