Somavally Dalvi

Biotechnology Institute — United States

Biochemistry, Genetics and Molecular Biology · Life Sciences

5h-index68citations15works1.72yr avg
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Research Topics

14-3-3 protein interactions(7), Ubiquitin and proteasome pathways(5), Microtubule and mitosis dynamics(3), Bacteriophages and microbial interactions(3), Genomics and Phylogenetic Studies(2)

Publications15 total

Cover Image
The FASEB Journal·2025Open Access
<scp>ATP</scp> ‐Driven Allosteric Regulation of 14‐3‐3: Positive Modulation of <scp>ATP</scp> Hydrolysis and Negative Regulation of Peptide Binding
The FASEB Journal·2025· 1 citedOpen Access
A bacterial host factor confines phage localization for excluding the infected compartment through cell division
Cell Reports·2025· 1 citedOpen Access
Hidden Allostery in 14-3-3 Proteins Orchestrated by ATP
Indian Journal of Medical and Paediatric Oncology·2024Open Access
A large attachment organelle mediates interaction between a novel Nanobdellota archaeon YN1 and its host
2024· 2 citedOpen Access
Large attachment organelle mediates interaction between <i>Nanobdellota</i> archaeon YN1 and its host
The ISME Journal·2024· 6 citedOpen Access
Investigating the architectural details of enveloped phages by cryo-electron tomography
Acta Crystallographica Section A Foundations and Advances·2023
Snapshots of urea‐induced early structural changes and unfolding of an ankyrin repeat protein at atomic resolution
Protein Science·2022· 3 citedOpen Access
Structural insights on the effects of mutation of a charged binding pocket residue on phosphopeptide binding to 14‐3‐3ζ protein
Proteins Structure Function and Bioinformatics·2022· 4 cited
A druggable pocket on PSMD10Gankyrin that can accommodate an interface peptide and doxorubicin
European Journal of Pharmacology·2021· 10 cited
From cells to atoms: Cryo‐EM as an essential tool to investigate pathogen biology, host–pathogen interaction, and drug discovery
Molecular Microbiology·2021· 19 cited
Structural insights on the effects of mutation of a charged binding pocket residue on phosphopeptide binding to 14-3-3 <i>ζ</i> Protein
2021Open Access
14–3‐3γ prevents centrosome duplication by inhibiting NPM1 function
Genes to Cells·2021· 11 cited
14-3-3γ prevents centrosome duplication by inhibiting NPM1 function
2019· 2 citedOpen Access
Two negatively charged invariant residues influence ligand binding and conformational dynamics of 14‐3‐3ζ
FEBS Letters·2019· 9 cited

Frequent Co-authors

Prasanna Venkatraman(9), Debnath Ghosal(5), Doulin C. Shepherd(3), Kruti Modi(3), Priyanka Bagdiya(3), Arunabha Bose(2), Suchismita Dey(2), Prafful Nadkarni(2), Mukund Sudarshan(2), Tapas K. Kundu(2), Sorab N. Dalal(2), Mukund Sudharsan Medur Gurushankar(2), Matthew D. Johnson(2), Hiroyuki D. Sakai(2), Bindusmita Paul(2), Manasi Mudaliyar(2), Michiru Shimizu(2), Shubha Udupa(2), Moriya Ohkuma(2), Norio Kurosawa(2)