As a postdoctoral associate in 1997, biochemist Karolin Luger helped vault nucleosomes into the spotlight (1) when she and colleagues revealed via X-ray crystallography the three-dimensional (3D) structure of this fundamental component of chromatin, the chromosome-forming material, in eukaryotic cells (2). The nucleosome was then the largest, most complex protein-DNA assemblage ever to have been crystallized. Luger, a professor of biochemistry at the University of Colorado Boulder, continues to analyze the structure and function of chromatin, which is a mixture of DNA and proteins that forms chromosomes and shapes gene transcription, DNA replication, and DNA repair. Luger"s team has conducted seminal research on nucleosome evolutionary origins, chromosomal proteins, and chromatin remodeling factors, including enzymes that serve as targets in the treatment of cancers involving deficiencies in DNA repair through homologous recombination. Elected to the National Academy of Sciences (NAS) in 2018, Luger and colleagues (3) review findings on compounds called primary poly(ADP-ribose) polymerase (PARP) inhibitors (PARPi) in her Inaugural Article, which provides insights into the development of next-generation drugs to treat several types of cancer.
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