Karolin Luger

About

Karolin Luger is a professor involved in the field of structural biology, with a focus on chromatin structure and dynamics. Her research encompasses the study of chromatin and histone proteins, exploring their roles in genome organization and regulation. The lab employs a variety of techniques including cryo-electron microscopy, X-ray crystallography, and biophysics to investigate the structural and mechanistic aspects of chromatin and related proteins. Her work aims to deepen understanding of how chromatin components interact and function, contributing to the broader knowledge of genome regulation and stability.

Research topics

• Biology
• Computer Science
• Genetics
• Cell biology
• Biophysics
• Computational biology
• Biochemistry

Selected publications

• Inhibitors of PARP: Number crunching and structure gazing

  Proceedings of the National Academy of Sciences · 2022 · 115 citations

  Senior authorCorresponding

  ). This review about inhibitors of PARP (PARPi) is for readers interested in the development of next-generation drugs for the treatment of cancer, providing insights into structure-activity relationships, in vitro vs. in vivo potency, PARP trapping, and synthetic lethality.

  DOI

• Virus-encoded histone doublets are essential and form nucleosome-like structures

  Cell · 2021 · 104 citations

  Senior authorCorresponding
  DOI

• The BRCT domain of PARP1 binds intact DNA and mediates intrastrand transfer

  Molecular Cell · 2021 · 93 citations

  Senior authorCorresponding
  DOI

• Histones with an unconventional DNA-binding mode in vitro are major chromatin constituents in the bacterium Bdellovibrio bacteriovorus

  Nature Microbiology · 2023-10-09 · 51 citations

  articleOpen accessCorresponding

  Histone proteins bind DNA and organize the genomes of eukaryotes and most archaea, whereas bacteria rely on different nucleoid-associated proteins. Homology searches have detected putative histone-fold domains in a few bacteria, but whether these function like archaeal/eukaryotic histones is unknown. Here we report that histones are major chromatin components in the bacteria Bdellovibrio bacteriovorus and Leptospira interrogans. Patterns of sequence evolution suggest important roles for histones…

  PublisherOA PDFDOI

• Slow Dissociation from the PARP1–HPF1 Complex Drives Inhibitor Potency

  Biochemistry · 2023-08-02 · 18 citations

  articleOpen access

  PARP1, upon binding to damaged DNA, is activated to perform poly ADP-ribosylation (PARylation) on itself and other proteins, which leads to relaxation of chromatin and recruitment of DNA repair factors. HPF1 was recently discovered as a protein cofactor of PARP1 that directs preferential PARylation of histones over other targets by contributing to and altering the PARP1 active site. Inhibitors of PARP1 (PARPi) are used in the treatment of BRCA–/– cancers, but the basis for their potency in cells…

  PublisherDOI

Recent grants

• NIH Grant R01GM067777

  NIH · $3.7M · 2017

• NIH Grant P01GM088409

  NIH · $14.1M · 2016

• Structure and Mechanism of Chromatin-Bound PARP1

  NIH · $3.8M · 2017–2027

Frequent coauthors

• Uma M. Muthurajan

  University of Colorado Boulder

  70 shared

• Samuel Bowerman

  University of Colorado Boulder

  58 shared

• Johannes Rudolph

  University of Colorado Boulder

  52 shared

• Joel Gottesfeld

  Scripps Research Institute

  38 shared

• Aaron R. Hieb

  38 shared

• Yajie Gu

  University of California, San Diego

  31 shared

• Jyothi Mahadevan

  31 shared

• Andrew J. Andrews

  31 shared

Labs

• Luger LabPI

Similar researchers at University of Colorado Boulder

• Kristi S. Ansethh-159
• Thomas R. Cechh-156
• Leslie A. Leinwandh-115