RecQ and Fe–S helicases have unique roles in DNA metabolism dictated by their unwinding directionality, substrate specificity, and protein interactions
Author:
Affiliation:
1. Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, NIH Biomedical Research Center, 251 Bayview Blvd, Baltimore, MD 21224, U.S.A.
Abstract
Publisher
Portland Press Ltd.
Subject
Biochemistry
Link
https://portlandpress.com/biochemsoctrans/article-pdf/46/1/77/433117/bst-2017-0044c.pdf
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3. Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5;Newman;Nucleic Acids Res.,2017
4. Structural mechanisms of DNA binding and unwinding in bacterial RecQ helicases;Manthei;Proc. Natl Acad. Sci. U.S.A.,2015
5. Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes;Newman;Nucleic Acids Res.,2015
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