Protein-protein interaction revealed by NMR T2 relaxation experiments: the lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus

This publication has 43 references indexed in Scilit:

• Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
  Nature Structural & Molecular Biology, 1999
• Kinetics and specificity of reductive acylation of wild‐type and mutated lipoyl domains of 2‐oxo‐acid dehydrogenase complexes from Azotobacter vinelandii
  European Journal of Biochemistry, 1998
• Solution Structure of the Lipoyl Domain of the 2-Oxoglutarate Dehydrogenase Complex fromAzotobacter vinelandii
  Journal of Molecular Biology, 1996
• Three-dimensional structure of a lipoyl domain fromthe dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
  Journal of Molecular Biology, 1995
• Three-dimensional Structure of the Lipoyl domain from Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex
  Journal of Molecular Biology, 1993
• Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible
  Biochemistry, 1992
• Interactions of lipoyl domains with the E1p subunits of the pyruvate dehydrogenase multienzyme complex from Escherichiacoli
  FEBS Letters, 1990
• A common structural motif in thiamin pyrophosphate‐binding enzymes
  FEBS Letters, 1989
• Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes
  Biochemistry, 1989
• Rapid intramolecular coupling of active sites in the pyruvate dehydrogenase complex of Escherichia coli : Mechanism for rate enhancement in a multimeric structure
  Proceedings of the National Academy of Sciences, 1978