Characterization of a conserved α-helical, coiled-coil motif at the C-terminal domain of the ATP-dependent FtsH (HflB) protease of Escherichia coli 1 1Edited by J. Karn

This publication has 54 references indexed in Scilit:

• Self-Processing of FtsH and Its Implication for the Cleavage Specificity of This Protease
  Biochemistry, 1999
• Roles of the Periplasmic Domain of Escherichia coliFtsH (HflB) in Protein Interactions and Activity Modulation
  Published by Elsevier ,1998
• The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
  The EMBO Journal, 1998
• Polypeptide binding of Escherichia coli FtsH (HflB)
  Molecular Microbiology, 1998
• The Proteasome: Paradigm of a Self-Compartmentalizing Protease
  Cell, 1998
• Processive Degradation of Proteins and Other Catalytic Properties of the Proteasome from Thermoplasma acidophilum
  Journal of Biological Chemistry, 1997
• Subunit a of proton ATPase F₀ sector is a substrate of the FtsH protease in Escherichia coli
  FEBS Letters, 1996
• Structure and mechanism of DNA topoisomerase II
  Nature, 1996
• FtsH, a Membrane-bound ATPase, Forms a Complex in the Cytoplasmic Membrane of Escherichia coli
  Journal of Biological Chemistry, 1995
• Translational regulatory signals within the coding region of the bacteriophage lambda cIII gene
  Journal of Bacteriology, 1986