Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function

Samankaltaisia teoksia

• Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin.
  Tekijä: Karnik, S S, et al.
  Julkaistu: (1988)
• Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
  Tekijä: Hwa, John, et al.
  Julkaistu: (2001)
• Structure and function in rhodopsin: Destabilization of rhodopsin by the binding of an antibody at the N-terminal segment provides support for involvement of the latter in an intradiscal tertiary structure
  Tekijä: Cha, Kiweon, et al.
  Julkaistu: (2000)
• Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.
  Tekijä: Davidson, F F, et al.
  Julkaistu: (1994)
• Structure and function in rhodopsin: Packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled
  Tekijä: Hwa, John, et al.
  Julkaistu: (1997)