Author

N. Gahlot

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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Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Navalkar· 2 shared A. S. Sawner· 2 shared D. Datta· 2 shared K. Patel· 2 shared L. Gadhe· 2 shared M. Poudyal· 2 shared P. Kadu· 2 shared S. K. Maji· 2 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiophysics

A. Navalkar

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2 papers

Recent·Most cited

Nucleo-cytoplasmic environment modulates spatio-temporal p53 phase separation

D. Datta, A. Navalkar, A. Sakunthala, A. Paul, K. Patel, S. Masurkar, L. Gadhe, S. Sengupta, M. Poudyal, J. Devi, A. S. Sawner, P. Kadu, R. Shaw, S. Pandey, S. Mukherjee, , S. K. Maji

This study shows that p53 phase separation and condensate formation are modulated by the nucleo-cytoplasmic environment and cancer-associated mutations affect condensate stability and DNA binding.

bioRxiv · Oct 16, 2023 · PreprintBiophysics

Liquid condensate is a common state of proteins and polypeptides at the regime of high intermolecular interactions

M. Poudyal, K. Patel, A. S. Sawner, L. Gadhe, P. Kadu, D. Datta, S. Mukherjee, S. Ray, A. Navalkar, S. Maiti, D. Chatterjee, R. Bera, N. Gahlot, R. K. Padinhateeri, S. K. Maji

The paper demonstrates that proteins and polypeptides can form liquid condensates under high intermolecular interaction conditions, showing that LLPS is a common state across diverse molecular structures.

bioRxiv · Dec 31, 2021Biophysics