Divalent Cations and Redox Conditions Regulate the Molecular Structure and Function of Visinin-Like Protein-1

@inproceedings{Wang2011DivalentCA,
  title={Divalent Cations and Redox Conditions Regulate the Molecular Structure and Function of Visinin-Like Protein-1},
  author={Conan K. Wang and Anne C Simon and Christian Moestrup Jessen and Cristiano L. P. de Oliveira and Lynsey A Mack and K H Braunewell and James B Ames and Jan Skov Pedersen and Andreas Hofmann},
  booktitle={PloS one},
  year={2011}
}
The NCS protein Visinin-like Protein 1 (VILIP-1) transduces calcium signals in the brain and serves as an effector of the non-retinal receptor guanylyl cyclases (GCs) GC-A and GC-B, and nicotinic acetyl choline receptors (nAchR). Analysis of the quaternary structure of VILIP-1 in solution reveals the existence of monomeric and dimeric species, the relative contents of which are affected but not exclusively regulated by divalent metal ions and Redox conditions. Using small-angle X-ray scattering… CONTINUE READING

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CRYSOL - a program to evaluate Xray solution scattering of biological macromolecules from atomic coordinates

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