The effects of phosphorylation on the structure and function of proteins.
Johnson
L N
LN
Laboratory of Molecular Biophysics, University of Oxford, United Kingdom.
Barford
D
D
D000495:Allosteric Site; D000595:Amino Acid Sequence; D000818:Animals; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins; D001665:Binding Sites; D002633:Chemotaxis; D004926:Escherichia coli / Q000201:enzymology; D007521:Isocitrate Dehydrogenase / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D008961:Models, Structural; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism*; D006005:Phosphorylases / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D010750:Phosphoproteins; D011506:Proteins; D007521:Isocitrate Dehydrogenase; D006005:Phosphorylases; D011494:Protein Kinases; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System