Cryoelectron microscopy of protein-lipid complexes of human myelin basic protein charge isomers differing in degree of citrullination.

Abstract

Myelin basic protein (MBP) is considered to be essential for the maintenance of stability of the myelin sheath. Reduction in cationicity of MBP, especially due to conversion of positively charged arginine residues to uncharged citrulline (Cit), has been found to be associated with multiple sclerosis (MS). Here, the interactions of an anionic… (More)

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Cite this paper

@article{Beniac2000CryoelectronMO, title={Cryoelectron microscopy of protein-lipid complexes of human myelin basic protein charge isomers differing in degree of citrullination.}, author={Daniel R. Beniac and D. D. Wood and Nades Palaniyar and F. Peter Ottensmeyer and Mario A. Moscarello and George Harauz}, journal={Journal of structural biology}, year={2000}, volume={129 1}, pages={80-95} }