Author

Chiranjit Chowdhury

National Chemical LaboratoryORCID 0000-0003-2026-5324Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Microbiology· 2 Bioengineering· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Organism:bacteria (other)· 2 Assay:proteomics· 2 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:metabolism & bioenergetics· 1

Frequent Co-Authors

Aishwarya S. DavkhariD· 2 shared Anindya Sundar GhoshiD· 2 shared Minal R. BhaleraoiD· 2 shared Sachin Bharat AgawaneiD· 2 shared Ajit Ramesh Sawant· 1 shared Anjali Sutar· 1 shared Ankita SahaiD· 1 shared Bayomi BijuiD· 1 shared

Activity by Year

2025-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersMicrobiology

Aishwarya S. DavkharORCID

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

MicrobiologybioRxivPreprintOct 8, 2026

Genetic analyses reveal distinct functional roles of Eut microcompartment shell proteins in ethanolamine metabolism in Salmonella

Minal R. Bhalerao, Anjali Sutar, Aishwarya S. Davkhar…·Chiranjit Chowdhury

DOI 10.64898/2026.10.07.757396

bacteria (other)metabolomics

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BioengineeringbioRxivPreprintAug 5, 2026

Genetic and Biochemical Characterization Reveals PduU as a Modular Tool for Tuning Pdu Microcompartment Permeability

Komal S. Timane, Chiranjit Chowdhury

This study shows that modifying PduU, a shell protein in bacterial microcompartments, tunes permeability without disrupting structure, enhancing propionate production.

DOI 10.64898/2026.07.29.741414

proteomicsexperimental assay

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Molecular BiologybioRxivPreprintMay 23, 2026

Deciphering the role of the non-active site ancillary residues in maintaining the activity and substrate specificity of OXA-232 beta-lactamase

Tejavath Ajith, Bayomi Biju, Diamond Jain…·Anindya Sundar Ghosh

This study investigates the role of non-active site residues in OXA-232 beta-lactamase, showing their impact on activity, substrate specificity, and structural stability through site-directed mutagenesis and biophysical analysis.

DOI 10.64898/2026.05.22.727341

experimental assay

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MicrobiologyResearch in MicrobiologyPeer-reviewedNov 1, 2025

Deletion of major shell proteins of ethanolamine utilization microcompartment reduces intrinsic antibiotic resistance, biofilm, and intracellular survival of Salmonella Typhimurium

Minal R. Bhalerao, Aishwarya S. Davkhar, Ajit Ramesh Sawant…·Chiranjit Chowdhury

1 citation

bacteria (other)proteomics

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