Author

J. Palinkas

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Research Focus:chromatin & epigenetic regulation· 2 Organism:E. coli· 2 Organism:human· 2 Assay:protein structure· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

G. M. Harami· 3 shared M. Kovacs· 3 shared Z. J. Kovacs· 3 shared G. Szakacs· 2 shared H. Harami-Papp· 2 shared J. Hegedüs· 2 shared K. Tarnok· 2 shared L. Mahmudova· 2 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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3 shared papersBiochemistry

G. M. Harami

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3 papers

Recent·Most cited

DNA-dependent phase separation by human SSB2 (NABP1/OBFC2A) protein points to adaptations to eukaryotic genome repair processes

Z. J. Kovacs, G. M. Harami, J. Palinkas, N. Kuljanishvili, J. Hegedüs, H. Harami-Papp, L. Mahmudova, L. Khamisi, G. Szakacs, M. Kovacs

This study shows human SSB2 forms phase separation condensates requiring ssDNA binding, revealing evolutionary adaptations in genome repair mechanisms compared to E. coli SSB.

bioRxiv · Sep 15, 2023Biochemistry

Redox-dependent condensation and cytoplasmic granulation by human ssDNA binding protein 1 delineate roles in oxidative stress response

G. M. Harami, J. Palinkas, Z. J. Kovacs, B. Jezso, K. Tarnok, H. Harami-Papp, J. Hegedüs, L. Mahmudova, N. Kucsma, S. Toth, G. Szakacs, M. Kovacs

This study shows hSSB1 undergoes redox-dependent LLPS to form cytoplasmic granules involved in oxidative stress response and genome repair.

bioRxiv · Jul 25, 2023Biochemistry

Phase separation by ssDNA binding protein controlled via protein-protein and protein-DNA interactions

G. M. Harami, Z. J. Kovacs, R. Pancsa, J. Palinkas, V. Barath, K. Tarnok, A. Malnasi-Csizmadia, M. Kovacs

This study shows that E. coli SSB forms liquid-liquid phase-separated condensates through interactions with ssDNA and other proteins, enabling rapid mobilization for DNA repair.

bioRxiv · Nov 20, 2019Biochemistry