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Banerjee, Rahul
- Uranium and Associated Polymetallic Mineralization in Palaeoproterozoic Khetabari Formation of Bomdila Group, Laggi Gamlin Area, West Siang District, Arunachal Pradesh, India
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1 Atomic Minerals Directorate for Exploration and Research, Shillong 793 019, IN
2 Atomic Minerals Directorate for Exploration and Research, Hyderabad 500 016, IN
1 Atomic Minerals Directorate for Exploration and Research, Shillong 793 019, IN
2 Atomic Minerals Directorate for Exploration and Research, Hyderabad 500 016, IN
Source
Current Science, Vol 119, No 4 (2020), Pagination: 603-606Abstract
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- Role of peptidyl-prolyl cis–trans isomerases in infectious diseases and host–pathogen interactions
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PDF Views:77
Authors
Affiliations
1 Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF-Bidhannagar, Kolkata 700 064, India; Homi Bhabha National Institute, Anushaktinagar, Mumbai 400 094, IN
1 Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF-Bidhannagar, Kolkata 700 064, India; Homi Bhabha National Institute, Anushaktinagar, Mumbai 400 094, IN
Source
Current Science, Vol 121, No 6 (2021), Pagination: 758-768Abstract
Peptidyl-prolyl cis–trans isomerases (PPIases) catalyse the cis–trans isomerization of Ca atoms about the peptide bond preceding a proline residue, thereby regulating a conformational switch which controls a plethora of cellular processes. PPIases play a key role in the survival, reproduction, proliferation and virulence of microbial pathogens vis-à-vis their human host. In addition, human PPIases either aid or retard viral replication and modulate host immune response. The article discusses the structure–function relationships of PPIases in the context of microbial virulence (with an emphasis on viruses), and on targeting PPIases for COVID-19, responsible for untold human sufferings.Keywords
Host immune response, infectious diseases, pathogenicity, virulence, peptidyl-prolyl cis–trans isomeraseFull Text
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