@inbook{0cb7774feb1b4b058266065eec6fb03b,
title = "Biochemical methods to monitor loading and activation of hexameric helicases",
abstract = "Ring-shaped hexameric helicases are an essential class of enzymes that unwind duplex nucleic acids to support a variety of cellular processes. Because of their critical roles in cells, hexameric helicase dysfunction has been linked to DNA damage and genomic instability. Biochemical characterization of hexameric helicase activity and regulation in vitro is necessary for understanding enzyme function and aiding drug discovery efforts. In this chapter, we describe protocols for characterizing mechanisms of helicase loading, activation, and unwinding using the model replicative hexameric DnaB helicase and its cognate DnaC loading factor from E. coli.",
keywords = "DNA unwinding, Helicase loading, Hexameric helicase",
author = "Fernandez, {Amy J.} and Berger, {James M.}",
note = "Funding Information: This work was supported by the NIGMS ([ R37-GM071747 ] to J.M.B. and [ T32-GM008403 ] to A.J.F.) and the NSF ([DGE-1746891] to AJF). Figures were created with Biorender. Publisher Copyright: {\textcopyright} 2022 Elsevier Inc.",
year = "2022",
month = jan,
doi = "10.1016/bs.mie.2022.03.061",
language = "English (US)",
isbn = "9780323914765",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "143--152",
editor = "Trakselis, {Michael A.}",
booktitle = "Helicase Enzymes Part A",
}