Author

V. K. Shukla

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Organism:E. coli· 1 Organism:human· 1 Assay:metagenomics· 1

Frequent Co-Authors

D. F. Hansen· 2 shared A. kumar· 1 shared A. M. Figueiredo· 1 shared G. Karunanithy· 1 shared G. T. Heller· 1 shared J. S. Singh· 1 shared N. A. Panchakshari· 1 shared P. Cherry· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiophysics

D. F. Hansen

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3 papers

Recent·Most cited

BiophysicsbioRxivSep 15, 2023

Solution State Methyl NMR Spectroscopy of Large Non-Deuterated Proteins Enabled by Deep Neural Networks

G. Karunanithy, V. K. Shukla, D. F. Hansen

This paper uses deep neural networks to process methyl-TROSY NMR spectra of non-deuterated proteins, achieving results comparable to deuterated samples.

DOI 10.1038/s41467-024-49378-8

E. colimetagenomics

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BiophysicsbioRxivMay 3, 2023

Small-molecule binding to an intrinsically disordered protein revealed by experimental NMR 19F transverse spin-relaxation

G. T. Heller, V. K. Shukla, A. M. Figueiredo, D. F. Hansen

This study shows that 19F transverse relaxation rates from NMR can detect small-molecule binding to intrinsically disordered proteins, demonstrating 5-fluoroindole binds to HCV NS5A with a Kd of 260 ± 110 M.

DOI 10.1021/jacs.3c11614

proteomicsexperimental assay

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BiochemistrybioRxivPreprintAug 18, 2021

Implications of critical nodes-dependent unidirectional cross-talk between Plasmodium and Human SUMO

R. K. Mishra, J. S. Singh, S. T K…·A. kumar

This study identifies critical residues in Plasmodium SUMO and Ubc9 that enable unidirectional cross-species interactions with human SUMOylation machinery, suggesting potential targets for antimalarial drugs.

DOI 10.1101/2021.08.18.456755

humanplant (other)

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