Publication: PARP1 proximity proteomics reveals interaction partners at stressed replication forks
PARP1 proximity proteomics reveals interaction partners at stressed replication forks
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Mosler, T., Baymaz, H. I., Gräf, J. F., Mikicic, I., Blattner, G., Bartlett, E., Ostermaier, M., Piccinno, R., Yang, J., Voigt, A., Gatti, M., Pellegrino, S., Altmeyer, M., Luck, K., Ahel, I., Roukos, V., & Beli, P. (2022). PARP1 proximity proteomics reveals interaction partners at stressed replication forks. Nucleic Acids Research, 50, 11600–11618. https://doi.org/10.1093/nar/gkac948
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PARP1 mediates poly-ADP-ribosylation of proteins on chromatin in response to different types of DNA lesions. PARP inhibitors are used for the treatment of BRCA1/2-deficient breast, ovarian, and prostate cancer. Loss of DNA replication fork protection is proposed as one mechanism that contributes to the vulnerability of BRCA1/2-deficient cells to PARP inhibitors. However, the mechanisms that regulate PARP1 activity at stressed replication forks remain poorly understood. Here, we performed proximity proteomics of PARP1 and isolation of
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Mosler, T., Baymaz, H. I., Gräf, J. F., Mikicic, I., Blattner, G., Bartlett, E., Ostermaier, M., Piccinno, R., Yang, J., Voigt, A., Gatti, M., Pellegrino, S., Altmeyer, M., Luck, K., Ahel, I., Roukos, V., & Beli, P. (2022). PARP1 proximity proteomics reveals interaction partners at stressed replication forks. Nucleic Acids Research, 50, 11600–11618. https://doi.org/10.1093/nar/gkac948