Author

J. S. Nowak

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

D. E. Otzen· 2 shared A. Abelein· 1 shared A. Farzadfard· 1 shared H. Biverstal· 1 shared H. Klute· 1 shared J. Johansson· 1 shared J. Nielsen· 1 shared L. Adam· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiophysics

D. E. Otzen

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2 papers

Recent·Most cited

Specific inhibition of α-synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS

L. Adam, R. Kumar, L. E. Arroyo-Garcia, W. H. Molenkamp, J. S. Nowak, H. Klute, A. Farzadfard, R. Alkenayeh, J. Nielsen, H. Biverstal, D. E. Otzen, J. Johansson, A. Abelein

This study shows that the Bri2 BRICHOS domain inhibits α-synuclein oligomer formation and toxicity by suppressing secondary nucleation and binding oligomers, suggesting its potential as a therapeutic target for Parkinson's disease.

bioRxiv · Dec 7, 2023Biophysics

Quantitating denaturation by formic acid: Imperfect repeats are essential to the stability of the functional amyloid protein FapC

L. F. B. Christensen, J. S. Nowak, T. V. Sonderby, S. A. Frank, D. E. Otzen

The paper quantifies how formic acid denatures functional amyloid FapC and shows that imperfect repeats are essential for fibril stability.

bioRxiv · Mar 9, 2020Biophysics