Author

T. K. Maiti

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 3 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 3 Assay:proteomics· 3 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Organism:mouse· 1

Frequent Co-Authors

S. Saha· 4 shared M. Surjit· 2 shared R. Verma· 2 shared S. Kumar· 2 shared A. Agrahari· 1 shared A. K. Dey· 1 shared A. Navalkar· 1 shared Anurag· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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4 shared papersMicrobiology

S. Saha

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Author profile →

4 papers

Recent·Most cited

Hepatitis C virus non-structural proteins modulate cellular kinases for increased cytoplasmic abundance of host factor HuR and facilitate viral replication

H. Raheja, B. George, S. K. Tripathi, S. Saha, T. K. Maiti, S. Das

This study identifies how HCV proteins NS3 and NS5A modulate host kinases to increase cytoplasmic HuR levels, enhancing viral replication.

bioRxiv · Aug 8, 2022Microbiology

RNA-protein interactome at the Hepatitis E virus internal ribosome entry site

S. Kumar, R. Verma, S. Saha, A. Agrahari, S. Shukla, Anurag, T. K. Maiti, S. Asthana, C. T. Ranjith-Kumar, M. Surjit

This study identifies the RNA-protein interactome of the Hepatitis E virus IRESl element and confirms its function as a bona fide internal ribosome entry site.

bioRxiv · Apr 11, 2022Microbiology

RNA-protein interaction analysis of SARS-CoV-2 5'- and 3'-untranslated regions identifies an antiviral role of lysosome-associated membrane protein-2

R. Verma, S. Saha, S. Kumar, S. Mani, T. K. Maiti, M. Surjit

This study identifies host proteins interacting with SARS-CoV-2 5' and 3' UTRs, revealing Lamp2a's antiviral role by reducing viral RNA levels.

bioRxiv · Jan 5, 2021Microbiology

Induction of intracellular wild-type p53 amyloids leading to cellular transformation and tumor formation in mice

A. Navalkar, S. Pandey, N. Singh, A. K. Dey, S. Saha, K. Patel, B. K. Mohanty, S. Jadhav, P. Chaudhari, T. K. Maiti, S. K. Maji

This study shows that wild-type p53 amyloid formation leads to cellular transformation and tumor formation in mice by enhancing survival, proliferation, and migration while suppressing tumor suppressors.

bioRxiv · Jun 4, 2020 · PreprintCancer Biology