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Jonathan Barroso-Gonzalez on Muck Rack

Jonathan Barroso-Gonzalez

As seen in: Cell Reports, Cell Press
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Articles

Anti-recombination function of MutSα restricts telomere extension by ALT-associated homology-directed repair

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By Jonathan Barroso-Gonzalez, Laura Garcia-Exposito, Bioinformatics Unit, Pablo Galaviz
| Cell Reports Verified
Highlights • Loss of MutSα mismatch repair complex causes telomere hyper-extension by ALT pathway • MutSα counteracts BLM and limits premature initiation of telomere extension • Simultaneous loss of MutSα and BLM leads to cell death Summary Alternative lengthening of telomeres (ALT) is a telomere-elongation mechanism observed in ∼15% of cancer subtypes. Current models indicate that ALT is mediated by homology-directed repair mechanisms.
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RAD51AP1 Is an Essential Mediator of Alternative Lengthening of Telomeres

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By Jonathan Barroso-Gonzalez, Laura Garcia-Exposito, Michelle L. Lynskey, Justin L. Roncaioli
| Cell Press Verified
(Molecular Cell 76, 11–26.e1–e7; October 3, 2019) Visiting international student Marco de Vitis generated data for this article but was inadvertently omitted from the author list. The co-authors have requested that Dr. de Vitis be added, and this change has now been effected. The authors regret this error and apologize for the miscommunication. Article Info Identification DOI: https://doi.org/10.1016/j.molcel.2020.06.026 Copyright © 2020 Elsevier Inc.
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RAD51AP1 Is an Essential Mediator of Alternative Lengthening of Telomeres

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By Jonathan Barroso-Gonzalez, Laura Garcia-Exposito, Michelle L. Lynskey, Justin L. Roncaioli
| Cell Press Verified
(Molecular Cell 76, 11–26.e1–e7; October 3, 2019) In Figure 4A of the originally published article, the labels for Beclin-1 and pBeclin-1 S15 mistakenly appeared in reverse order. Figure 4A has now been corrected online and appears below. The authors regret the error. Article Info Identification DOI: https://doi.org/10.1016/j.molcel.2019.08.009 Copyright © 2019 Elsevier Inc.
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