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Volumn 10, Issue AUG, 2016, Pages

Multifaceted role of sialylation in prion diseases

Author keywords

Amyloid; Neuraminidase; Prion disease; Prions; Sialic acid; Sialylation; Sialyltransferase; Species barrier

Indexed keywords

GLYCAN; PRION PROTEIN; SIALIDASE; SIALYLTRANSFERASE;

EID: 84988353314     PISSN: 16624548     EISSN: 1662453X     Source Type: Journal    
DOI: 10.3389/fnins.2016.00358     Document Type: Review
Times cited : (48)

References (160)
  • 1
    • 84905590992 scopus 로고    scopus 로고
    • Neurodegeneration: alzheimer's disease under strain
    • Aguzzi, A. (2014). Neurodegeneration: alzheimer's disease under strain. Nature 512, 32-34. doi: 10.1038/512032a.
    • (2014) Nature , vol.512 , pp. 32-34
    • Aguzzi, A.1
  • 2
    • 0141514778 scopus 로고    scopus 로고
    • Immune system and peripheral nerves in propagation of prions to CNS
    • Aguzzi, A., Heppner, F. L., Heikenwalder, M., Prinz, M., Mertz, K., Seeger, H., et al. (2003). Immune system and peripheral nerves in propagation of prions to CNS. Br. Med. Bull. 66, 141-159. doi: 10.1093/bmb/66.1.141.
    • (2003) Br. Med. Bull. , vol.66 , pp. 141-159
    • Aguzzi, A.1    Heppner, F.L.2    Heikenwalder, M.3    Prinz, M.4    Mertz, K.5    Seeger, H.6
  • 3
    • 84888311810 scopus 로고    scopus 로고
    • The immunology of prion diseases
    • Aguzzi, A., Nuvolone, M., and Zhu, C. (2013). The immunology of prion diseases. Nat. Rev. Immunol. 13, 888-902. doi: 10.1038/nri3553.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 888-902
    • Aguzzi, A.1    Nuvolone, M.2    Zhu, C.3
  • 4
    • 84893858360 scopus 로고    scopus 로고
    • SAXS structural study of PrP(Sc) reveals ~11 nm diameter of basic double intertwined fibers
    • Amenitsch, H., Benetti, F., Ramos, A., Legname, G., and Requena, J. R. (2013). SAXS structural study of PrP(Sc) reveals ~11 nm diameter of basic double intertwined fibers. Prion 7, 496-500. doi: 10.4161/pri.27190.
    • (2013) Prion , vol.7 , pp. 496-500
    • Amenitsch, H.1    Benetti, F.2    Ramos, A.3    Legname, G.4    Requena, J.R.5
  • 5
    • 0017357632 scopus 로고
    • Role of sialic acid in survival of erythrocytes in the circulation: interaction of neuraminidase-treated and untreated erythrocytes with spleen and liver at the cellular level
    • Aminoff, D., Bruegge, W. F., Bell, W. C., Sarpolis, K., and Williams, R. (1977). Role of sialic acid in survival of erythrocytes in the circulation: interaction of neuraminidase-treated and untreated erythrocytes with spleen and liver at the cellular level. Proc. Acad. Natl. Sci. U.S.A. 74, 1521-1524. doi: 10.1073/pnas.74.4.1521.
    • (1977) Proc. Acad. Natl. Sci. U.S.A. , vol.74 , pp. 1521-1524
    • Aminoff, D.1    Bruegge, W.F.2    Bell, W.C.3    Sarpolis, K.4    Williams, R.5
  • 6
    • 0034536342 scopus 로고    scopus 로고
    • Early accumulation of PrP(Sc) in gut-associated lymphoid and nervous tissues of susceptible sheep from a Romanov flock with natural scrapie
    • Andréoletti, O., Berthon, P., Marc, D., Sarradin, P., Grosclaude, J., van Keulen, L., et al. (2000). Early accumulation of PrP(Sc) in gut-associated lymphoid and nervous tissues of susceptible sheep from a Romanov flock with natural scrapie. J. Gen. Virol. 81, 3115-3126. doi: 10.1099/0022-1317-81-12-3115.
    • (2000) J. Gen. Virol. , vol.81 , pp. 3115-3126
    • Andréoletti, O.1    Berthon, P.2    Marc, D.3    Sarradin, P.4    Grosclaude, J.5    van Keulen, L.6
  • 7
    • 18744362997 scopus 로고    scopus 로고
    • BSE prions propagate as either variant CJD-like or sporadic CJD-like prion stains in transgenic mice expressing human prion protein
    • Asante, E. A., Linehan, J. M., Desbruslais, M., Joiner, S., Gowland, I., Wood, A. L., et al. (2002). BSE prions propagate as either variant CJD-like or sporadic CJD-like prion stains in transgenic mice expressing human prion protein. EMBO J. 21, 6358-6366. doi: 10.1093/emboj/cdf653.
    • (2002) EMBO J. , vol.21 , pp. 6358-6366
    • Asante, E.A.1    Linehan, J.M.2    Desbruslais, M.3    Joiner, S.4    Gowland, I.5    Wood, A.L.6
  • 8
    • 79956080260 scopus 로고    scopus 로고
    • Current trend in the structure-activity relationships of sialylatransferases
    • Audry, M., Jeanneau, C., Imberty, A., Harduin-Lepers, A., Delannoy, P., and Breton, C. (2011). Current trend in the structure-activity relationships of sialylatransferases. Glycobiology 21, 716-726. doi: 10.1093/glycob/cwq189.
    • (2011) Glycobiology , vol.21 , pp. 716-726
    • Audry, M.1    Jeanneau, C.2    Imberty, A.3    Harduin-Lepers, A.4    Delannoy, P.5    Breton, C.6
  • 9
    • 79953286302 scopus 로고    scopus 로고
    • The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease
    • Ayers, J. I., Schutt, C. R., Shikiya, R. A., Aguzzi, A., Kincaid, A. E., and Bartz, J. C. (2011). The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease. PLoS Pathog. 7:e1001317. doi: 10.1371/journal.ppat.1001317.
    • (2011) PLoS Pathog. , vol.7
    • Ayers, J.I.1    Schutt, C.R.2    Shikiya, R.A.3    Aguzzi, A.4    Kincaid, A.E.5    Bartz, J.C.6
  • 10
    • 33846069216 scopus 로고    scopus 로고
    • Prion interference is due to a reduction in strain-specific PrPSc levels
    • Bartz, J. C., Kramer, M. L., Sheehan, M. H., Hutter, J. A., Ayers, J. I., Bessen, R. A., et al. (2007). Prion interference is due to a reduction in strain-specific PrPSc levels. J. Virol. 81, 689-697. doi: 10.1128/JVI.01751-06.
    • (2007) J. Virol. , vol.81 , pp. 689-697
    • Bartz, J.C.1    Kramer, M.L.2    Sheehan, M.H.3    Hutter, J.A.4    Ayers, J.I.5    Bessen, R.A.6
  • 11
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native à-helical conformation is under kinetic control
    • Baskakov, I. V., Legname, G., Prusiner, S. B., and Cohen, F. E. (2001). Folding of prion protein to its native à-helical conformation is under kinetic control. J. Biol. Chem. 276, 19687-19690. doi: 10.1074/jbc. C100180200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 12
    • 84981340901 scopus 로고    scopus 로고
    • Sialic acid within the glycosylphosphatidylinositol anchor targets the cellular prion protein to synapses
    • [Epub ahead of print]
    • Bate, C., Nolan, W., McHale-Owen, H., and Williams, A. (2016a). Sialic acid within the glycosylphosphatidylinositol anchor targets the cellular prion protein to synapses. J. Biol. Chem. doi: 10.1074/jbc. M115.672394. [Epub ahead of print].
    • (2016) J. Biol. Chem
    • Bate, C.1    Nolan, W.2    McHale-Owen, H.3    Williams, A.4
  • 13
    • 84952905627 scopus 로고    scopus 로고
    • Sialic acid on the glycosylphosphatidylinositol anchor regulates PrP-mediated cell signaling and prion formation
    • Bate, C., Nolan, W., and Williams, A. (2016b). Sialic acid on the glycosylphosphatidylinositol anchor regulates PrP-mediated cell signaling and prion formation. J. Biol. Chem. 291, 160-170. doi: 10.1074/jbc. M115.672394.
    • (2016) J. Biol. Chem. , vol.291 , pp. 160-170
    • Bate, C.1    Nolan, W.2    Williams, A.3
  • 14
    • 84866561144 scopus 로고    scopus 로고
    • Clustring of sialylated glycocylphosphatidylinositol anchors mediated PrP-induced activation of cytoplasmic phospholipase A2 and synapse damage
    • Bate, C., and Williams, A. (2012a). Clustring of sialylated glycocylphosphatidylinositol anchors mediated PrP-induced activation of cytoplasmic phospholipase A2 and synapse damage. Prion 6, 350-353. doi: 10.4161/pri.21751.
    • (2012) Prion , vol.6 , pp. 350-353
    • Bate, C.1    Williams, A.2
  • 15
    • 84858061475 scopus 로고    scopus 로고
    • Neurodegeneration induced by clustering of sialylated glycosylphosphatidylinositols of prion proteins
    • Bate, C., and Williams, A. (2012b). Neurodegeneration induced by clustering of sialylated glycosylphosphatidylinositols of prion proteins. J. Biol. Chem. 287, 7935-7944. doi: 10.1074/jbc. M111.275743.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7935-7944
    • Bate, C.1    Williams, A.2
  • 16
    • 84856306158 scopus 로고    scopus 로고
    • Facilitated cross-species transmission of prions in extraneural tissue
    • Béringue, V., Herzog, L., Jaumain, E., Reine, F., Sibille, P., Le Dur, A., et al. (2012). Facilitated cross-species transmission of prions in extraneural tissue. Science 335, 472-475. doi: 10.1126/science.1215659.
    • (2012) Science , vol.335 , pp. 472-475
    • Béringue, V.1    Herzog, L.2    Jaumain, E.3    Reine, F.4    Sibille, P.5    Le Dur, A.6
  • 17
    • 84876014342 scopus 로고    scopus 로고
    • Prion infectivity in the spleen of a PRNP heterozygous individual with subclinical variant Creutzfeldt-Jakob disease
    • Bishop, M. T., Diack, A. B., Ritchie, D. L., Ironside, J. W., Will, R. G., and Manson, J. C. (2013). Prion infectivity in the spleen of a PRNP heterozygous individual with subclinical variant Creutzfeldt-Jakob disease. Brain 136, 1139-1145. doi: 10.1093/brain/awt032.
    • (2013) Brain , vol.136 , pp. 1139-1145
    • Bishop, M.T.1    Diack, A.B.2    Ritchie, D.L.3    Ironside, J.W.4    Will, R.G.5    Manson, J.C.6
  • 18
    • 33646059507 scopus 로고    scopus 로고
    • Predicting susceptibility and incubation time of human-to-human transmission of vCJD
    • Bishop, M. T., Hart, P., Aitchison, L., Baybutt, H. N., Plinston, C., Thomson, V., et al. (2006). Predicting susceptibility and incubation time of human-to-human transmission of vCJD. Lancet Neurol. 5, 393-398. doi: 10.1016/S1474-4422(06)70413-6.
    • (2006) Lancet Neurol. , vol.5 , pp. 393-398
    • Bishop, M.T.1    Hart, P.2    Aitchison, L.3    Baybutt, H.N.4    Plinston, C.5    Thomson, V.6
  • 19
    • 0022000573 scopus 로고
    • Scrapie PrP 27-30 is a sialoglycoprotein
    • Bolton, D. C., Meyer, R. K., and Prusiner, S. B. (1985). Scrapie PrP 27-30 is a sialoglycoprotein. J. Virol. 53, 596-606.
    • (1985) J. Virol. , vol.53 , pp. 596-606
    • Bolton, D.C.1    Meyer, R.K.2    Prusiner, S.B.3
  • 20
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • Braak, H., and Braak, E. (1991). Neuropathological staging of Alzheimer-related changes. Acta Neuropathol. 82, 239-259. doi: 10.1007/BF00308809.
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 21
    • 84904873895 scopus 로고    scopus 로고
    • Peripheral prion disease pathogenesis is unaltered in the absence of sialoadhesin (Siglec-1/CD169)
    • Bradford, B. M., Crocker, P. R., and Mabbott, N. A. (2014). Peripheral prion disease pathogenesis is unaltered in the absence of sialoadhesin (Siglec-1/CD169). Immunology 143, 120-129. doi: 10.1111/imm.12294.
    • (2014) Immunology , vol.143 , pp. 120-129
    • Bradford, B.M.1    Crocker, P.R.2    Mabbott, N.A.3
  • 22
    • 84897859634 scopus 로고    scopus 로고
    • Microglial phagocytosis of live neurons
    • Brown, G. C., and Neher, J. J. (2014). Microglial phagocytosis of live neurons. Nat. Rev. Neurosci. 15, 209-216. doi: 10.1038/nrn3710.
    • (2014) Nat. Rev. Neurosci. , vol.15 , pp. 209-216
    • Brown, G.C.1    Neher, J.J.2
  • 23
    • 0032746253 scopus 로고    scopus 로고
    • Scrapie replication in lyphoid tissues depends on prion protein-expressing follicular dendritic cells
    • Brown, K. L., Stewart, K., Ritchie, D. L., Mabbott, N. A., Williams, A., Fraser, H., et al. (1999). Scrapie replication in lyphoid tissues depends on prion protein-expressing follicular dendritic cells. Nat. Med. 5, 1308-1312. doi: 10.1038/15264.
    • (1999) Nat. Med. , vol.5 , pp. 1308-1312
    • Brown, K.L.1    Stewart, K.2    Ritchie, D.L.3    Mabbott, N.A.4    Williams, A.5    Fraser, H.6
  • 24
    • 0025786828 scopus 로고
    • The human spongiform encephalopathies: kuru, Creutzfeldt-Jakob disease, and the Gerstmann-Sträussler-Scheinker syndrome
    • Brown, P., and Gajdusek, D. C. (1991). The human spongiform encephalopathies: kuru, Creutzfeldt-Jakob disease, and the Gerstmann-Sträussler-Scheinker syndrome. Curr. Top. Microbiol. Immunol. 172, 1-20. doi: 10.1007/978-3-642-76540-7_1.
    • (1991) Curr. Top. Microbiol. Immunol. , vol.172 , pp. 1-20
    • Brown, P.1    Gajdusek, D.C.2
  • 25
    • 77954759617 scopus 로고    scopus 로고
    • Human dendritic cells contain cell surface sialyltransferase activity
    • Cabral, M. G., Piteira, A. R., Silva, Z., Ligeiro, D., Brossmer, R., and Videira, P. A. (2010). Human dendritic cells contain cell surface sialyltransferase activity. Immunol. Lett. 131, 89-96. doi: 10.1016/j.imlet.2010.02.009.
    • (2010) Immunol. Lett. , vol.131 , pp. 89-96
    • Cabral, M.G.1    Piteira, A.R.2    Silva, Z.3    Ligeiro, D.4    Brossmer, R.5    Videira, P.A.6
  • 26
    • 84865600794 scopus 로고    scopus 로고
    • A common BACE1 polymorphism is a risk factor for sporadic Creutzfeldt-Jakob disease
    • Calero, O., Bullido, M. J., Clarimón, J., Frank-García, A., Martínez-Martín, P., Lleó, A., et al. (2012). A common BACE1 polymorphism is a risk factor for sporadic Creutzfeldt-Jakob disease. PLoS ONE 7:0043926. doi: 10.1371/journal.pone.0043926.
    • (2012) PLoS ONE , vol.7
    • Calero, O.1    Bullido, M.J.2    Clarimón, J.3    Frank-García, A.4    Martínez-Martín, P.5    Lleó, A.6
  • 29
    • 0345505687 scopus 로고    scopus 로고
    • Prion protein as trans-ineracting partner for neurons is involved in neurite outgrowth and neuronal survival
    • Chen, S., Mangé, A., Dong, L., Lehmann, S., and Schachner, M. (2003). Prion protein as trans-ineracting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol. Cell. Neurosci. 22, 227-233. doi: 10.1016/S1044-7431(02)00014-3.
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 227-233
    • Chen, S.1    Mangé, A.2    Dong, L.3    Lehmann, S.4    Schachner, M.5
  • 30
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: a parallel, in-register b-structure
    • Cobb, N. J., Sönnichsen, F. D., McHaourab, H., Surewicz, W.,and K. (2007). Molecular architecture of human prion protein amyloid: a parallel, in-register b-structure. Proc. Acad. Natl. Sci. U.S.A. 104, 18946-18951. doi: 10.1073/pnas.0706522104.
    • (2007) Proc. Acad. Natl. Sci. U.S.A. , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sönnichsen, F.D.2    McHaourab, H.3    Surewicz, W.K.4
  • 31
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen, F. E., and Prusiner, S. B. (1998). Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67, 793-819. doi: 10.1146/annurev.biochem.67.1.793.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 33
    • 13344293718 scopus 로고
    • Unaltered susceptibility to BSE in transgenic mice expressing human prion protein
    • Collinge, J., Palmer, M. S., Sidle, K. C., Hill, A. F., Gowland, I., Meads, J., et al. (1995). Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature 378, 779-783. doi: 10.1038/378779a0.
    • (1995) Nature , vol.378 , pp. 779-783
    • Collinge, J.1    Palmer, M.S.2    Sidle, K.C.3    Hill, A.F.4    Gowland, I.5    Meads, J.6
  • 34
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of "new variant" CJD
    • Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J., and Hill, A. F. (1996). Molecular analysis of prion strain variation and the aetiology of "new variant" CJD. Nature 383, 685-690. doi: 10.1038/383685a0.
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 35
    • 1942437467 scopus 로고    scopus 로고
    • Masking of CD22 by cis ligands does not prevent redistribution of CD22 to sites of cell contact
    • Collins, B. E., Blixt, O., DeSieno, A. R., Bovin, N., Marth, J. D., and Paulson, J. C. (2004). Masking of CD22 by cis ligands does not prevent redistribution of CD22 to sites of cell contact. Proc. Acad. Natl. Sci. U.S.A. 101, 6104-6109. doi: 10.1073/pnas.0400851101.
    • (2004) Proc. Acad. Natl. Sci. U.S.A. , vol.101 , pp. 6104-6109
    • Collins, B.E.1    Blixt, O.2    DeSieno, A.R.3    Bovin, N.4    Marth, J.D.5    Paulson, J.C.6
  • 36
    • 0032588891 scopus 로고    scopus 로고
    • PrPC glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains
    • DeArmond, S. J., Qiu, Y., Sànchez, H., Spilman, P. R., Ninchak-Casey, A., Alonso, D., et al. (1999). PrPC glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains. J. Neuropathol. Exp. Neurol. 58, 1000-1009.
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 1000-1009
    • DeArmond, S.J.1    Qiu, Y.2    Sànchez, H.3    Spilman, P.R.4    Ninchak-Casey, A.5    Alonso, D.6
  • 37
    • 0015518449 scopus 로고
    • Competition between different scrapie agents in mice
    • Dickinson, A. G., Fraser, H., Meikle, V. M. H., and Outram, G. W. (1972). Competition between different scrapie agents in mice. Nat. New Biol. 237, 244-245. doi: 10.1038/newbio237244a0.
    • (1972) Nat. New Biol. , vol.237 , pp. 244-245
    • Dickinson, A.G.1    Fraser, H.2    Meikle, V.M.H.3    Outram, G.W.4
  • 38
    • 0024434503 scopus 로고
    • Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein
    • Endo, T., Groth, D., Prusiner, S. B., and Kobata, A. (1989). Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 28, 8380-8388. doi: 10.1021/bi00447a017.
    • (1989) Biochemistry , vol.28 , pp. 8380-8388
    • Endo, T.1    Groth, D.2    Prusiner, S.B.3    Kobata, A.4
  • 39
    • 0033229717 scopus 로고    scopus 로고
    • C-Type lectins and sialyl lewis X Oligosaccharides versatile roles in cell-cell interaction
    • Fukuda, M., Hiraoka, N., and Yeh, J. C. (1999). C-Type lectins and sialyl lewis X Oligosaccharides versatile roles in cell-cell interaction. J. Cell Biol. 147, 467-470. doi: 10.1083/jcb.147.3.467.
    • (1999) J. Cell Biol. , vol.147 , pp. 467-470
    • Fukuda, M.1    Hiraoka, N.2    Yeh, J.C.3
  • 40
    • 80052702962 scopus 로고    scopus 로고
    • Relationship between conformational stability and amplification efficiency of prions
    • Gonzalez-Montalban, N., Makarava, N., Savtchenko, R., and Baskakov, I. V. (2011). Relationship between conformational stability and amplification efficiency of prions. Biochemistry 50, 7933-7940. doi: 10.1021/bi200950v.
    • (2011) Biochemistry , vol.50 , pp. 7933-7940
    • Gonzalez-Montalban, N.1    Makarava, N.2    Savtchenko, R.3    Baskakov, I.V.4
  • 41
    • 2942616602 scopus 로고    scopus 로고
    • Evidance for assembly of prions with left-handed b-helices into trimers
    • Govaerts, C., Wille, H., Prusiner, S. B., and Cohen, F. E. (2004). Evidance for assembly of prions with left-handed b-helices into trimers. Proc. Acad. Natl. Sci. U.S.A. 101, 8342-8347. doi: 10.1073/pnas.0402254101.
    • (2004) Proc. Acad. Natl. Sci. U.S.A. , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 42
    • 0029895390 scopus 로고    scopus 로고
    • Ecto-sialyltransferase of human B lymphocytes reconstitutes differentiation markers in the presence of exogenous CMP-N-acetyl neuraminic acid
    • Gross, H. J., Merling, A., Moldenhauer, G., and Schwartz-Albiez, R. (1996). Ecto-sialyltransferase of human B lymphocytes reconstitutes differentiation markers in the presence of exogenous CMP-N-acetyl neuraminic acid. Blood 87, 5113-5126.
    • (1996) Blood , vol.87 , pp. 5113-5126
    • Gross, H.J.1    Merling, A.2    Moldenhauer, G.3    Schwartz-Albiez, R.4
  • 43
    • 84906861755 scopus 로고    scopus 로고
    • Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids
    • Groveman, B. R., Dolan, M. A., Taubner, L. M., Kraus, A., Wickner, R. B., and Caughey, B. (2014). Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids. J. Biol. Chem. 289, 24129-24142. doi: 10.1074/jbc. M114.578344.
    • (2014) J. Biol. Chem. , vol.289 , pp. 24129-24142
    • Groveman, B.R.1    Dolan, M.A.2    Taubner, L.M.3    Kraus, A.4    Wickner, R.B.5    Caughey, B.6
  • 44
    • 66249119564 scopus 로고    scopus 로고
    • Glycosylation-related gene expression profiling in the brain and spleen of scrapie-affected mouse
    • Guillerme-Bosselut, F., Forestier, L., Jayat-Vignoles, C., Vilotte, J. L., Popa, I., Portoukalian, J., et al. (2009). Glycosylation-related gene expression profiling in the brain and spleen of scrapie-affected mouse. Glycobiology 19, 879-889. doi: 10.1093/glycob/cwp062.
    • (2009) Glycobiology , vol.19 , pp. 879-889
    • Guillerme-Bosselut, F.1    Forestier, L.2    Jayat-Vignoles, C.3    Vilotte, J.L.4    Popa, I.5    Portoukalian, J.6
  • 45
    • 84903880339 scopus 로고    scopus 로고
    • Accelerated, spleen-based titration of variant Creutzfeldt-Jakob disease infectivity in transgenic mice expressing human prion protein with sensitivity comparable to that of survival time bioassay
    • Halliez, S., Reine, F., Herzog, L., Juamain, E., Haïk, S., Rezaei, H., et al. (2014). Accelerated, spleen-based titration of variant Creutzfeldt-Jakob disease infectivity in transgenic mice expressing human prion protein with sensitivity comparable to that of survival time bioassay. J. Virol. 88, 8678-8686. doi: 10.1128/JVI.01118-14.
    • (2014) J. Virol. , vol.88 , pp. 8678-8686
    • Halliez, S.1    Reine, F.2    Herzog, L.3    Juamain, E.4    Haïk, S.5    Rezaei, H.6
  • 47
    • 0033573778 scopus 로고    scopus 로고
    • Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples
    • Hill, A. F., Butterworth, R. J., Joiner, S., Jackson, G., Rossor, M. N., Thomas, D. J., et al. (1999). Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples. Lancet 353, 183-189. doi: 10.1016/S0140-6736(98)12075-5.
    • (1999) Lancet , vol.353 , pp. 183-189
    • Hill, A.F.1    Butterworth, R.J.2    Joiner, S.3    Jackson, G.4    Rossor, M.N.5    Thomas, D.J.6
  • 48
    • 0032578283 scopus 로고    scopus 로고
    • Prion immunoreactivity in appendix before clinical onset of variant Creutzfeldt-Jakob disease
    • Hilton, D. A., Fathers, E., Edwards, P., Ironside, J. W., and Zajicek, J. (1998). Prion immunoreactivity in appendix before clinical onset of variant Creutzfeldt-Jakob disease. Lancet 352, 703-704. doi: 10.1016/S0140-6736(98)24035-9.
    • (1998) Lancet , vol.352 , pp. 703-704
    • Hilton, D.A.1    Fathers, E.2    Edwards, P.3    Ironside, J.W.4    Zajicek, J.5
  • 49
    • 3242716876 scopus 로고    scopus 로고
    • Prevalence of lymphoreticular prion protein accumulation in UK tissue samples
    • Hilton, D. A., Ghani, A. C., Conyers, L., Edwards, P., McCardle, L., Ritchie, D., et al. (2004). Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J. Pathol. 203, 733-739. doi: 10.1002/path.1580.
    • (2004) J. Pathol. , vol.203 , pp. 733-739
    • Hilton, D.A.1    Ghani, A.C.2    Conyers, L.3    Edwards, P.4    McCardle, L.5    Ritchie, D.6
  • 50
    • 0036135693 scopus 로고    scopus 로고
    • Migrating intestinal dendritic cells transport PrPSc from the gut
    • Huang, F. P., Farquhar, C. F., Mabbott, N. A., Bruce, M. E., and MacPherson, G. G. (2002). Migrating intestinal dendritic cells transport PrPSc from the gut. J. Gen. Virol. 83, 267-271. doi: 10.1099/0022-1317-83-1-267.
    • (2002) J. Gen. Virol. , vol.83 , pp. 267-271
    • Huang, F.P.1    Farquhar, C.F.2    Mabbott, N.A.3    Bruce, M.E.4    MacPherson, G.G.5
  • 51
    • 84863012533 scopus 로고    scopus 로고
    • Desialylation accelerates platelet clearance after refrigeration and initiates GPIba metalloproteinase-mediated cleavage in mice
    • Jansen, A. J. G., Josefsson, E. C., Rumjantseva, V., Liu, Q. P., Falet, H., Bergmeier, W., et al. (2012). Desialylation accelerates platelet clearance after refrigeration and initiates GPIba metalloproteinase-mediated cleavage in mice. Blood 119, 1263-1273. doi: 10.1182/blood-2011-05-355628.
    • (2012) Blood , vol.119 , pp. 1263-1273
    • Jansen, A.J.G.1    Josefsson, E.C.2    Rumjantseva, V.3    Liu, Q.P.4    Falet, H.5    Bergmeier, W.6
  • 52
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • Jucker, M., and Walker, L. C. (2013). Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45-51. doi: 10.1038/nature12481.
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 53
    • 84957111737 scopus 로고    scopus 로고
    • Knocking out of cellular neuraminidases Neu1, Neu3 or Neu4 does not affect sialylation status of the prion protein
    • Katorcha, E., Klimova, N., Makarava, N., Savtchenko, R., Pan, X., Annunziata, I., et al. (2015a). Knocking out of cellular neuraminidases Neu1, Neu3 or Neu4 does not affect sialylation status of the prion protein. PLoS ONE 10:e0143218. doi: 10.1371/journal.pone.0143218.
    • (2015) PLoS ONE , vol.10
    • Katorcha, E.1    Klimova, N.2    Makarava, N.3    Savtchenko, R.4    Pan, X.5    Annunziata, I.6
  • 54
    • 84947266934 scopus 로고    scopus 로고
    • Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio
    • Katorcha, E., Makarava, N., Savtchenko, R., and Baskakov, I. V. (2015b). Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio. Sci. Rep. 5:16912. doi: 10.1038/srep16912.
    • (2015) Sci. Rep. , vol.5 , pp. 16912
    • Katorcha, E.1    Makarava, N.2    Savtchenko, R.3    Baskakov, I.V.4
  • 55
    • 84907588736 scopus 로고    scopus 로고
    • Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity
    • Katorcha, E., Makarava, N., Savtchenko, R., D'Azzo, A., and Baskakov, I. V. (2014). Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity. PLoS Pathog. 10:e1004366. doi: 10.1371/journal.ppat.1004366.
    • (2014) PLoS Pathog. , vol.10
    • Katorcha, E.1    Makarava, N.2    Savtchenko, R.3    D'Azzo, A.4    Baskakov, I.V.5
  • 56
    • 84982106504 scopus 로고    scopus 로고
    • Sialylation of GPI anchors of mammalian prions is regulated in a host-, tissue-and cell-specific manner
    • [Epub ahead of print]
    • Katorcha, E., Srivastava, S., Klimova, N., and Baskakov, I. V. (2016). Sialylation of GPI anchors of mammalian prions is regulated in a host-, tissue-and cell-specific manner. J. Biol. Chem. doi: 10.1074/jbc. M116.732040. [Epub ahead of print].
    • (2016) J. Biol. Chem
    • Katorcha, E.1    Srivastava, S.2    Klimova, N.3    Baskakov, I.V.4
  • 57
    • 0032588923 scopus 로고    scopus 로고
    • Identification of an alpha2,6-sialyltransferase induced early after lymphocyte activation
    • Kaufmann, M., Blaser, C., Takashima, S., Schwartz-Albiez, R., Tsuji, S., and Pircher, H. (1999). Identification of an alpha2,6-sialyltransferase induced early after lymphocyte activation. Int. Immunol. 11, 731-738. doi: 10.1093/intimm/11.5.731.
    • (1999) Int. Immunol. , vol.11 , pp. 731-738
    • Kaufmann, M.1    Blaser, C.2    Takashima, S.3    Schwartz-Albiez, R.4    Tsuji, S.5    Pircher, H.6
  • 58
    • 0021989356 scopus 로고
    • Competition between strains of scrapie depends on the blocking agent being infectious
    • Kimberlin, R. H., and Walker, C. A. (1985). Competition between strains of scrapie depends on the blocking agent being infectious. Intervirology 23, 74-81. doi: 10.1159/000149588.
    • (1985) Intervirology , vol.23 , pp. 74-81
    • Kimberlin, R.H.1    Walker, C.A.2
  • 59
    • 84886679165 scopus 로고    scopus 로고
    • Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles
    • Kovacs, G. G., Makarava, N., Savtchenko, R., and Baskakov, I. V. (2013). Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles. Am. J. Pathol. 183, 1539-1547. doi: 10.1016/j.ajpath.2013.07.024.
    • (2013) Am. J. Pathol. , vol.183 , pp. 1539-1547
    • Kovacs, G.G.1    Makarava, N.2    Savtchenko, R.3    Baskakov, I.V.4
  • 60
    • 84855290942 scopus 로고    scopus 로고
    • Prion Uptake in the Gut: identification of the first uptake and replication sites
    • Kujala, P., Raymond, C. R., Romeijn, M., Godsave, S. F., van Kasteren, S. I., Wille, H., et al. (2011). Prion Uptake in the Gut: identification of the first uptake and replication sites. PLoS Pathog. 7:e1002449. doi: 10.1371/journal.ppat.1002449.
    • (2011) PLoS Pathog. , vol.7
    • Kujala, P.1    Raymond, C.R.2    Romeijn, M.3    Godsave, S.F.4    van Kasteren, S.I.5    Wille, H.6
  • 62
    • 77953846750 scopus 로고    scopus 로고
    • Treatment with normal prion protein delays differentiation and helps to maintain proliferating activity in human embryonic stem cells
    • Lee, Y. J., and Baskakov, I. V. (2010). Treatment with normal prion protein delays differentiation and helps to maintain proliferating activity in human embryonic stem cells. J. Neurochem. 114, 362-373. doi: 10.1111/j.1471-4159.2010.06601.x.
    • (2010) J. Neurochem. , vol.114 , pp. 362-373
    • Lee, Y.J.1    Baskakov, I.V.2
  • 63
    • 84872084807 scopus 로고    scopus 로고
    • The cellular form of the prion protein is involved in controlling cell cycle dynamics, self-renewal, and the fate of human embryonic stem cell differentiation
    • Lee, Y. J., and Baskakov, I. V. (2013). The cellular form of the prion protein is involved in controlling cell cycle dynamics, self-renewal, and the fate of human embryonic stem cell differentiation. J. Neurochem. 124, 310-322. doi: 10.1111/j.1471-4159.2012.07913.x.
    • (2013) J. Neurochem. , vol.124 , pp. 310-322
    • Lee, Y.J.1    Baskakov, I.V.2
  • 64
    • 84919771119 scopus 로고    scopus 로고
    • The cellular form of the prion protein guides the differentiation of human embryonic stem cells into neuron-, oligodendrocyte-, and astrocyte-committed lineages
    • Lee, Y. J., and Baskakov, I. V. (2014). The cellular form of the prion protein guides the differentiation of human embryonic stem cells into neuron-, oligodendrocyte-, and astrocyte-committed lineages. Prion 8, 266-275. doi: 10.4161/pri.32079.
    • (2014) Prion , vol.8 , pp. 266-275
    • Lee, Y.J.1    Baskakov, I.V.2
  • 66
    • 34548182551 scopus 로고    scopus 로고
    • Normal cellular prion protein is a ligand of selectins: binding requires Lex but is inhibited by sLex
    • Li, C., Wong, P., Pan, T., Xiao, F., Yin, S., Chang, B., et al. (2007). Normal cellular prion protein is a ligand of selectins: binding requires Lex but is inhibited by sLex. Biochem. J. 406, 333-341. doi: 10.1042/BJ20061857.
    • (2007) Biochem. J. , vol.406 , pp. 333-341
    • Li, C.1    Wong, P.2    Pan, T.3    Xiao, F.4    Yin, S.5    Chang, B.6
  • 67
    • 36448998174 scopus 로고    scopus 로고
    • Cellular prion protein expression in astrocytes modulates neuronal survival and differentiation
    • Lima, F. R., Arantes, C. P., Muras, A. G., Nomizo, R., Brentani, R. R., and Martins, V. R. (2007). Cellular prion protein expression in astrocytes modulates neuronal survival and differentiation. J. Neurochem. 103, 2164-2176. doi: 10.1111/j.1471-4159.2007.04904.x.
    • (2007) J. Neurochem. , vol.103 , pp. 2164-2176
    • Lima, F.R.1    Arantes, C.P.2    Muras, A.G.3    Nomizo, R.4    Brentani, R.R.5    Martins, V.R.6
  • 68
    • 84856007233 scopus 로고    scopus 로고
    • Sialic acid on the neuronal glycocalyx prevents complement C1 binding and complement receptor-3-mediated removal by microglia
    • Linnartz, B., Kopatz, J., Tenner, A. J., and Neumann, H. (2012). Sialic acid on the neuronal glycocalyx prevents complement C1 binding and complement receptor-3-mediated removal by microglia. J. Neurosci. 32, 946-952. doi: 10.1523/JNEUROSCI.3830-11.2012.
    • (2012) J. Neurosci. , vol.32 , pp. 946-952
    • Linnartz, B.1    Kopatz, J.2    Tenner, A.J.3    Neumann, H.4
  • 69
    • 84954370985 scopus 로고    scopus 로고
    • Sialylation of neurites inhibits complement-mediated macrophage removal in a human macrophage-neuron Co-Culture System
    • Linnartz-Gerlach, B., Schuy, C., Shahraz, A., Tenner, A. J., and Neumann, H. (2016). Sialylation of neurites inhibits complement-mediated macrophage removal in a human macrophage-neuron Co-Culture System. Glia 64, 35-47. doi: 10.1002/glia.22901.
    • (2016) Glia , vol.64 , pp. 35-47
    • Linnartz-Gerlach, B.1    Schuy, C.2    Shahraz, A.3    Tenner, A.J.4    Neumann, H.5
  • 70
    • 84855290517 scopus 로고    scopus 로고
    • Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease
    • Makarava, N., Kovacs, G. G., Savtchenko, R., Alexeeva, I., Budka, H., Rohwer, R. G., et al. (2011). Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease. PLoS Pathog. 7:e1002419. doi: 10.1371/journal.ppat.1002419.
    • (2011) PLoS Pathog. , vol.7
    • Makarava, N.1    Kovacs, G.G.2    Savtchenko, R.3    Alexeeva, I.4    Budka, H.5    Rohwer, R.G.6
  • 72
    • 84859193614 scopus 로고    scopus 로고
    • Fast and ultrasensitive method for quantitating prion infectivity titer
    • Makarava, N., Savtchenko, R., Alexeeva, I., Rohwer, R. G., and Baskakov, I. V. (2012b). Fast and ultrasensitive method for quantitating prion infectivity titer. Nat. Commun. 3, 741. doi: 10.1038/ncomms1730.
    • (2012) Nat. Commun. , vol.3 , pp. 741
    • Makarava, N.1    Savtchenko, R.2    Alexeeva, I.3    Rohwer, R.G.4    Baskakov, I.V.5
  • 73
    • 84962481036 scopus 로고    scopus 로고
    • New molecular insight into mechanism of evolution of mammalian synthetic prions
    • Makarava, N., Savtchenko, R., Alexeeva, I., Rohwer, R. G., and Baskakov, I. V. (2016). New molecular insight into mechanism of evolution of mammalian synthetic prions. Am. J. Pathol. 186, 1006-1014. doi: 10.1016/j.ajpath.2015.11.013.
    • (2016) Am. J. Pathol. , vol.186 , pp. 1006-1014
    • Makarava, N.1    Savtchenko, R.2    Alexeeva, I.3    Rohwer, R.G.4    Baskakov, I.V.5
  • 74
    • 84872088301 scopus 로고    scopus 로고
    • Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification J
    • Makarava, N., Savtchenko, R., and Baskakov, I. V. (2013). Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification J. Biol. Chem. 288, 33-41. doi: 10.1074/jbc. M112.419531.
    • (2013) Biol. Chem. , vol.288 , pp. 33-41
    • Makarava, N.1    Savtchenko, R.2    Baskakov, I.V.3
  • 75
    • 85012047382 scopus 로고    scopus 로고
    • Two alternative pathways for generating transmissible prion disease de novo
    • Makarava, N., Savtchenko, R., and Baskakov, I. V. (2015). Two alternative pathways for generating transmissible prion disease de novo. Acta Neuropathol. Commun. 3:69. doi: 10.1186/s40478-015-0248-5.
    • (2015) Acta Neuropathol. Commun. , vol.3 , pp. 69
    • Makarava, N.1    Savtchenko, R.2    Baskakov, I.V.3
  • 77
    • 0037031849 scopus 로고    scopus 로고
    • Genetically altered mice with different sialyltransferase defficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetilation
    • Martin, L. T., Marth, J. D., Varki, A., and Varki, N. M. (2002). Genetically altered mice with different sialyltransferase defficiencies show tissue-specific alterations in sialylation and sialic acid 9-O-acetilation. J. Biol. Chem. 277, 32930-32938. doi: 10.1074/jbc. M203362200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32930-32938
    • Martin, L.T.1    Marth, J.D.2    Varki, A.3    Varki, N.M.4
  • 78
    • 84855282475 scopus 로고    scopus 로고
    • Follicular dendritic cell-specific prion protein (PrP) expression alone is sufficient to sustain prion infection in the spleen
    • McCulloch, L., Brown, K. L., Bradford, B. M., Hopkins, J., Bailey, M., Rajewsky, K., et al. (2011). Follicular dendritic cell-specific prion protein (PrP) expression alone is sufficient to sustain prion infection in the spleen. PLoS Pathog. 7:e1002402. doi: 10.1371/journal.ppat.1002402.
    • (2011) PLoS Pathog. , vol.7
    • McCulloch, L.1    Brown, K.L.2    Bradford, B.M.3    Hopkins, J.4    Bailey, M.5    Rajewsky, K.6
  • 79
    • 84942693490 scopus 로고    scopus 로고
    • The prion protein controls polysialylation of neural cell adhesion molecule 1 during cellular morphogenesis
    • Mehrabian, M., Brethour, D., Wang, H., Xi, Z., Rogaeva, E., and Schmitt-Ulms, G. (2015). The prion protein controls polysialylation of neural cell adhesion molecule 1 during cellular morphogenesis. PLoS ONE 10:e0133741. doi: 10.1371/journal.pone.0133741.
    • (2015) PLoS ONE , vol.10
    • Mehrabian, M.1    Brethour, D.2    Wang, H.3    Xi, Z.4    Rogaeva, E.5    Schmitt-Ulms, G.6
  • 81
    • 1642393802 scopus 로고    scopus 로고
    • Chronic wasting disease of cervids
    • Miller, M. W., and Williams, E. S. (2004). Chronic wasting disease of cervids. Curr. Top. Microbiol. Immunol. 284, 193-214. doi: 10.1007/978-3-662-08441-0_8.
    • (2004) Curr. Top. Microbiol. Immunol. , vol.284 , pp. 193-214
    • Miller, M.W.1    Williams, E.S.2
  • 82
    • 84861413498 scopus 로고    scopus 로고
    • Mammalian sialidases: physiological and pathological roles in cellular functions
    • Miyagi, T., and Yamaguchi, K. (2012). Mammalian sialidases: physiological and pathological roles in cellular functions. Glycobiology 22, 880-896. doi: 10.1093/glycob/cws057.
    • (2012) Glycobiology , vol.22 , pp. 880-896
    • Miyagi, T.1    Yamaguchi, K.2
  • 83
    • 0042381231 scopus 로고    scopus 로고
    • Heterogeneity and regulation of cellular prion protein glycoforms in neuronal cell lines
    • Monnet, C., Marthiens, V., Enslen, H., Frobert, Y., Sobel, A., and Mège, R. M. (2003). Heterogeneity and regulation of cellular prion protein glycoforms in neuronal cell lines. Eur. J. Neurosci. 18, 542-548. doi: 10.1046/j.1460-9568.2003.02777.x.
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 542-548
    • Monnet, C.1    Marthiens, V.2    Enslen, H.3    Frobert, Y.4    Sobel, A.5    Mège, R.M.6
  • 84
    • 77956568840 scopus 로고    scopus 로고
    • Sialidases in vertebrates: a family of enzymes tailored for several cell functions
    • Monti, E., Bonten, E., D'Azzo, A., Bresciani, R., Venerando, B., Borsani, G., et al. (2010). Sialidases in vertebrates: a family of enzymes tailored for several cell functions. Adv. Carbohydr. Chem. Biochem. 64, 403-479. doi: 10.1016/S0065-2318(10)64007-3.
    • (2010) Adv. Carbohydr. Chem. Biochem. , vol.64 , pp. 403-479
    • Monti, E.1    Bonten, E.2    D'Azzo, A.3    Bresciani, R.4    Venerando, B.5    Borsani, G.6
  • 85
    • 0034686002 scopus 로고    scopus 로고
    • Impaired prion replication in spleens of mice lacking functional follicular dendritic cells
    • Montrasio, F., Frigg, R., Glatzel, M., Klein, M. A., Mackay, F., Aguzzi, A., et al. (2000). Impaired prion replication in spleens of mice lacking functional follicular dendritic cells. Science 288, 1257-1259. doi: 10.1126/science.288.5469.1257.
    • (2000) Science , vol.288 , pp. 1257-1259
    • Montrasio, F.1    Frigg, R.2    Glatzel, M.3    Klein, M.A.4    Mackay, F.5    Aguzzi, A.6
  • 86
    • 84928034534 scopus 로고    scopus 로고
    • Titration of biologically active amyloid-β seeds in a transgenic mouse model of Alzheimer's disease
    • Morales, R., Bravo-Alegria, J., Duran-Aniotz, C., and Soto, C. (2015). Titration of biologically active amyloid-β seeds in a transgenic mouse model of Alzheimer's disease. Sci. Rep. 5:9343. doi: 10.1038/srep09349.
    • (2015) Sci. Rep. , vol.5 , pp. 9343
    • Morales, R.1    Bravo-Alegria, J.2    Duran-Aniotz, C.3    Soto, C.4
  • 87
    • 84958260195 scopus 로고    scopus 로고
    • Strain-dependent profile of misfolded prion protein aggregates
    • Morales, R., Hu, P. P., Duran-Aniotz, C., Moda, F., Diaz-Espinoza, R., Chen, B., et al. (2016). Strain-dependent profile of misfolded prion protein aggregates. Sci. Rep. 6:20526. doi: 10.1038/srep20526.
    • (2016) Sci. Rep. , vol.6 , pp. 20526
    • Morales, R.1    Hu, P.P.2    Duran-Aniotz, C.3    Moda, F.4    Diaz-Espinoza, R.5    Chen, B.6
  • 88
    • 0032717011 scopus 로고    scopus 로고
    • Prion protein and neuronal differentiation: quantitative analysis of prnp gene expression in a murine inducible neuroectodermal progenitor
    • Mouillet-Richard, S., Laurendeau, I., Vidaud, M., Kellermann, O., and Laplamche, J. L. (1999). Prion protein and neuronal differentiation: quantitative analysis of prnp gene expression in a murine inducible neuroectodermal progenitor. Microbes Infect. 1, 969-976. doi: 10.1016/S1286-4579(99)80514-0.
    • (1999) Microbes Infect. , vol.1 , pp. 969-976
    • Mouillet-Richard, S.1    Laurendeau, I.2    Vidaud, M.3    Kellermann, O.4    Laplamche, J.L.5
  • 89
    • 84896772790 scopus 로고    scopus 로고
    • Remodeling of marrow hematopoietic stem and progenitor cells by non-self ST6Gal-1 sialyltransferase
    • Nasirikenari, M., Veillon, L., Collins, C. C., Azadi, P., and Lau, J. T. (2014). Remodeling of marrow hematopoietic stem and progenitor cells by non-self ST6Gal-1 sialyltransferase. J. Biol. Chem. 289, 7178-7189. doi: 10.1074/jbc. M113.508457.
    • (2014) J. Biol. Chem. , vol.289 , pp. 7178-7189
    • Nasirikenari, M.1    Veillon, L.2    Collins, C.C.3    Azadi, P.4    Lau, J.T.5
  • 90
    • 84922728689 scopus 로고    scopus 로고
    • Ferrets exclusively synthesize Neu5Ac and express naturally humanized influenza A virus receptors
    • Ng, P. S., Böhm, R., Hartley-Tassell, L. E., Steen, J. A., Wang, H., Lukowski, S. W., et al. (2014). Ferrets exclusively synthesize Neu5Ac and express naturally humanized influenza A virus receptors. Nat. Commun. 5, 5750. doi: 10.1038/ncomms6750.
    • (2014) Nat. Commun. , vol.5 , pp. 5750
    • Ng, P.S.1    Böhm, R.2    Hartley-Tassell, L.E.3    Steen, J.A.4    Wang, H.5    Lukowski, S.W.6
  • 91
    • 33751572491 scopus 로고    scopus 로고
    • The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro
    • Nishina, K., Deleault, N. R., Mahal, S., Baskakov, I., Luhrs, T., Riek, R., et al. (2006). The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry 45, 14129-14139. doi: 10.1021/bi061526k.
    • (2006) Biochemistry , vol.45 , pp. 14129-14139
    • Nishina, K.1    Deleault, N.R.2    Mahal, S.3    Baskakov, I.4    Luhrs, T.5    Riek, R.6
  • 92
    • 34347251972 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein induce axonal degeneration in NTERA2-derived terminally differentiated neurons
    • Novitskaya, V., Makarava, N., Sylvester, I., Bronstein, I. B., and Baskakov, I. V. (2007). Amyloid fibrils of mammalian prion protein induce axonal degeneration in NTERA2-derived terminally differentiated neurons. J. Neurochem. 102, 398-407. doi: 10.1111/j.1471-4159.2007.04537.x.
    • (2007) J. Neurochem. , vol.102 , pp. 398-407
    • Novitskaya, V.1    Makarava, N.2    Sylvester, I.3    Bronstein, I.B.4    Baskakov, I.V.5
  • 93
    • 77954382827 scopus 로고    scopus 로고
    • Two amyloid states of the prion protein display significantly different folding patterns
    • Ostapchenko, V. G., Sawaya, M. R., Makarava, N., Savtchenko, R., Nilsson, K. P., Eisenberg, D., et al. (2010). Two amyloid states of the prion protein display significantly different folding patterns. J. Mol. Biol. 400, 908-921. doi: 10.1016/j.jmb.2010.05.051.
    • (2010) J. Mol. Biol. , vol.400 , pp. 908-921
    • Ostapchenko, V.G.1    Sawaya, M.R.2    Makarava, N.3    Savtchenko, R.4    Nilsson, K.P.5    Eisenberg, D.6
  • 94
    • 80052393715 scopus 로고    scopus 로고
    • Expression of prion protein in mouse erythroid progenitors and differentiating murine erythroleukemia cells
    • Panigaj, M., Glier, H., Wildova, M., and Holada, K. (2011). Expression of prion protein in mouse erythroid progenitors and differentiating murine erythroleukemia cells. PLoS ONE 6:e24599. doi: 10.1371/journal.pone.0024599.
    • (2011) PLoS ONE , vol.6
    • Panigaj, M.1    Glier, H.2    Wildova, M.3    Holada, K.4
  • 95
    • 13244273868 scopus 로고    scopus 로고
    • Biochemical fingerprints of prion diseases: scrapie prion protein in human prion diseases that share prion genotype and type
    • Pan, T., Li, R., Kang, S. C., Pastore, M., Wong, B. S., Ironside, J., et al. (2005). Biochemical fingerprints of prion diseases: scrapie prion protein in human prion diseases that share prion genotype and type. J. Neurochem. 92, 132-142. doi: 10.1111/j.1471-4159.2004.02859.x.
    • (2005) J. Neurochem. , vol.92 , pp. 132-142
    • Pan, T.1    Li, R.2    Kang, S.C.3    Pastore, M.4    Wong, B.S.5    Ironside, J.6
  • 96
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden, A. H., Head, M. W., Ritchie, D. L., Bell, J. E., and Ironside, J. W. (2004). Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 364, 527-529. doi: 10.1016/S0140-6736(04)16811-6.
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, J.E.4    Ironside, J.W.5
  • 97
    • 77749322732 scopus 로고    scopus 로고
    • Variant CJD infection in the spleen of a neurologically asymptomatic UK adult patient with haemophilia
    • Peden, A., McCardle, L., Head, M. W., Love, S., Ward, H. J., Cousens, S. N., et al. (2010). Variant CJD infection in the spleen of a neurologically asymptomatic UK adult patient with haemophilia. Haemophilia 16, 296-304. doi: 10.1111/j.1365-2516.2009.02181.x.
    • (2010) Haemophilia , vol.16 , pp. 296-304
    • Peden, A.1    McCardle, L.2    Head, M.W.3    Love, S.4    Ward, H.J.5    Cousens, S.N.6
  • 98
    • 0035086136 scopus 로고    scopus 로고
    • Strain-specified relative conformational stability of the scrapie prion protein
    • Peretz, D., Scott, M. R., Groth, D., Williamson, R. A., Burton, D. R., Cohen, F. E., et al. (2001). Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci. 10, 854-863. doi: 10.1110/ps.39201.
    • (2001) Protein Sci. , vol.10 , pp. 854-863
    • Peretz, D.1    Scott, M.R.2    Groth, D.3    Williamson, R.A.4    Burton, D.R.5    Cohen, F.E.6
  • 99
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. (1982). Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144. doi: 10.1126/science.6801762.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 101
    • 84880279999 scopus 로고    scopus 로고
    • Desialylation of Surface Receptors as a New Dimension in Cell Signaling
    • Pshezhetsky, A. V., and Ashmarina, L. I. (2013). Desialylation of Surface Receptors as a New Dimension in Cell Signaling. Biochemistry (Mosc) 78, 736-745. doi: 10.1134/S0006297913070067.
    • (2013) Biochemistry (Mosc) , vol.78 , pp. 736-745
    • Pshezhetsky, A.V.1    Ashmarina, L.I.2
  • 102
    • 84858766894 scopus 로고    scopus 로고
    • Regulatori circuits mediated by lectin-glycan interaction in autoimmunity and cancer
    • Rabinovich, G. A., and Croci, D. O. (2012). Regulatori circuits mediated by lectin-glycan interaction in autoimmunity and cancer. Immunity 36, 322-335. doi: 10.1016/j.immuni.2012.03.004.
    • (2012) Immunity , vol.36 , pp. 322-335
    • Rabinovich, G.A.1    Croci, D.O.2
  • 103
    • 84896908507 scopus 로고    scopus 로고
    • The Structure of the infectious prion protein: experimental data and molecular models
    • Requena, J. R., and Wille, H. (2014). The Structure of the infectious prion protein: experimental data and molecular models. Prion 8, 60-66. doi: 10.4161/pri.28368.
    • (2014) Prion , vol.8 , pp. 60-66
    • Requena, J.R.1    Wille, H.2
  • 104
    • 54249151500 scopus 로고    scopus 로고
    • Expression of sialyltransferase activity on intact human neutrophils
    • Rifat, S., Kang, T. J., Mann, D., Zhang, L., Puche, A. C., Stamatos, N. M., et al. (2008). Expression of sialyltransferase activity on intact human neutrophils. J. Leukoc. Biol. 84, 1075-1081. doi: 10.1189/jlb.0706462.
    • (2008) J. Leukoc. Biol. , vol.84 , pp. 1075-1081
    • Rifat, S.1    Kang, T.J.2    Mann, D.3    Zhang, L.4    Puche, A.C.5    Stamatos, N.M.6
  • 105
    • 0344239773 scopus 로고    scopus 로고
    • Glycosylation differences between the normal and pathogenic prion protein isoforms
    • Rudd, P. M., Endo, T., Colominas, C., Groth, D., Wheeler, S. F., Harvey, D. J., et al. (1999). Glycosylation differences between the normal and pathogenic prion protein isoforms. Proc. Natl. Acad. Sci. U.S.A. 96, 13044-13049. doi: 10.1073/pnas.96.23.13044.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13044-13049
    • Rudd, P.M.1    Endo, T.2    Colominas, C.3    Groth, D.4    Wheeler, S.F.5    Harvey, D.J.6
  • 107
    • 79960075550 scopus 로고    scopus 로고
    • Enhanced neural progenitor/stem cells self-renewal via the interaction of stress-inducible protein 1 with the prion protein
    • Santos, T. G., Silva, I. R., Costa-Silva, B., Lepigue, A. P., Martins, V. R., and Lopes, M. H. (2011). Enhanced neural progenitor/stem cells self-renewal via the interaction of stress-inducible protein 1 with the prion protein. Stem Cells 29, 1126-1136. doi: 10.1002/stem.664.
    • (2011) Stem Cells , vol.29 , pp. 1126-1136
    • Santos, T.G.1    Silva, I.R.2    Costa-Silva, B.3    Lepigue, A.P.4    Martins, V.R.5    Lopes, M.H.6
  • 108
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione, A., Syntyk, V., Leshchyns'ka, I., and Schachner, M. (2005). Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J. Cell Biol. 169 341-354. doi: 10.1083/jcb.200409127.
    • (2005) J. Cell Biol. , vol.169 , pp. 341-354
    • Santuccione, A.1    Syntyk, V.2    Leshchyns'ka, I.3    Schachner, M.4
  • 109
    • 0036884424 scopus 로고    scopus 로고
    • A blast from the past: clearance of apoptotic cells regulates immune responses
    • Savill, J., Dransfield, I., Gregory, C., and Haslett, C. (2002). A blast from the past: clearance of apoptotic cells regulates immune responses. Nat. Rev. Immunol. 2, 965-975. doi: 10.1038/nri957.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 965-975
    • Savill, J.1    Dransfield, I.2    Gregory, C.3    Haslett, C.4
  • 110
    • 80054018708 scopus 로고    scopus 로고
    • 'O-Acetylated sialic acids and their role in immune defence,'
    • ed A. M. Wu (New York, NY; Dordrecht; Heidelberg; London: Springer Science)
    • Schauer, R., Srinivasan, G. V., Wipfer, D., Kniep, B., and Schwartz-Albiez, R. (2011). "O-Acetylated sialic acids and their role in immune defence," in The Molecular Immunology of Complex Carbohydrates-3, ed A. M. Wu (New York, NY; Dordrecht; Heidelberg; London: Springer Science), 525-548.
    • (2011) The Molecular Immunology of Complex Carbohydrates-3 , pp. 525-548
    • Schauer, R.1    Srinivasan, G.V.2    Wipfer, D.3    Kniep, B.4    Schwartz-Albiez, R.5
  • 111
    • 0035861987 scopus 로고    scopus 로고
    • Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein
    • Schmitt-Ulms, G., Legname, G., Baldwin, M. A., Ball, H. L., Bradon, N., Bosque, P. J., et al. (2001). Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. J. Mol. Biol. 314, 1209-1225. doi: 10.1006/jmbi.2000.5183.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1209-1225
    • Schmitt-Ulms, G.1    Legname, G.2    Baldwin, M.A.3    Ball, H.L.4    Bradon, N.5    Bosque, P.J.6
  • 112
    • 84893727929 scopus 로고    scopus 로고
    • Association of prion protein genotype and scrapie prion protein type with cellular prion protein charge isoform profiles in cerebrospinal fluid of humans with sporadic or familial prion diseases
    • Schmitz, M., Lullmann, K., Zafar, S., Ebert, E., Wohlhage, M., Oikonomou, P., et al. (2014). Association of prion protein genotype and scrapie prion protein type with cellular prion protein charge isoform profiles in cerebrospinal fluid of humans with sporadic or familial prion diseases. Neurobiol. Aging 35, 1177-1188. doi: 10.1016/j.neurobiolaging.2013.11.010.
    • (2014) Neurobiol. Aging , vol.35 , pp. 1177-1188
    • Schmitz, M.1    Lullmann, K.2    Zafar, S.3    Ebert, E.4    Wohlhage, M.5    Oikonomou, P.6
  • 113
    • 62449089908 scopus 로고    scopus 로고
    • Prion interference with multiple prion isolates
    • Schutt, C. R., and Bartz, J. C. (2008). Prion interference with multiple prion isolates. Prion 2, 61-63. doi: 10.4161/pri.2.2.6806.
    • (2008) Prion , vol.2 , pp. 61-63
    • Schutt, C.R.1    Bartz, J.C.2
  • 114
    • 17644401028 scopus 로고    scopus 로고
    • Cell surface sialylation and ecto-sialyltransferase activity of human CD34 progenitors from peripheral blood and bone marrow
    • Schwartz-Albiez, R., Merling, A., Martin, S., Haas, R., and Gross, H. J. (2004). Cell surface sialylation and ecto-sialyltransferase activity of human CD34 progenitors from peripheral blood and bone marrow. Glycoconj. J. 21, 451-459. doi: 10.1007/s10719-004-5535-5.
    • (2004) Glycoconj. J. , vol.21 , pp. 451-459
    • Schwartz-Albiez, R.1    Merling, A.2    Martin, S.3    Haas, R.4    Gross, H.J.5
  • 115
    • 77951996350 scopus 로고    scopus 로고
    • Coinfecting prion strains compete for a limiting cellular resource
    • Shikiya, R. A., Ayers, J. I., Schutt, C. R., Kincaid, A. E., and Bartz, J. C. (2010). Coinfecting prion strains compete for a limiting cellular resource. J. Virol. 84, 5706-5714. doi: 10.1128/JVI.00243-10.
    • (2010) J. Virol. , vol.84 , pp. 5706-5714
    • Shikiya, R.A.1    Ayers, J.I.2    Schutt, C.R.3    Kincaid, A.E.4    Bartz, J.C.5
  • 116
    • 0032883356 scopus 로고    scopus 로고
    • Oral transmission and early lymphoid tropism of chronic wasting disease PrPres in mule deer fawns (Odocoileus hemionus)
    • Sigurdson, C. J., Williams, E. S., Miller, M. W., Spraker, T. R., O'Rourke, K. I., and Hoover, E. A. (1999). Oral transmission and early lymphoid tropism of chronic wasting disease PrPres in mule deer fawns (Odocoileus hemionus). J. Gen. Virol. 80, 2757-2764. doi: 10.1099/0022-1317-80-10-2757.
    • (1999) J. Gen. Virol. , vol.80 , pp. 2757-2764
    • Sigurdson, C.J.1    Williams, E.S.2    Miller, M.W.3    Spraker, T.R.4    O'Rourke, K.I.5    Hoover, E.A.6
  • 117
    • 12144291519 scopus 로고    scopus 로고
    • Cross-linking cellular prion protein triggers neuronal apoptosis in vivo
    • Solforosi, L., Criado, J. R., McGavern, D. B., Wirz, S., Sánchez-Alavez, M., Sugama, S., et al. (2004). Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science 303, 1514-1516. doi: 10.1126/science.1094273.
    • (2004) Science , vol.303 , pp. 1514-1516
    • Solforosi, L.1    Criado, J.R.2    McGavern, D.B.3    Wirz, S.4    Sánchez-Alavez, M.5    Sugama, S.6
  • 118
    • 79954607779 scopus 로고    scopus 로고
    • An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity
    • Solomon, I. H., Khatri, N., Biasini, E., Massignan, T., Huettner, J. E., and Harris, D. A. (2011). An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity. J. Biol. Chem. 286, 14724-14736. doi: 10.1074/jbc. M110.214973.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14724-14736
    • Solomon, I.H.1    Khatri, N.2    Biasini, E.3    Massignan, T.4    Huettner, J.E.5    Harris, D.A.6
  • 119
    • 0033038181 scopus 로고    scopus 로고
    • Host and transmissible spongiform encephalopathy agent strain control glycosylation of PrP
    • Somerville, R. A. (1999). Host and transmissible spongiform encephalopathy agent strain control glycosylation of PrP. J. Gen. Virol. 80, 1865-1872. doi: 10.1099/0022-1317-80-7-1865.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1865-1872
    • Somerville, R.A.1
  • 120
    • 84883742582 scopus 로고    scopus 로고
    • The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein
    • Sonati, T., Reimann, R. R., Falsig, J., Baral, P. K., O'Connor, T., Hornemann, S., et al. (2012). The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein. Nature 501, 102-106. doi: 10.1038/nature12402.
    • (2012) Nature , vol.501 , pp. 102-106
    • Sonati, T.1    Reimann, R.R.2    Falsig, J.3    Baral, P.K.4    O'Connor, T.5    Hornemann, S.6
  • 121
    • 33644816759 scopus 로고    scopus 로고
    • Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
    • Soto, C., Estrada, L., and Castilla, J. (2006). Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem. Sci. 31, 150-155. doi: 10.1016/j.tibs.2006.01.002.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 150-155
    • Soto, C.1    Estrada, L.2    Castilla, J.3
  • 122
    • 33745058355 scopus 로고    scopus 로고
    • Structural differences between TSEs strains investigated by FT-IR spectroscopy
    • Spassov, S., Beekes, M., and Naumann, D. (2006). Structural differences between TSEs strains investigated by FT-IR spectroscopy. Biochim. Biophys. Acta 1760, 1138-1149. doi: 10.1016/j.bbagen.2006.02.018.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1138-1149
    • Spassov, S.1    Beekes, M.2    Naumann, D.3
  • 124
    • 0026780714 scopus 로고
    • Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid
    • Stahl, N., Baldwin, M. A., Hecker, R., Pan, K. M., Burlingame, A. L., and Prusiner, S. B. (1992). Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid. Biochemistry 31, 5043-5053. doi: 10.1021/bi00136a600.
    • (1992) Biochemistry , vol.31 , pp. 5043-5053
    • Stahl, N.1    Baldwin, M.A.2    Hecker, R.3    Pan, K.M.4    Burlingame, A.L.5    Prusiner, S.B.6
  • 125
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., et al. (1993). Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002. doi: 10.1021/bi00059a016.
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6
  • 126
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl, N., Borchelt, D. R., Hsiao, K., and Prusiner, S. B. (1987). Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-240. doi: 10.1016/0092-8674(87)90150-4.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 127
    • 33644766915 scopus 로고    scopus 로고
    • Prion protein (PrPC) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis
    • Steele, A. D., Emsley, J. G., Ozdinler, P. H., Lindquist, S., and Macklis, J. D. (2006). Prion protein (PrPC) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc. Acad. Natl. Sci. U.S.A. 103, 3416-3421. doi: 10.1073/pnas.0511290103.
    • (2006) Proc. Acad. Natl. Sci. U.S.A. , vol.103 , pp. 3416-3421
    • Steele, A.D.1    Emsley, J.G.2    Ozdinler, P.H.3    Lindquist, S.4    Macklis, J.D.5
  • 128
    • 0033551196 scopus 로고    scopus 로고
    • Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions
    • Stimson, E., Hope, J., Chong, A., and Burlingame, A. L. (1999). Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38, 4885-4895. doi: 10.1021/bi982330q.
    • (1999) Biochemistry , vol.38 , pp. 4885-4895
    • Stimson, E.1    Hope, J.2    Chong, A.3    Burlingame, A.L.4
  • 129
    • 84904333974 scopus 로고    scopus 로고
    • Distinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice
    • Stöhr, J., Condello, C., Watts, C. J., Bloch, L., Oehler, A., Nick, M., et al. (2014). Distinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice. Proc. Acad. Natl. Sci. U.S.A. 111, 10329-10334. doi: 10.1073/pnas.1408968111.
    • (2014) Proc. Acad. Natl. Sci. U.S.A. , vol.111 , pp. 10329-10334
    • Stöhr, J.1    Condello, C.2    Watts, C.J.3    Bloch, L.4    Oehler, A.5    Nick, M.6
  • 130
    • 82555176496 scopus 로고    scopus 로고
    • Crystal structure of human prostate-specific antigen in a sandwich antibody complex
    • Stura, E. A., Muller, B. H., Bossus, M., Michel, S., Jolivet-Reynaud, C., and Ducancel, F. (2011). Crystal structure of human prostate-specific antigen in a sandwich antibody complex. J. Mol. Biol. 414, 530-544. doi: 10.1016/j.jmb.2011.10.007.
    • (2011) J. Mol. Biol. , vol.414 , pp. 530-544
    • Stura, E.A.1    Muller, B.H.2    Bossus, M.3    Michel, S.4    Jolivet-Reynaud, C.5    Ducancel, F.6
  • 131
    • 34247856087 scopus 로고    scopus 로고
    • Site-specific conformational studies of PrP amyloid fibrils revealed two cooperative folding domain within amyloid structure
    • Sun, Y., Breydo, L., Makarava, N., Yang, Q., Bocharova, O. V., and Baskakov, I. V. (2007). Site-specific conformational studies of PrP amyloid fibrils revealed two cooperative folding domain within amyloid structure. J. Biol. Chem. 282, 9090-9097. doi: 10.1074/jbc. M608623200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9090-9097
    • Sun, Y.1    Breydo, L.2    Makarava, N.3    Yang, Q.4    Bocharova, O.V.5    Baskakov, I.V.6
  • 132
    • 39049119728 scopus 로고    scopus 로고
    • Conformational stability of PrP amyloid firbils controls their smallest possible fragment size
    • Sun, Y., Makarava, N., Lee, C. I., Laksanalamai, P., Robb, F. T., and Baskakov, I. V. (2008). Conformational stability of PrP amyloid firbils controls their smallest possible fragment size. J. Mol. Biol. 376, 1155-1167. doi: 10.1016/j.jmb.2007.12.053.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1155-1167
    • Sun, Y.1    Makarava, N.2    Lee, C.I.3    Laksanalamai, P.4    Robb, F.T.5    Baskakov, I.V.6
  • 133
    • 0030868794 scopus 로고    scopus 로고
    • Changes in weight and compositions of major mambrane components oh human brain during the span of adult human life of Swedes
    • Svennerholm, L., Bostrom, K., and Jungbjer, B. (1997). Changes in weight and compositions of major mambrane components oh human brain during the span of adult human life of Swedes. Acta Neuropathol. 94, 345-352. doi: 10.1007/s004010050717.
    • (1997) Acta Neuropathol. , vol.94 , pp. 345-352
    • Svennerholm, L.1    Bostrom, K.2    Jungbjer, B.3
  • 134
    • 80052869514 scopus 로고    scopus 로고
    • Orally administered prion protein is incorporated by m cells and spreads into lymphoid tissues with macrophages in prion protein knockout mice
    • Takakura, I., Muiyazawa, K., Kanaya, T., Itani, W., Watanabe, K., Ohwada, S., et al. (2011). Orally administered prion protein is incorporated by m cells and spreads into lymphoid tissues with macrophages in prion protein knockout mice. Am. J. Pathol. 179, 1301-1309. doi: 10.1016/j.ajpath.2011.05.058.
    • (2011) Am. J. Pathol. , vol.179 , pp. 1301-1309
    • Takakura, I.1    Muiyazawa, K.2    Kanaya, T.3    Itani, W.4    Watanabe, K.5    Ohwada, S.6
  • 135
    • 45749155148 scopus 로고    scopus 로고
    • Characterization of mouse sialylatransferase gene: their evolution and diversity
    • Takashima, S. (2008). Characterization of mouse sialylatransferase gene: their evolution and diversity. Biosci. Biotechnol. Biochem. 72, 1155-1167. doi: 10.1271/bbb.80025.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1155-1167
    • Takashima, S.1
  • 136
    • 2242438080 scopus 로고    scopus 로고
    • Characterization of the second type of human beta-galactoside alpha 2,6-sialyltransferase (ST6Gal II), which sialylates Galbeta 1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes
    • Takashima, S., Truji, S., and Tsujimoto, M. (2002). Characterization of the second type of human beta-galactoside alpha 2,6-sialyltransferase (ST6Gal II), which sialylates Galbeta 1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes. J. Biol. Chem. 277, 45719-45728. doi: 10.1074/jbc. M206808200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45719-45728
    • Takashima, S.1    Truji, S.2    Tsujimoto, M.3
  • 137
    • 0141703289 scopus 로고    scopus 로고
    • Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal I and II
    • Takashima, S., Tsuji, S., and Tsujimoto, M. (2003). Comparison of the enzymatic properties of mouse beta-galactoside alpha2,6-sialyltransferases, ST6Gal I and II. J. Biochem. 134, 287-296. doi: 10.1093/jb/mvg142.
    • (2003) J. Biochem. , vol.134 , pp. 287-296
    • Takashima, S.1    Tsuji, S.2    Tsujimoto, M.3
  • 138
    • 78249275848 scopus 로고    scopus 로고
    • Noninvasive imaging of dendrimer-type N-glycan clusters: in vivo dynamics dependence on oligosaccharide structure
    • Tanaka, K., Siwu, E. R. O., Minami, K., Hasegawa, K., Nozaki, S., Kanayama, Y., et al. (2010). Noninvasive imaging of dendrimer-type N-glycan clusters: in vivo dynamics dependence on oligosaccharide structure. Angew. Chem. Int. Ed. Engl. 49, 8195-8200. doi: 10.1002/anie.201000892.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 8195-8200
    • Tanaka, K.1    Siwu, E.R.O.2    Minami, K.3    Hasegawa, K.4    Nozaki, S.5    Kanayama, Y.6
  • 139
    • 4043137988 scopus 로고    scopus 로고
    • Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein
    • Thomzig, A., Spassov, S., Friedrich, M., Naumann, D., and Beekes, M. (2004). Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein. J. Biol. Chem. 279, 33854. doi: 10.1074/jbc.m403730200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33854
    • Thomzig, A.1    Spassov, S.2    Friedrich, M.3    Naumann, D.4    Beekes, M.5
  • 140
    • 0023676109 scopus 로고
    • Purification and properties of the cellular and scrapie hamster prion proteins
    • Turk, E., Teplow, D. B., Hood, L. E., and Prusiner, S. B. (1988). Purification and properties of the cellular and scrapie hamster prion proteins. Eur. J. Biochem. 176, 21-30. doi: 10.1111/j.1432-1033.1988.tb14246.x.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 21-30
    • Turk, E.1    Teplow, D.B.2    Hood, L.E.3    Prusiner, S.B.4
  • 141
    • 84862898615 scopus 로고    scopus 로고
    • The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc)
    • Turnbaugh, J. A., Unterberger, U., Saá, P., Massignan, T., Fluharty, B. R., Bowman, F. P., et al. (2012). The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc). J. Neurosci. 32, 8817-8830. doi: 10.1523/JNEUROSCI.1103-12.2012.
    • (2012) J. Neurosci. , vol.32 , pp. 8817-8830
    • Turnbaugh, J.A.1    Unterberger, U.2    Saá, P.3    Massignan, T.4    Fluharty, B.R.5    Bowman, F.P.6
  • 142
    • 78149307698 scopus 로고    scopus 로고
    • The a-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel á-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance
    • Tycko, R., Savtchenko, R., Ostapchenko, V. G., Makarava, N., and Baskakov, I. V. (2010). The a-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel á-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance. Biochemistry 49, 9488-9497. doi: 10.1021/bi1013134.
    • (2010) Biochemistry , vol.49 , pp. 9488-9497
    • Tycko, R.1    Savtchenko, R.2    Ostapchenko, V.G.3    Makarava, N.4    Baskakov, I.V.5
  • 143
    • 0032813946 scopus 로고    scopus 로고
    • Suppression of PrP(Sc)-and HIV-1 gp120 induced neuronal cell death by sulfated colominic acid
    • Ushijima, H., Perovic, S., Leuck, J., Rytik, P. G., Müller, W. E., and Schröder, H. C. (1999). Suppression of PrP(Sc)-and HIV-1 gp120 induced neuronal cell death by sulfated colominic acid. J. Neurovirol. 5, 289-299. doi: 10.3109/13550289909015815.
    • (1999) J. Neurovirol. , vol.5 , pp. 289-299
    • Ushijima, H.1    Perovic, S.2    Leuck, J.3    Rytik, P.G.4    Müller, W.E.5    Schröder, H.C.6
  • 144
    • 0002530622 scopus 로고    scopus 로고
    • 'Sialic acids,'
    • eds A. Varki, R. Cummings, J. Esko, H. Freeze, G. Hart, and J. Marth (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • Varki, A. (1999). "Sialic acids," in Essentials of Glycobiology, eds A. Varki, R. Cummings, J. Esko, H. Freeze, G. Hart, and J. Marth (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), 195-210.
    • (1999) Essentials of Glycobiology , pp. 195-210
    • Varki, A.1
  • 145
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • Varki, A. (2008). Sialic acids in human health and disease. Trends Mol. Med. 14, 351-360. doi: 10.1016/j.molmed.2008.06.002.
    • (2008) Trends Mol. Med. , vol.14 , pp. 351-360
    • Varki, A.1
  • 146
    • 77952369047 scopus 로고    scopus 로고
    • Uniquely human evolution of sialic acid genetics and biology
    • Varki, A. (2010). Uniquely human evolution of sialic acid genetics and biology. Proc. Acad. Natl. Sci. U.S.A. 107, 8939-8946. doi: 10.1073/pnas.0914634107.
    • (2010) Proc. Acad. Natl. Sci. U.S.A. , vol.107 , pp. 8939-8946
    • Varki, A.1
  • 147
    • 33845704378 scopus 로고    scopus 로고
    • Junctional expression of the prion protein PrPC by brain endothelial cells: a role in trans-andothelial migration of human monocytes
    • Viegas, P., Chaverot, N., Enslen, H., Perrière, N., Couraud, P. O., and Cazaubon, S. (2006). Junctional expression of the prion protein PrPC by brain endothelial cells: a role in trans-andothelial migration of human monocytes. J. Cell Sci. 119, 4634-4643. doi: 10.1242/jcs.03222.
    • (2006) J. Cell Sci. , vol.119 , pp. 4634-4643
    • Viegas, P.1    Chaverot, N.2    Enslen, H.3    Perrière, N.4    Couraud, P.O.5    Cazaubon, S.6
  • 148
    • 10044224475 scopus 로고    scopus 로고
    • Human prion protein with valine 129 prevents expression of variant CJD phenotype
    • Wadsworth, J. D., Asante, E. A., Desbruslais, M., Linehan, J. M., Joiner, S., Gowland, I., et al. (2004). Human prion protein with valine 129 prevents expression of variant CJD phenotype. Science 306, 1793-1796. doi: 10.1126/science.1103932.
    • (2004) Science , vol.306 , pp. 1793-1796
    • Wadsworth, J.D.1    Asante, E.A.2    Desbruslais, M.3    Linehan, J.M.4    Joiner, S.5    Gowland, I.6
  • 149
    • 0035928432 scopus 로고    scopus 로고
    • Tissues distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunobloting assay
    • Wadsworth, J. D., Joiner, S., Hill, A. F., Campbell, T. A., Desbruslais, M., Luthert, P. J., et al. (2001). Tissues distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunobloting assay. Lancet 358, 171-180. doi: 10.1016/S0140-6736(01)05403-4.
    • (2001) Lancet , vol.358 , pp. 171-180
    • Wadsworth, J.D.1    Joiner, S.2    Hill, A.F.3    Campbell, T.A.4    Desbruslais, M.5    Luthert, P.J.6
  • 150
    • 84937392013 scopus 로고    scopus 로고
    • Neurodegenerative diseases: expanding the prion concept
    • Walker, L. C., and Jucker, M. (2015). Neurodegenerative diseases: expanding the prion concept. Annu. Rev. Neurosci. 38, 87-103. doi: 10.1146/annurev-neuro-071714-033828.
    • (2015) Annu. Rev. Neurosci. , vol.38 , pp. 87-103
    • Walker, L.C.1    Jucker, M.2
  • 151
    • 84923766678 scopus 로고    scopus 로고
    • a2,6-linked sialic acids on N-glycans modulate the adhesion of hepatocarcinoma cells to lymph nodes
    • Wang, S., Chen, X., Wei, A., Yu, X., Niang, B., and Zhang, J. (2015). a2,6-linked sialic acids on N-glycans modulate the adhesion of hepatocarcinoma cells to lymph nodes. Tumor Biol. 36, 885-892. doi: 10.1007/s13277-014-2638-x.
    • (2015) Tumor Biol. , vol.36 , pp. 885-892
    • Wang, S.1    Chen, X.2    Wei, A.3    Yu, X.4    Niang, B.5    Zhang, J.6
  • 152
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
    • Wasmer, C., Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R., and Meier, B. H. (2008). Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science 319, 1523-1526. doi: 10.1126/science.1151839.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 153
    • 84904322386 scopus 로고    scopus 로고
    • Serial propagation of distinct strains of Aβ prions from Alzheimer's disease patients
    • Watts, C. J., Condello, C., Stöhr, J., Oehler, A., Lee, J., DeArmond, S. J., et al. (2014). Serial propagation of distinct strains of Aβ prions from Alzheimer's disease patients. Proc. Acad. Natl. Sci. U.S.A. 111, 10323-10328. doi: 10.1073/pnas.1408900111.
    • (2014) Proc. Acad. Natl. Sci. U.S.A. , vol.111 , pp. 10323-10328
    • Watts, C.J.1    Condello, C.2    Stöhr, J.3    Oehler, A.4    Lee, J.5    DeArmond, S.J.6
  • 154
    • 80053228890 scopus 로고    scopus 로고
    • A nine amino acid domain is essential for mutant prion protein toxicity
    • Westergard, L., Turnbaugh, J. A., and Harris, D. A. (2011). A nine amino acid domain is essential for mutant prion protein toxicity. J. Neurosci. 31, 14005-14017. doi: 10.1523/JNEUROSCI.1243-11.2011.
    • (2011) J. Neurosci. , vol.31 , pp. 14005-14017
    • Westergard, L.1    Turnbaugh, J.A.2    Harris, D.A.3
  • 155
  • 157
    • 33845227845 scopus 로고    scopus 로고
    • Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jakob disease associated with blood transfusion: a case report
    • Wroe, S. J., Pal, S., Siddique, D., Hyare, H., Macfariane, R., Joiner, S., et al. (2006). Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jakob disease associated with blood transfusion: a case report. Lancet 368, 2061-2067. doi: 10.1016/S0140-6736(06)69835-8.
    • (2006) Lancet , vol.368 , pp. 2061-2067
    • Wroe, S.J.1    Pal, S.2    Siddique, D.3    Hyare, H.4    Macfariane, R.5    Joiner, S.6
  • 158
    • 4644259154 scopus 로고    scopus 로고
    • Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes
    • Zanusso, G., Farinazzo, A., Prelli, F., Fiorini, F., Gelati, M., Ferrari, S., et al. (2004). Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes. J. Biol. Chem. 279, 38936-38942. doi: 10.1074/jbc. M405468200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38936-38942
    • Zanusso, G.1    Farinazzo, A.2    Prelli, F.3    Fiorini, F.4    Gelati, M.5    Ferrari, S.6
  • 159
    • 33144456321 scopus 로고    scopus 로고
    • Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal
    • Zhang, C. C., Steele, A. D., Lindquist, S., and Lodish, H. F. (2006). Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proc. Acad. Natl. Sci. U.S.A. 103, 21814-21819. doi: 10.1073/pnas.0510577103.
    • (2006) Proc. Acad. Natl. Sci. U.S.A. , vol.103 , pp. 21814-21819
    • Zhang, C.C.1    Steele, A.D.2    Lindquist, S.3    Lodish, H.F.4
  • 160
    • 84879263293 scopus 로고    scopus 로고
    • Modification of glycosylation mediates the invasive properties of murine hepatocarcinoma cell lines to lymph nodes
    • Zhang, Z., Sun, J., Hao, L., Liu, C., Ma, H., and Jia, L. (2013). Modification of glycosylation mediates the invasive properties of murine hepatocarcinoma cell lines to lymph nodes. PLoS ONE 8:e65218. doi: 10.1371/journal.pone.0065218.
    • (2013) PLoS ONE , vol.8
    • Zhang, Z.1    Sun, J.2    Hao, L.3    Liu, C.4    Ma, H.5    Jia, L.6


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