(2012). Piecing Together the Details of Bacterial DNA Gyrase Specialization♦: Mechanisms for Defining Supercoiling Set Point of DNA Gyrase Orthologs. I. A Nonconserved Acidic C-terminal Tail Modulates Escherichia coli Gyrase ActivityMechanisms for Defining Supercoiling Set Point of DNA Gyrase Orthologs. II. The Shape of the GyrA Subunit C-terminal Domain (CTD) Is Not a Sole Determinant for Controlling Supercoiling Efficiency. American Society for Biochemistry and Molecular Biology.
Citação norma ChicagoPiecing Together the Details of Bacterial DNA Gyrase Specialization♦: Mechanisms for Defining Supercoiling Set Point of DNA Gyrase Orthologs. I. A Nonconserved Acidic C-terminal Tail Modulates Escherichia Coli Gyrase ActivityMechanisms for Defining Supercoiling Set Point of DNA Gyrase Orthologs. II. The Shape of the GyrA Subunit C-terminal Domain (CTD) Is Not a Sole Determinant for Controlling Supercoiling Efficiency. American Society for Biochemistry and Molecular Biology, 2012.
MLA CitationPiecing Together the Details of Bacterial DNA Gyrase Specialization♦: Mechanisms for Defining Supercoiling Set Point of DNA Gyrase Orthologs. I. A Nonconserved Acidic C-terminal Tail Modulates Escherichia Coli Gyrase ActivityMechanisms for Defining Supercoiling Set Point of DNA Gyrase Orthologs. II. The Shape of the GyrA Subunit C-terminal Domain (CTD) Is Not a Sole Determinant for Controlling Supercoiling Efficiency. American Society for Biochemistry and Molecular Biology, 2012.