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Gene Review

PLP1  -  proteolipid protein 1

Bos taurus

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Disease relevance of PLP1


High impact information on PLP1


Biological context of PLP1


Anatomical context of PLP1


Associations of PLP1 with chemical compounds

  • We propose that PLP is integrated into the lipid bilayer of myelin with the NH2 terminus and three positively charged hydrophilic loops oriented toward the extracytosolic side of the membrane, whereas one strongly negative hydrophilic loop and the positively charged COOH terminus cover the cytosolic side of the lipid bilayer [10].
  • To identify the Cys residue(s) involved in the thioester linkage(s), reduced and carboxyamidomethylated proteolipid protein was labeled with [14C]iodoacetamide upon deacylation with neutral hydroxylamine [7].
  • Integral membrane proteins significantly decrease the molecular motion in lipid bilayers: a deuteron NMR relaxation study of membranes containing myelin proteolipid apoprotein [11].
  • Liposomes reconstituted with the myelin proteolipid apoprotein transport protons, as assayed by quenching of the fluorescence of 9-aminoacridine [13].
  • Expression of a proteolipid gene from a high-copy-number plasmid confers trifluoperazine resistance to Saccharomyces cerevisiae [14].

Physical interactions of PLP1

  • Its proteins consisted of (1) two basic proteins (16,000 and 18,500 apparent Mr) that reacted with anti-human CNS myelin basic protein antibodies and (2) a major protein (29,000 apparent Mr) that stained with concanavalin A-horseradish peroxidase and bound to anti-rat CNS myelin proteolipid protein (PLP) antibodies [15].

Other interactions of PLP1


Analytical, diagnostic and therapeutic context of PLP1


  1. Induction of circulating myelin basic protein and proteolipid protein-specific transforming growth factor-beta1-secreting Th3 T cells by oral administration of myelin in multiple sclerosis patients. Fukaura, H., Kent, S.C., Pietrusewicz, M.J., Khoury, S.J., Weiner, H.L., Hafler, D.A. J. Clin. Invest. (1996) [Pubmed]
  2. Chronic experimental allergic encephalomyelitis produced by bovine proteolipid apoprotein: immunological studies in rabbits. Cambi, F., Lees, M.B., Williams, R.M., Macklin, W.B. Ann. Neurol. (1983) [Pubmed]
  3. Chronic experimental allergic encephalomyelitis and antibody responses in rabbits immunized with bovine proteolipid apoprotein. van der Veen, R.C., Sobel, R.A., Lees, M.B. J. Neuroimmunol. (1986) [Pubmed]
  4. Two genes encoding the bovine mitochondrial ATP synthase proteolipid specify precursors with different import sequences and are expressed in a tissue-specific manner. Gay, N.J., Walker, J.E. EMBO J. (1985) [Pubmed]
  5. Mutational analysis of yeast vacuolar H(+)-ATPase. Noumi, T., Beltrán, C., Nelson, H., Nelson, N. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  6. cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H+-ATPases. Mandel, M., Moriyama, Y., Hulmes, J.D., Pan, Y.C., Nelson, H., Nelson, N. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  7. Cysteine-108 is an acylation site in myelin proteolipid protein. Bizzozero, O.A., Good, L.K., Evans, J.E. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  8. The primary structure of bovine brain myelin lipophilin (proteolipid apoprotein). Stoffel, W., Hillen, H., Schröder, W., Deutzmann, R. Hoppe-Seyler's Z. Physiol. Chem. (1983) [Pubmed]
  9. Structural analysis and transcript processing of the bovine proteolipid protein (PLP) gene. Baumgartner, B.G., Masabanda, J., Fries, R., Brenig, B. DNA Seq. (2000) [Pubmed]
  10. Structure and molecular arrangement of proteolipid protein of central nervous system myelin. Stoffel, W., Hillen, H., Giersiefen, H. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  11. Integral membrane proteins significantly decrease the molecular motion in lipid bilayers: a deuteron NMR relaxation study of membranes containing myelin proteolipid apoprotein. Meier, P., Sachse, J.H., Brophy, P.J., Marsh, D., Kothe, G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  12. The immunopathology of chronic experimental allergic encephalomyelitis induced in rabbits with bovine proteolipid protein. Sobel, R.A., van der Veen, R.C., Lees, M.B. J. Immunol. (1986) [Pubmed]
  13. Interactions of dicyclohexylcarbodiimide with myelin proteolipid. Lin, L.F., Lees, M.B. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  14. Expression of a proteolipid gene from a high-copy-number plasmid confers trifluoperazine resistance to Saccharomyces cerevisiae. Shih, C.K., Kwong, J., Montalvo, E., Neff, N. Mol. Cell. Biol. (1990) [Pubmed]
  15. Major central nervous system myelin glycoprotein of the African lungfish (Protopterus dolloi) cross-reacts with myelin proteolipid protein antibodies, indicating a close phylogenetic relationship with amphibians. Waehneldt, T.V., Matthieu, J.M., Jeserich, G. J. Neurochem. (1986) [Pubmed]
  16. The bovine papillomavirus type 4 E8 protein binds to ductin and causes loss of gap junctional intercellular communication in primary fibroblasts. Faccini, A.M., Cairney, M., Ashrafi, G.H., Finbow, M.E., Campo, M.S., Pitts, J.D. J. Virol. (1996) [Pubmed]
  17. Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. I. Binding of cytochrome c to cardiolipin/phosphatidylcholine membranes in the absence of oxidase. Salamon, Z., Tollin, G. Biophys. J. (1996) [Pubmed]
  18. Structure of the proteolipid protein extracted from bovine central nervous system myelin with nondenaturing detergents. Smith, R., Cook, J., Dickens, P.A. J. Neurochem. (1984) [Pubmed]
  19. Molecular cloning and sequencing of cDNAs encoding the proteolipid subunit of the vacuolar H(+)-ATPase from a higher plant. Lai, S.P., Watson, J.C., Hansen, J.N., Sze, H. J. Biol. Chem. (1991) [Pubmed]
  20. Solid-phase immunoassays for quantitation of antibody to bovine white matter proteolipid apoprotein. Macklin, W.B., Lees, M.B. J. Neurochem. (1982) [Pubmed]
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