Author

Agnieszka Michaś

Institute of PhysicsORCID 0000-0002-7005-4368Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

Anna Niedźwiecka-KornaśiD· 3 shared Barbara P. KlepkaiD· 2 shared Maja K. Cieplak-RotowskaiD· 1 shared Michał DadleziD· 1 shared Michał K. BiałobrzewskiiD· 1 shared Michał WojciechowskiiD· 1 shared Nahum SonenbergiD· 1 shared Radost WaszkiewicziD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiophysics

Anna Niedźwiecka-KornaśORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

GW182 silencing domain engages the tristetraprolin-binding pocket of CNOT1 to recruit CNOT1 into multiprotein condensates

Michał K. Białobrzewski, Maja K. Cieplak-Rotowska, A Stelmachowska, Zuzanna Staszałek, Nahum Sonenberg, Michał Dadlez, Anna Niedźwiecka-Kornaś

The paper identifies a shared CNOT1 binding site used by GW182 and TTP, revealing SLiM-mediated competition in CCR4-NOT complex recruitment.

bioRxiv · Jul 17, 2026 · PreprintBiophysics

Guiding calcium carbonate formation via liquid phase separation of extremely charged coral protein AGARP

Barbara P. Klepka, Agnieszka Michaś, Tomasz Wojciechowski, Anna Niedźwiecka-Kornaś

This study shows that AGARP, a coral protein, influences calcium carbonate nucleation and growth through liquid-liquid phase separation, forming a protein-calcium condensate as a crystallization precursor.

Small · Sep 24, 2025Peer-reviewedBiophysics

Electrostatic Collapse of Intrinsically Disordered Acid-Rich Protein Is Sensitive to Counterion Valency

Barbara P. Klepka, Radost Waszkiewicz, Michał Wojciechowski, Agnieszka Michaś, Anna Niedźwiecka-Kornaś

This study investigates how counterion valency affects the electrostatic collapse of an intrinsically disordered protein, showing divalent cations induce greater compaction than monovalent cations.

bioRxiv · Jul 9, 2025 · PreprintBiophysics