AG
Anindya Sundar Ghosh
Also known as: Ghosh A S
Indian Institute of Technology Kharagpur, University of North Dakota School of Medicine and Health Sciences, Bose Institute
Employment
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Indian Institute of Technology Kharagpur Professor2018 - Present
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Indian Institute of Technology Kharagpur Associate Professor2011 - 2018
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Indian Institute of Technology Kharagpur Assistant Professor2004 - 2011
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University of North Dakota School of Medicine and Health Sciences Postdoctoral Research Associate2001 - 2004
Education
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Bose Institute Ph.D from Calcutta University1993 - 1999
Projects & Funding
Projects & funding information is unavailable.
Publications (59)
- Placentrex disrupts the biofilm formation of Pseudomonas aeruginosa through multi-target transcriptional reprogramming Save
- Deciphering the Role of the Nonactive Site Ancillary Residues in Maintaining the Activity and Substrate Specificity of the OXA-232 β-Lactamase Save
- Rv0783c of Mycobacterium tuberculosis acts as a proton-motive force dependent multidrug efflux transporter involved in the efflux of structurally unrelated antibiotics and enhancing biofilm formation Save
- Deletion of major shell proteins of ethanolamine utilization microcompartment reduces intrinsic antibiotic resistance, biofilm, and intracellular survival of Salmonella Typhimurium Save
- Putative MFS transporter Rv1250 of Mycobacterium tuberculosis is involved in multidrug efflux activity Save
- Deletion of major shell proteins of ethanolamine utilization microcompartment reduces intrinsic antibiotic resistance, biofilm, and intracellular survival of Salmonella Typhimurium Save
- Conserved ancillary residues situated proximally to the VIM-2 active-site affect its metallo β-lactamase activity Save
- MSMEG_3978 (BlaE) from Mycobacterium smegmatis is an extended-spectrum beta-lactamase with a critical tyrosine residue governing its deacylation Save
- Involvement of CorA of Mycobacterium smegmatis in exerting intrinsic resistance towards structurally unrelated antibiotics Save
- Conserved ancillary residues situated proximally to the VIM-2 active site affect its metallo β-lactamase activity Save