Author

G. Cornilescu

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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Assay:ChIP-seq· 3 Research Focus:chromatin & epigenetic regulation· 3 Approach:experimental assay· 3 Organism:human· 1 Approach:statistical model· 1

Frequent Co-Authors

C. M. Evans· 3 shared J. L. Markley· 3 shared K. C. Glass· 3 shared M. Phillips· 3 shared B. Demeler· 2 shared J. C. Gay· 2 shared M. Tonelli· 2 shared M. Y. Lubula· 2 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiochemistry

C. M. Evans

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3 papers

Recent·Most cited

Coordination of di-acetylated histone ligands by the ATAD2 bromodomain

C. M. Evans, M. Phillips, K. L. Malone, M. Tonelli, G. Cornilescu, C. Cornilescu, S. Holton, M. Gorjanacz, L. Wang, S. Carlson, J. C. Gay, J. C. Nix, B. Demeler, J. L. Markley, K. C. Glass

This study identifies how the ATAD2 bromodomain recognizes di-acetylated histone tails through residue-specific interactions and confirms its monomeric state using biophysical techniques.

bioRxiv · Jul 23, 2021Biochemistry

Structural insights into the recognition of mono- and di-acetylated histones by the ATAD2B bromodomain

J. T. Lloyd, K. McLaughlin, M. Y. Lubula, J. C. Gay, A. Dest, C. Gao, M. Phillips, M. Tonelli, G. Cornilescu, M. R. Marunde, C. M. Evans, S. P. Boyson, S. Carlson, M.-C. Keogh, J. L. Markley, , K. C. Glass

This study investigates the ligand specificity of the ATAD2B bromodomain, showing it binds mono- and di-acetylated histones and identifies structural features critical for this recognition.

bioRxiv · May 12, 2020 · PreprintBiochemistry

The BRPF1 bromodomain is a molecular reader of di-acetyllysine

J. O. Obi, M. Y. Lubula, G. Cornilescu, A. Henrickson, K. McGuire, C. M. Evans, M. Phillips, S. P. Boyson, B. Demeler, J. L. Markley, K. C. Glass

This study identifies the BRPF1 bromodomain as a selective reader of di-acetyllysine modifications on histone H4 and characterizes its binding preferences and mechanisms.

bioRxiv · Feb 13, 2020Biochemistry