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Andreas Sturzenegger

Researcher at University of Zurich

Publications -  5
Citations -  395

Andreas Sturzenegger is an academic researcher from University of Zurich. The author has contributed to research in topics: DNA repair & Replication protein A. The author has an hindex of 5, co-authored 5 publications receiving 338 citations. Previous affiliations of Andreas Sturzenegger include Academy of Sciences of the Czech Republic.

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Journal ArticleDOI

DNA2 Cooperates with the WRN and BLM RecQ Helicases to Mediate Long-range DNA End Resection in Human Cells

TL;DR: Evidence is presented that WRN and BLM act epistatically with DNA2 to promote the long-range resection of double strand break ends in human cells and new mechanistic insights are provided into the process of DNA end resection in mammalian cells.
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Mechanistic insight into the interaction of BLM helicase with intra-strand G-quadruplex structures.

TL;DR: It is shown that the activity of BLM is substrate dependent, and highly regulated by a short ssDNA segment that separates the G4 motif from dsDNA, and a model is presented that proposes a unique role for G4 structures in modulating theActivity of DNA processing enzymes.
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The MMS22L–TONSL heterodimer directly promotes RAD51‐dependent recombination upon replication stress

TL;DR: By specifically regulating RAD51 activity at uncoupled replication forks, MMS22L–TONSL stabilizes perturbed replication forks by promoting replication fork reversal and stimulating their HR‐mediated restart in vivo.
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Human RECQ5 helicase promotes repair of DNA double-strand breaks by synthesis-dependent strand annealing

TL;DR: It is suggested that RECQ5 acts during the post-synaptic phase of synthesis-dependent strand annealing to prevent formation of aberrant RAD51 filaments on the extended invading strand, thus limiting its channeling into potentially hazardous crossover pathway of HR.
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The Mismatch-Binding Factor MutSβ Can Mediate ATR Activation in Response to DNA Double-Strand Breaks

TL;DR: It is suggested that hairpin loops might form in ssDNA generated at sites of DNA damage and trigger ATR activation in a process mediated by MutSβ.