Modeling the structural consequences of BEST1 missense mutations

Adv Exp Med Biol. 2012:723:611-8. doi: 10.1007/978-1-4614-0631-0_78.
No abstract available

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bestrophins
  • Chloride Channels / chemistry*
  • Chloride Channels / genetics*
  • Computer Simulation
  • Disease Models, Animal
  • Dog Diseases / genetics*
  • Dog Diseases / physiopathology
  • Dogs
  • Eye Proteins / chemistry*
  • Eye Proteins / genetics*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Models, Chemical*
  • Mutation, Missense / physiology
  • Structure-Activity Relationship
  • Vitelliform Macular Dystrophy / genetics*
  • Vitelliform Macular Dystrophy / physiopathology
  • Water / chemistry

Substances

  • BEST1 protein, human
  • Bestrophins
  • Chloride Channels
  • Eye Proteins
  • Membrane Proteins
  • Water