IndraLab

Statements


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"Usp1 modulates DNA replication, polymerase choice and DNA repair by PCNA and as a result Usp1 knock-out mice are genetically unstable and hypersensitive to DNA damage [XREF_BIBR], [XREF_BIBR]."

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"As another example of genes involved in DNA damage, Usp1 is a key modulator of DNA repair, partly through de-ubiquitination of its known targets such as FANCD2 (Oestergaard et al., 2007) and PCNA (T. T. Huang et al., 2006)."

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"Because CHK1 is a cell cycle regulated and DNA damage checkpoint protein, we asked whether (a) the downregulation of CHK1 in USP1 depleted cells is an experimental artefact resulting from modifications of the cell cycle and/or altered DNA repair capabilities caused by USP1 depletion and (b) USP1 depletion modifies the G2 checkpoint in response to DNA damage."

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"These results suggest that inhibition of the expression of USP1 has great potential to inhibit DNA repair, leading to increased DNA damage originated from DNA alkylating agents such as cisplatin, and ultimately enhancing the anti-tumor effect.Subsequently, we verified that a selective USP1i of C527 in combination of cisplatin showed obvious synergistic anti-tumor effect, which holds great promise for further combination therapy."

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"Blockade of Deubiquitylating Enzyme USP1 Inhibits DNA Repair and Triggers Apoptosis in Multiple Myeloma Cells."

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"Inhibition of USP1 by small molecule inhibitors disrupts DNA repair and replication and is being pursued as a potential anticancer therapeutic in BRCA1/2 mutant cancers."

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"The USP1 protein leads to regulated DNA repair through deubiquitination and homologous recombination pathways, and inhibits cell differentiation by stabilizing tumor-promoting inhibitors of DNA-binding proteins."

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"As another example of genes involved in DNA damage , Usp1 is a key modulator of DNA repair , partly through de-ubiquitination of its known targets such as FANCD2 ( Oestergaard et al ., 2007 ) and PCNA ( T. T. Huang et al ., 2006 ) ."

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"The deubiquitinating enzyme, USP1 is known to promote DNA repair via complexing with UAF1."

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"De-ubiquitination of the monoubiquitinated ID2 complex by USP1-UAF1 stimulates its unloading from chromatin and knockdown of USP1 impairs subsequent DNA repair steps ."