about
DNA end resection by CtIP and exonuclease 1 prevents genomic instabilityCDK targets Sae2 to control DNA-end resection and homologous recombinationDeficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes cells to interstrand crosslinking agentsHuman CtIP promotes DNA end resectionControlling DNA-End Resection: An Emerging Task for Ubiquitin and SUMOCullin3-KLHL15 ubiquitin ligase mediates CtIP protein turnover to fine-tune DNA-end resectionRIF1 is essential for 53BP1-dependent nonhomologous end joining and suppression of DNA double-strand break resection.Pa-AGOG, the founding member of a new family of archaeal 8-oxoguanine DNA-glycosylases.γ-Radiation promotes immunological recognition of cancer cells through increased expression of cancer-testis antigens in vitro and in vivoAPC/C(Cdh1) controls CtIP stability during the cell cycle and in response to DNA damage.Carcinogenic bacterial pathogen Helicobacter pylori triggers DNA double-strand breaks and a DNA damage response in its host cellsCtIP-dependent DNA resection is required for DNA damage checkpoint maintenance but not initiation.Controlling DNA-end resection: a new task for CDKs.MRE11 complex links RECQ5 helicase to sites of DNA damage.HELQ promotes RAD51 paralogue-dependent repair to avert germ cell loss and tumorigenesis.Activation of ATR-Chk1 pathway facilitates EBV-mediated transformation of primary tonsillar B-cells.Targeting DNA double-strand break signalling and repair: recent advances in cancer therapy.Differential DNA repair pathway choice in cancer cells after proton- and photon-irradiation.miR-19, a component of the oncogenic miR-17∼92 cluster, targets the DNA-end resection factor CtIP.FANCD2 and CtIP cooperate to repair DNA interstrand crosslinks.Prolyl isomerase PIN1 regulates DNA double-strand break repair by counteracting DNA end resection.A novel uracil-DNA glycosylase with broad substrate specificity and an unusual active site.FAN1 interaction with ubiquitylated PCNA alleviates replication stress and preserves genomic integrity independently of BRCA2An iron-sulfur cluster in the family 4 uracil-DNA glycosylases.The ubiquitin ligase APC/C(Cdh1) puts the brakes on DNA-end resection.Prolyl isomerization: a new PIN code for DSB repair.Biochemical characterization of uracil processing activities in the hyperthermophilic archaeon Pyrobaculum aerophilum.Direct interaction between uracil-DNA glycosylase and a proliferating cell nuclear antigen homolog in the crenarchaeon Pyrobaculum aerophilum.Enzymology of base excision repair in the hyperthermophilic archaeon Pyrobaculum aerophilum.A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure.Author Correction: FAN1 interaction with ubiquitylated PCNA alleviates replication stress and preserves genomic integrity independently of BRCA2.Deficiency in homologous recombination renders Mammalian cells more sensitive to proton versus photon irradiation.A short BRCA2-derived cell-penetrating peptide targets RAD51 function and confers hypersensitivity towards PARP inhibition.Targeting p38α Increases DNA Damage, Chromosome Instability, and the Anti-tumoral Response to Taxanes in Breast Cancer Cells.CtIP-Mediated Fork Protection Synergizes with BRCA1 to Suppress Genomic Instability upon DNA Replication StressNoncanonical Mismatch Repair as a Source of Genomic Instability in Human CellsIdentification of a miniature Sae2/Ctp1/CtIP ortholog from Paramecium tetraurelia required for sexual reproduction and DNA double-strand break repairContext Matters: RNF168 Connects with PALB2 to Rewire Homologous Recombination in BRCA1 Haploinsufficiency
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description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Alessandro A Sartori
@ast
Alessandro A Sartori
@en
Alessandro A Sartori
@es
Alessandro A Sartori
@nl
type
label
Alessandro A Sartori
@ast
Alessandro A Sartori
@en
Alessandro A Sartori
@es
Alessandro A Sartori
@nl
altLabel
Alex Sartori
@en
prefLabel
Alessandro A Sartori
@ast
Alessandro A Sartori
@en
Alessandro A Sartori
@es
Alessandro A Sartori
@nl
P106
P21
P31
P496
0000-0003-2770-0333