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• W2058703060 endingPage "26" @default.
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• W2058703060 abstract "Fanconi anemia (FA) is a rare autosomal recessive or X-linked disorder characterized by aplastic anemia, cancer susceptibility and cellular sensitivity to DNA-crosslinking agents. Eight FA proteins (FANCA, -B, -C, -E, -F, -G, -L and -M) and three non-FA proteins (FAAP100, FAAP24 and HES1) form the FA nuclear core complex that is required for monoubiquitination of the FANCD2–FANCI dimer upon DNA damage. The other three FA proteins, FANCD1/BRCA2, FANCJ/BACH1/BRIP1 and FANCN/PALB2, act in parallel or downstream of the FANCD2–FANCI dimer. Despite the isolation and characterization of several FA proteins, the mechanism by which these proteins protect cells from DNA interstrand crosslinking agents has been unclear. This is because a majority of the FA proteins lack any recognizable functional domains that can provide insight into their function. The recently discovered FANCM (Hef) and FANCJ (BRIP1/BACH1) proteins contain helicase domains, providing potential insight into the role of FA proteins in DNA repair. FANCM with its partner, FAAP24, and FANCJ bind and metabolize a variety of DNA substrates. In this review, we focus on the discovery, structure, and function of the FANCM–FAAP24 and FANCJ proteins." @default.
• W2058703060 created "2016-06-24" @default.
• W2058703060 creator A5005999934 @default.
• W2058703060 creator A5061968490 @default.
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• W2058703060 date "2009-07-01" @default.
• W2058703060 modified "2023-09-29" @default.
• W2058703060 title "FANCM–FAAP24 and FANCJ: FA proteins that metabolize DNA" @default.
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• W2058703060 doi "https://doi.org/10.1016/j.mrfmmm.2009.04.002" @default.
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