Serine 106 preserves the tertiary structure, function, and stability of a cyclophilin from Staphylococcus aureus-Reference-Cited by-同舟云学术

Serine 106 preserves the tertiary structure, function, and stability of a cyclophilin from Staphylococcus aureus

Published:2021-12-30 Issue: Volume: Page:1-16
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Seal Soham¹,Banerjee Nilanjan²,Mahato Rohit¹,Kundu Tanmoy¹,Sinha Debabrata¹,Chakraborty Tushar¹,Sinha Debasmita¹,Sau Keya³,Chatterjee Subhrangsu²,Sau Subrata¹

Affiliation:

1. Department of Biochemistry, Bose Institute, Kolkata, West Bengal, India

2. Department of Biophysics, Bose Institute, Kolkata, West Bengal, India

3. Department of Biotechnology, Haldia Institute of Technology, Haldia, West Bengal, India

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2021.2021992

Reference52 articles.

1. Characterization of the Staphylococcus aureus Heat Shock, Cold Shock, Stringent, and SOS Responses and Their Effects on Log-Phase mRNA Turnover

2. Deletion of loop fragment adjacent to active site diminishes the stability and activity of exo-inulinase

3. New strategies for targeting and treatment of multi-drug resistant Staphylococcus aureus

4. Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse

5. The Amber biomolecular simulation programs

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