Author

M. Gielnik

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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Assay:protein structure· 3 Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Approach:biophysical modeling· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. Graslund· 3 shared M. Kozak· 3 shared S. K. T. S. Warmlander· 3 shared J. Jarvet· 2 shared A. Barth· 1 shared A. Noormagi· 1 shared A. Szymanska· 1 shared E. Berntsson· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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3 shared papersBiophysics

A. Graslund

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Author profile →

3 papers

Recent·Most cited

Characterization of uranyl ion binding to amyloid beta (Aβ) peptides: effects on Aβ structure and aggregation

E. Berntsson, F. Vosough, A. Noormagi, K. Padari, F. Asplund, M. Gielnik, S. Paul, J. Jarvet, V. Tougu, P. M. Roos, M. Kozak, A. Graslund, A. Barth, M. Pooga, P. Palumaa, S. K. T. S. Warmlander

This study investigates how uranyl ions bind to amyloid beta peptides, altering their structure and aggregation, potentially contributing to Alzheimer's disease pathology.

bioRxiv · Mar 29, 2023Biophysics

The Prion Protein Octarepeat Domain Forms Transient β-sheet Structures Upon Residue-Specific Cu(II) and Zn(II) Binding

M. Gielnik, A. Szymanska, X. Dong, J. Jarvet, Z. M. Svedruzic, A. Graslund, M. Kozak, S. K. T. S. Warmlander

This study investigates how Cu(II) and Zn(II) binding affects the structure of the prion protein's octarepeat domain, suggesting a potential role in amyloid formation in TSEs.

bioRxiv · Dec 12, 2021 · PreprintBiophysics

The engineered peptide construct NCAM1-Aβ inhibits aggregation of the human prion protein (PrP)

M. Gielnik, L. Zhukova, I. Zhukov, A. Graslund, M. Kozak, S. K. T. S. Warmlander

The paper shows that the engineered peptide NCAM1-Aβ inhibits human PrP aggregation using atomic force microscopy.

bioRxiv · Jan 4, 2021Biochemistry