Binding Modes of Aromatic Ligands to Mammalian Heme Peroxidases with Associated Functional Implications: CRYSTAL STRUCTURES OF LACTOPEROXIDASE COMPLEXES WITH ACETYLSALICYLIC ACID, SALICYLHYDROXAMIC ACID, AND BENZYLHYDROXAMIC ACID

Eitemau Tebyg

• Structural Evidence of Substrate Specificity in Mammalian Peroxidases: STRUCTURE OF THE THIOCYANATE COMPLEX WITH LACTOPEROXIDASE AND ITS INTERACTIONS AT 2.4 Å RESOLUTION
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  Cyhoeddwyd: (2009)
• Mode of Binding of the Tuberculosis Prodrug Isoniazid to Heme Peroxidases: BINDING STUDIES AND CRYSTAL STRUCTURE OF BOVINE LACTOPEROXIDASE WITH ISONIAZID AT 2.7 Å RESOLUTION
  gan: Singh, Amit K., et al.
  Cyhoeddwyd: (2010)
• Structural evidence for the order of preference of inorganic substrates in mammalian heme peroxidases: crystal structure of the complex of lactoperoxidase with four inorganic substrates, SCN(-), I(-), Br(–) and Cl(-)
  gan: Singh, Amit K, et al.
  Cyhoeddwyd: (2011)
• Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases – structural determination of the lactoperoxidase–methimazole complex at 1.97 Å resolution
  gan: Singh, Rashmi Prabha, et al.
  Cyhoeddwyd: (2016)
• Lactoperoxidase: structural insights into the function,ligand binding and inhibition
  gan: Sharma, Sujata, et al.
  Cyhoeddwyd: (2013)