Author

G. Szakacs

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 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

G. M. Harami· 2 shared H. Harami-Papp· 2 shared J. Hegedüs· 2 shared J. Palinkas· 2 shared L. Mahmudova· 2 shared M. Kovacs· 2 shared Z. J. Kovacs· 2 shared A. Schamberger· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersBiochemistry

G. M. Harami

Mutual co-authors in cluster

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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

Nucleotide binding is the critical regulator of ABCG2 conformational transitions

Z. Gyöngy, G. Mocsar, E. Hegedus, T. Stockner, Z. Ritter, L. Homolya, A. Schamberger, T. I. Orban, J. Remenyik, G. Szakacs, K. Goda

This study investigates how nucleotide binding regulates conformational transitions in ABCG2, showing it induces the inward-to-outward facing switch and interacts with substrate binding.

bioRxiv · Oct 19, 2022Biochemistry