Binding of the Catabolite Repressor Protein CcpA to Its DNA Target Is Regulated by Phosphorylation of its Corepressor HPr

This publication has 38 references indexed in Scilit:

• Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signals
  Journal of Molecular Biology, 1997
• The Domain Organization of Human Topoisomerase I
  Journal of Biological Chemistry, 1996
• Phosphorylation of serine‐46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure
  Protein Science, 1995
• NMRPipe: A multidimensional spectral processing system based on UNIX pipes
  Journal of Biomolecular NMR, 1995
• Specific recognition of the Bacillus subtilis gnt cis‐acting catabolite‐responsive element by a protein complex formed between CcpA and seryl‐phosphorylated HPr
  Molecular Microbiology, 1995
• High-resolution Structure of the Phosphorylated Form of the Histidine-containing Phosphocarrier Protein HPr fromEscherichia coliDetermined by Restrained Molecular Dynamics from NMR-NOE Data
  Journal of Molecular Biology, 1995
• Possible function and some properties of the CcpA protein of Bacillus subtilis
  Microbiology, 1994
• The NMR determination of the IIA^mtl binding site on HPr of the Escherichia coli phosphoenol pyruvate‐dependent phosphotransferase system
  FEBS Letters, 1993
• The MIDAS display system
  Journal of Molecular Graphics, 1988
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970