Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer.

Podobne knjige/članki

• Overexpression of neuronal nitric oxide synthase in insect cells reveals requirement of haem for tetrahydrobiopterin binding.
  od: List, B M, et al.
  Izdano: (1996)
• Delineation of the arginine- and tetrahydrobiopterin-binding sites of neuronal nitric oxide synthase.
  od: Boyhan, A, et al.
  Izdano: (1997)
• Inducible nitric oxide synthase: identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin.
  od: Cho, H J, et al.
  Izdano: (1995)
• Brain nitric oxide synthase is a haemoprotein.
  od: Klatt, P, et al.
  Izdano: (1992)
• Uptake of nitric oxide synthase inhibitors by macrophage RAW 264.7 cells.
  od: Schmidt, K, et al.
  Izdano: (1994)