Author

N. Lupilov

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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Biochemistry· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Assay:proteomics· 4 Organism:E. coli· 3 Organism:human· 3 Research Focus:cell type annotation· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:differential expression· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

L. I. Leichert· 5 shared J. E. Bandow· 3 shared A. Müller· 2 shared A. Ulfig· 2 shared L. Quadros Barse· 2 shared M. Varatnitskaya· 2 shared A. M. Imann· 1 shared A. V. Schulz· 1 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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5 shared papersBiochemistry

L. I. Leichert

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5 papers

Recent·Most cited

Comparison of the mechanism of antimicrobial action of the gold(I) compound auranofin in Gram-positive and Gram-negative bacteria

L. Quadros Barse, A. Ulfig, M. Varatnitskaya, M. Vazquez-Hernandez, J. Yoo, A. M. Imann, N. Lupilov, K. Becker, M. Fischer, J. E. Bandow, L. I. Leichert

This paper investigates how auranofin affects Gram-positive and Gram-negative bacteria, finding that Gram-negative bacteria are more resistant due to efflux systems and glutathione levels.

Microbiology Spectrum · Nov 5, 2024Peer-reviewedBiochemistry

Auranofin induces disulfide bond-mimicking S-Au-S bonds in protein thiol pairs

L. Quadros Barse, P. Duchting, N. Lupilov, J. E. Bandow, U. Kramer, L. I. Leichert

This study shows auranofin forms S-Au-S bonds between cysteine thiols in proteins, independent of thioredoxin reductase, suggesting a new mechanism for its antibacterial activity.

bioRxiv · Jan 15, 2024 · PreprintBiochemistry

The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli

L. R. Knoke, J. Zimmermann, N. Lupilov, J. F. Schneider, B. Celebi, B. Morgan, L. I. Leichert

This study investigates the role of glutathione in periplasmic redox homeostasis and oxidative protein folding in E. coli using genetically encoded redox probes.

bioRxiv · Mar 7, 2023Biochemistry

An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated proteins

M. Varatnitskaya, J. Fasel, A. Müller, N. Lupilov, Y. Shi, K. Fuchs, M. Krewing, C. Jung, T. Jacob, B. Sitek, J. E. Bandow, K. S. Carroll, L. I. Leichert

This study identifies specific chlorinated residues in RidA that are critical for its chaperone activity under oxidative stress.

bioRxiv · Oct 26, 2021Biochemistry

N-chlorination mediates protective and immunomodulatory effects of oxidized human plasma proteins

A. Ulfig, A. V. Schulz, A. Müller, N. Lupilov, L. I. Leichert

This study shows that N-chlorination of plasma proteins by HOCl converts them into chaperones and immune activators, with implications for neutrophil survival and inflammation.

bioRxiv · Apr 11, 2019Biochemistry