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Amit Singh

Researcher at National Institute of Technology, Patna

Publications -  773
Citations -  18812

Amit Singh is an academic researcher from National Institute of Technology, Patna. The author has contributed to research in topics: Digital watermarking & Medicine. The author has an hindex of 57, co-authored 640 publications receiving 13795 citations. Previous affiliations of Amit Singh include Ithaca College & Center for Infectious Disease Research and Policy.

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Mycobacterium tuberculosis WhiB3 responds to O2 and nitric oxide via its [4Fe-4S] cluster and is essential for nutrient starvation survival

TL;DR: It is shown that Mtb WhiB3 responds to the dormancy signals NO and O2 through its iron-sulfur (Fe-S) cluster, and EPR analysis demonstrates that NO forms a protein-bound dinitrosyl–iron–dithiol complex with the Fe-S cluster, indicating that NO specifically targets the WhiBs 3Fe-4S cluster.
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Multi-layer security of medical data through watermarking and chaotic encryption for tele-health applications

TL;DR: Experimental results clearly indicated that the proposed technique is highly robust and sufficient secure for various forms of attacks without any significant distortions between watermarked and cover image.
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Reengineering redox sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection

TL;DR: In this article, a real-time image of mycothiol redox potential (EMSH) within Mtb cells during infection was used to measure the changes in intramycobacterial EMSH with unprecedented sensitivity and specificity.
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An improved DWT-SVD domain watermarking for medical information security

TL;DR: Experimental results demonstrate that the suggested watermarking technique archives high robustness against attacks in comparison to the other scheme for medical images, and verification its robustness for various attacks while maintaining imperceptibility, security and compression ratio.
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Dissecting virulence pathways of Mycobacterium tuberculosis through protein–protein association

TL;DR: A simple system based upon the functional reconstitution of two small murine dihydrofolate reductase domains independently fused to two interacting proteins that will be a major contributor to the systematic assembly of mycobacterial protein interaction maps that will lead to the development of better strategies for the control of tuberculosis.