Author

D. Sulskis

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· 4 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Approach:biophysical modeling· 1 Organism:E. coli· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

A. Sakalauskas· 3 shared M. Ziaunys· 3 shared V. Smirnovas· 3 shared K. Mikalauskaite· 2 shared R. Snieckute· 2 shared A. Kopustas· 1 shared B. M. Burmann· 1 shared D. Veiveris· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

A. Sakalauskas

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

S100A9 Inhibits and Redirects Prion Protein 89-230 Fragment Amyloid Aggregation

M. Ziaunys, D. Sulskis, K. Mikalauskaite, A. Sakalauskas, R. Snieckute, V. Smirnovas

This study investigates how S100A9 interacts with prion protein 89-230 fragment, showing it modulates aggregation pathways and inhibits nucleation.

bioRxiv · Feb 6, 2024Biochemistry

Liquid-liquid Phase Separation of Alpha-synuclein Increases the Structural Variability of Fibrils Formed during Amyloid Aggregation

M. Ziaunys, D. Sulskis, D. Veiveris, A. Kopustas, R. Snieckute, K. Mikalauskaite, A. Sakalauskas, M. Tutkus, V. Smirnovas

This study compares alpha-synuclein aggregation under conditions that promote or negate liquid-liquid phase separation, showing that phase separation leads to more structurally variable and toxic fibrils.

bioRxiv · Dec 28, 2023Biophysics

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.

bioRxiv · May 31, 2023 · PreprintBiochemistry

Structural basis of DegP-protease temperature-dependent activation

D. Sulskis, J. Thoma, B. M. Burmann

This study identifies a temperature-dependent molecular lock in DegP PDZ domains that regulates its structural transition and proteolytic activity.

Science Advances · Dec 10, 2021Peer-reviewedBiophysics