Gina Arents

The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.

Gina Arents, Rufus W. Burlingame, B.-C. Wang et al. · Proceedings of the National Academy of Sciences · 1991 · 734 citations

The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization.

Gina Arents, Evangelos N. Moudrianakis · Proceedings of the National Academy of Sciences · 1995 · 352 citations · Full text

Protein Assembly, Biomolecular Structure Prediction, Structural Bioinformatics +23

Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA.

Gina Arents, Evangelos N. Moudrianakis · Proceedings of the National Academy of Sciences · 1993 · 335 citations

Dna, Epigenetic Change, Molecular Biology +22

Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription.

Warren D. Kruger, Craig L. Peterson, Anita Sil et al. · Genes & Development · 1995 · 243 citations · Full text

Histone Modifications, Ho Gene, Epigenetic Change +21

An Asymmetric Model for the Nucleosome: A Binding Site for Linker Histones Inside the DNA Gyres

Dmitry Pruss, Blaine Bartholomew, Jim Persinger et al. · Science · 1996 · 235 citations

Protein Superhelix, Epigenetic Change, Molecular Biology +21