Distinctive Roles of the Two ATP-binding Sites in ClpA, the ATPase Component of Protease Ti in Escherichia coli

This publication has 16 references indexed in Scilit:

• [19] Rapid and efficient site-specific mutagenesis without phenotypic selection
  Published by Elsevier ,2004
• Proteases in Escherichia coli
  Science, 1993
• Proteases and protein degradation inEscherichia coli
  Cellular and Molecular Life Sciences, 1992
• The mechanism and functions of ATP‐dependent proteases in bacterial and animal cells
  European Journal of Biochemistry, 1992
• Hspl04 is a highly conserved protein with two essential nucleotide-binding sites
  Nature, 1991
• Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La.
  Proceedings of the National Academy of Sciences, 1987
• [32] Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors
  Published by Elsevier ,1983
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• [10] Assay of inorganic phosphate, total phosphate and phosphatases
  Published by Elsevier ,1966