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- W2893566652 abstract "Abstract The RecQ family represents one of the most highly conserved groups of 3′–5′ DNA helicases essential for maintaining genomic stability in all kingdoms of life. Besides a core helicase domain that couples nucleotide hydrolysis to DNA unwinding, many RecQ helicases also contain additional conserved domains which are implicated in lending unique functional characteristics to each helicase. Present in the majority of RecQ-like helicases, C-terminal to the conserved helicase domain is the RQC domain which is composed of a zinc-binding domain and a helix-turn-helix fold called winged-helix domain. Here, we compare and contrast the structure and functions of zinc-binding domain of Escherichia coli RecQ and the human RecQ homologs. Such systematic analyses help illustrate the relationship between multiple RecQ helicases elucidating specialized functions of individual RecQ proteins and recognizing fundamental similarities among the various RecQ homologs." @default.
- W2893566652 created "2018-10-05" @default.
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- W2893566652 date "2019-01-01" @default.
- W2893566652 modified "2023-09-25" @default.
- W2893566652 title "Role of Zinc-Binding Domains of RecQ Helicases" @default.
- W2893566652 doi "https://doi.org/10.1016/b978-0-12-814685-9.00011-7" @default.
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