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BibTeX file of [Han13] [show it without abstract]

@article{Han13, author={Huijong Han and Matti Myllykoski and Salla Ruskamo and Chaozhan Wang and Petri Kursula}, title={Myelin-specific proteins: a structurally diverse group of membrane-interacting molecules}, journal={BioFactors}, volume={39}, pages={233--241}, year={2013}, keywords={myelin; protein structure; membrane protein; intrinsic disorder; CSSB-HZI; DESY; review;}, url={https://doi.org/10.1002/biof.1076}, doi={10.1002/biof.1076}, abstract={The myelin sheath is a multilayered membrane in the nervous system, which has unique biochemical properties. Myelin carries a set of specific high-abundance proteins, the structure and function of which are still poorly understood. The proteins of the myelin sheath are involved in a number of neurological diseases, including autoimmune diseases and inherited neuropathies. In this review, we briefly discuss the structural properties and functions of selected myelin-specific proteins (P0, myelin oligodendrocyte glycoprotein, myelin-associated glycoprotein, myelin basic protein, myelin-associated oligodendrocytic basic protein, P2, proteolipid protein, peripheral myelin protein of 22 kDa, 2',3'-cyclic nucleotide 3'-phosphodiesterase, and periaxin); such properties include, for example, interactions with lipid bilayers and the presence of large intrinsically disordered regions in some myelin proteins. A detailed understanding of myelin protein structure and function at the molecular level will be required to fully grasp their physiological roles in the myelin sheath.} }

Huijong Han, Matti Myllykoski, Salla Ruskamo, Chaozhan Wang, and Petri Kursula, Myelin-specific proteins: a structurally diverse group of membrane-interacting molecules, BioFactors 39, 233–241 (2013)

[abstract]

doi:10.1002/biof.1076

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