Author

S. Korolev

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· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Assay:protein structure· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

C. M. Jenkins· 1 shared G. Dellaire· 1 shared I. Miller· 1 shared J. B. Hopkins· 1 shared J. Deveryshetty· 1 shared J. M. Redington· 1 shared J.-Y. Masson· 1 shared K. R. Malley· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiochemistry

C. M. Jenkins

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.

Y. Kyriukha, M. B. Watkins, J. M. Redington, R. Dastvan, V. N. Uversky, J. B. Hopkins, N. Pozzi, S. Korolev

This study identifies the PALB2 DNA-binding domain as an intrinsically disordered region that promotes DNA compaction through oligomerization, revealing a novel strand exchange mechanism.

bioRxiv · Jun 1, 2023Biophysics

Novel strand exchange activity of the human PALB2 DNA Binding Domain and its critical role for DNA repair in cells

J. Deveryshetty, M. Ryzhikov, N. Brahati, T. Peterlini, G. Dellaire, J.-Y. Masson, S. Korolev

The paper identifies a DNA-binding domain in PALB2 that enhances RAD51-mediated DNA repair and can promote strand exchange independently of RAD51.

bioRxiv · Jan 8, 2019Biochemistry

A novel dimeric active site and regulation mechanism revealed by the crystal structure of iPLA2β

K. R. Malley, O. Koroleva, I. Miller, R. Sanishvili, C. M. Jenkins, R. W. Gross, S. Korolev

The paper presents the first crystal structure of iPLA2β, revealing a dimeric active site and regulation mechanism that could inform therapeutic inhibitor development.

bioRxiv · Sep 29, 2017Biochemistry