Author

J. Jarvet

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· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

A. Graslund· 4 shared S. K. T. S. Warmlander· 4 shared A. Barth· 3 shared E. Berntsson· 3 shared S. Paul· 3 shared F. Vosough· 2 shared M. Gielnik· 2 shared M. Kozak· 2 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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4 shared papersBiophysics

A. Graslund

Mutual co-authors in cluster

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4 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

6-gingerol interferes with amyloid-beta (Aβ) peptide aggregation

E. Berntsson, S. Paul, S. B. Sholts, J. Jarvet, A. Barth, A. Graslund, S. K. T. S. Warmlander

This study shows that 6-gingerol inhibits Aβ40 peptide aggregation in vitro without interacting with monomers, suggesting it as a potential anti-Alzheimer's compound.

bioRxiv · Jan 3, 2021Biochemistry

Lithium ions display weak interaction with amyloid-beta (Aβ) peptides and have minor effects on their aggregation

E. Berntsson, S. Paul, F. Vosough, S. B. Sholts, J. Jarvet, P. M. Roos, A. Barth, A. Graslund, S. K. T. S. Warmlander

This study investigates the interaction between lithium ions and amyloid-beta peptides, finding weak interactions and minor effects on aggregation, suggesting lithium's benefits in Alzheimer's may not stem from direct peptide interactions.

bioRxiv · Jan 3, 2021Biochemistry