Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nataliia Serbyn"'
Publikováno v:
The EMBO Journal.
Publikováno v:
Cancer Research. 83:6105-6105
Genome evolution can happen gradually or via bursts of rearrangements. Chromoplexy is an example of a process driving rapid genome evolution. This mutational signature is detected in ~18% of human cancers (PCAWG Consortium, 2020) and is frequently ob
Autor:
Françoise Stutz, Huilin Zhou, Ivona Bagdiul, Raymond T. Suhandynata, Benoît Kornmann, Agnès H. Michel, Nataliia Serbyn
Publikováno v:
SSRN Electronic Journal.
SUMMARYSeveral endogenous metabolites, environmental agents, and therapeutic drugs promote formation of covalent DNA-protein crosslinks (DPCs). Persistent DPCs pose a serious threat to genome integrity and are eliminated by multiple repair pathways.
Autor:
Benoît Kornmann, Huilin Zhou, Agnès H. Michel, Nataliia Serbyn, Françoise Stutz, Audrey Noireterre, Raymond T. Suhandynata, Ivona Bagdiul
Publikováno v:
Cell Reports. 37:110034
Endogenous metabolites, environmental agents, and therapeutic drugs promote formation of covalent DNA-protein crosslinks (DPCs). Persistent DPCs compromise genome integrity and are eliminated by multiple repair pathways. Aberrant Top1-DNA crosslinks,
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-17 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-17 (2017)
Polymerase eta (Polη) is a low fidelity translesion synthesis DNA polymerase that rescues damage-stalled replication by inserting deoxy-ribonucleotides opposite DNA damage sites resulting in error-free or mutagenic damage bypass. In this study we id
Autor:
Audrey Noireterre, Françoise Stutz, Agnès H. Michel, Nataliia Serbyn, Ivona Bagdiul, Benoît Kornmann, Michael Plank, Robbie Loewith
Publikováno v:
Molecular Cell, Vol. 77, No 5 (2020) pp. 1066-1079
Molecular Cell, 77 (5)
Molecular Cell
Molecular Cell, 77 (5)
Molecular Cell
SUMMARYNaturally occurring or drug-induced DNA-protein crosslinks (DPCs) interfere with key DNA transactions if not timely repaired. The unique family of DPC-specific proteases Wss1/SPRTN targets DPC protein moieties for degradation, including topois