Author

V. Smirnovas

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· 3 Approach:biophysical modeling· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1 Assay:protein structure· 1

Frequent Co-Authors

A. L. Bula· 1 shared A. Lends· 1 shared A. Sakalauskas· 1 shared B. Kovacech· 1 shared C. K. Xu· 1 shared D. Sulskis· 1 shared E. Gazit· 1 shared G. Kucinskas· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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1 shared paperBiophysics

A. L. Bula

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivPreprintMay 31, 2023

Formation of amyloid fibrils by the regulatory 14-3-3ζ protein

D. Sulskis, M. Ziaunys, A. Sakalauskas, V. Smirnovas

This study investigates the formation of amyloid fibrils by the 14-3-3ζ protein using bioinformatics and structural analysis methods.

DOI 10.1101/2023.05.31.543065

humanproteomics

𝕏 PostBluesky

BiophysicsbioRxivPreprintFeb 1, 2023

dGAE(297-391) tau fragment promotes formation of CTE-like full-length tau filaments

K. Kitoka, A. Lends, G. Kucinskas…·K. Jaudzems

The paper shows that the dGAE tau fragment seeds the formation of CTE-like full-length tau filaments in vitro.

DOI 10.1101/2023.02.01.526268

protein structureexperimental assay

𝕏 PostBluesky

BiophysicsbioRxivMay 26, 2020

Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses

J. Pansieri, I. A. Iashchishyn, H. Fakhouri…·L. Morozova-Roche

The paper investigates the co-aggregation of S100A9 and Aβ42 amyloids using CDMS, microscopy, and kinetic analysis, revealing templating of S100A9 fibrils on Aβ42 surfaces.

DOI 10.1039/c9sc05905a

humanproteomics

𝕏 PostBluesky