This novel dual nature of AMN107 Src-bcr-Abl inhibitor ketaminazole, possessing both anti-fungal and antiinflammatory activity, could potentially have therapeutic uses against fungal infections that have an anti-inflammatory component. The genome of mammalian cells is under constant threat from both endogenous and exogenous DNA damaging agents that can introduce mutagenic and cytotoxic DNA lesions. For example, it has been estimated that spontaneous depurination events result in more than 10,000 abasic lesions per mammalian cell per day. Left unrepaired, DNA damage can result in detrimental biological consequences to the organism, including cell death and mutations that drive transformation to malignancy. Cells use various DNA repair systems as defenses to protect their genomes from DNA damaging agents and to maintain genome stability. Not surprisingly, cells with a defect in one of their DNA repair mechanisms are typically more sensitive to certain genotoxic agents and suffer increased mutagenesis. Most antitumor drugs induce DNA lesions that ultimately block or interfere with DNA replication in rapidly dividing Temozolomide cancer cells, resulting in increased susceptibility to activation of various programmed cell death responses. An elevated DNA repair capacity in tumor cells results in anticancer drug and radiation resistance, severely limiting the efficacy of these agents. Recent basic and clinical studies have demonstrated emerging concept designs to block the functions of various proteins in specific DNA repair pathways, which would sensitize cancer cells to DNA damaging agents and potentially lead to an improved therapeutic outcome. The base excision repair pathway is responsible for correcting damage to single DNA bases or to the sugar moiety of the phosphodiester backbone. Typically, the BER process starts with the enzymatic removal of a damaged base by either a monoor a bi-functional DNA glycosylase, which creates an abasic site or in some instances a DNA strand break. The AP site is incised by an essential enzyme known as apurinic/apyrimidinic endonuclease-1, which generates a single-stranded gap in DNA with 39-hydroxyl and 59-deoxyribosephosphate termini. This gap is filled in and ultimately sealed by the concerted action of DNA polymerases and ligases. In mammalian cells, APE1 is responsible for at least 95% of the endonuclease activity that incises at abasic sites as part of the short-patch and long-patch BER subpathways. APE1 has been found not only to be required for animal viability, as deletion of both alleles of the APE1 gene in mice leads to embryonic lethality, but also for cell viability in culture.