메뉴 건너뛰기




Volumn 54, Issue 30, 2015, Pages 4731-4740

RNA Binds to Tau Fibrils and Sustains Template-Assisted Growth

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON SPIN RESONANCE SPECTROSCOPY; MAGNETIC RESONANCE; PARAMAGNETIC RESONANCE; POLYSACCHARIDES;

EID: 84938629772     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00453     Document Type: Article
Times cited : (53)

References (69)
  • 1
    • 0033850407 scopus 로고    scopus 로고
    • Tau protein isoforms, phosphorylation and role in neurodegenerative disorders
    • Buee, L., Bussiere, T., Buee-Scherrer, V., Delacourte, A., and Hof, P. R. (2000) Tau protein isoforms, phosphorylation and role in neurodegenerative disorders Brain Res. Rev. 33, 95-130 10.1016/S0165-0173(00)00019-9
    • (2000) Brain Res. Rev. , vol.33 , pp. 95-130
    • Buee, L.1    Bussiere, T.2    Buee-Scherrer, V.3    Delacourte, A.4    Hof, P.R.5
  • 2
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H. and Braak, E. (1991) Neuropathological stageing of Alzheimer-related changes Acta Neuropathol. 82, 239-259 10.1007/BF00308809
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 3
    • 33749150163 scopus 로고    scopus 로고
    • Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
    • Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., and Del Tredici, K. (2006) Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry Acta Neuropathol. 112, 389-404 10.1007/s00401-006-0127-z
    • (2006) Acta Neuropathol. , vol.112 , pp. 389-404
    • Braak, H.1    Alafuzoff, I.2    Arzberger, T.3    Kretzschmar, H.4    Del Tredici, K.5
  • 7
    • 84861758226 scopus 로고    scopus 로고
    • Trans-cellular Propagation of Tau Aggregation by Fibrillar Species
    • Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., and Diamond, M. I. (2012) Trans-cellular Propagation of Tau Aggregation by Fibrillar Species J. Biol. Chem. 287, 19440-19451 10.1074/jbc.M112.346072
    • (2012) J. Biol. Chem. , vol.287 , pp. 19440-19451
    • Kfoury, N.1    Holmes, B.B.2    Jiang, H.3    Holtzman, D.M.4    Diamond, M.I.5
  • 8
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms
    • Goedert, M., Spillantini, M. G., Cairns, N. J., and Crowther, R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms Neuron 8, 159-168 10.1016/0896-6273(92)90117-V
    • (1992) Neuron , vol.8 , pp. 159-168
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 9
    • 84877906835 scopus 로고    scopus 로고
    • Tau pathology and neurodegeneration
    • Spillantini, M. G. and Goedert, M. (2013) Tau pathology and neurodegeneration Lancet Neurol. 12, 609-622 10.1016/S1474-4422(13)70090-5
    • (2013) Lancet Neurol. , vol.12 , pp. 609-622
    • Spillantini, M.G.1    Goedert, M.2
  • 11
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • Novak, M., Kabat, J., and Wischik, C. M. (1993) Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament EMBO J. 12, 365-370
    • (1993) EMBO J. , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 14
    • 84875279731 scopus 로고    scopus 로고
    • The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush
    • Wegmann, S., Medalsy, I. D., Mandelkow, E., and Muller, D. J. (2013) The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush Proc. Natl. Acad. Sci. U. S. A. 110, E313-321 10.1073/pnas.1212100110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. E313-E321
    • Wegmann, S.1    Medalsy, I.D.2    Mandelkow, E.3    Muller, D.J.4
  • 15
  • 16
    • 0037126688 scopus 로고    scopus 로고
    • Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments
    • Barghorn, S. and Mandelkow, E. (2002) Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments Biochemistry 41, 14885-14896 10.1021/bi026469j
    • (2002) Biochemistry , vol.41 , pp. 14885-14896
    • Barghorn, S.1    Mandelkow, E.2
  • 18
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure
    • von Bergen, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (2001) Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure J. Biol. Chem. 276, 48165-48174 10.1074/jbc.M105196200
    • (2001) J. Biol. Chem. , vol.276 , pp. 48165-48174
    • Von Bergen, M.1    Barghorn, S.2    Li, L.3    Marx, A.4    Biernat, J.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 19
    • 0042307302 scopus 로고    scopus 로고
    • Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure
    • Berriman, J., Serpell, L. C., Oberg, K. A., Fink, A. L., Goedert, M., and Crowther, R. A. (2003) Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure Proc. Natl. Acad. Sci. U. S. A. 100, 9034-9038 10.1073/pnas.1530287100
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9034-9038
    • Berriman, J.1    Serpell, L.C.2    Oberg, K.A.3    Fink, A.L.4    Goedert, M.5    Crowther, R.A.6
  • 21
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., and Crowther, R. A. (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans Nature 383, 550-553 10.1038/383550a0
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 22
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction
    • Perez, M., Valpuesta, J. M., Medina, M., Montejo de Garcini, E., and Avila, J. (1996) Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction J. Neurochem. 67, 1183-1190 10.1046/j.1471-4159.1996.67031183.x
    • (1996) J. Neurochem. , vol.67 , pp. 1183-1190
    • Perez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 23
    • 0030923223 scopus 로고    scopus 로고
    • Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease
    • Wilson, D. M. and Binder, L. I. (1997) Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease Am. J. Pathol. 150, 2181-2195
    • (1997) Am. J. Pathol. , vol.150 , pp. 2181-2195
    • Wilson, D.M.1    Binder, L.I.2
  • 24
    • 0033539689 scopus 로고    scopus 로고
    • Ligand-dependent tau filament formation: implications for Alzheimer's disease progression
    • King, M. E., Ahuja, V., Binder, L. I., and Kuret, J. (1999) Ligand-dependent tau filament formation: implications for Alzheimer's disease progression Biochemistry 38, 14851-14859 10.1021/bi9911839
    • (1999) Biochemistry , vol.38 , pp. 14851-14859
    • King, M.E.1    Ahuja, V.2    Binder, L.I.3    Kuret, J.4
  • 25
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments
    • Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (1996) RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments FEBS Lett. 399, 344-349 10.1016/S0014-5793(96)01386-5
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 26
    • 0031439109 scopus 로고    scopus 로고
    • Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation
    • Hasegawa, M., Crowther, R. A., Jakes, R., and Goedert, M. (1997) Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfation J. Biol. Chem. 272, 33118-33124 10.1074/jbc.272.52.33118
    • (1997) J. Biol. Chem. , vol.272 , pp. 33118-33124
    • Hasegawa, M.1    Crowther, R.A.2    Jakes, R.3    Goedert, M.4
  • 27
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • Crowther, R. A., Olesen, O. F., Jakes, R., and Goedert, M. (1992) The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease FEBS Lett. 309, 199-202 10.1016/0014-5793(92)81094-3
    • (1992) FEBS Lett. , vol.309 , pp. 199-202
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 28
    • 0028121105 scopus 로고
    • Assembly of Alzheimer-like filaments from full-length tau protein
    • Crowther, R. A., Olesen, O. F., Smith, M. J., Jakes, R., and Goedert, M. (1994) Assembly of Alzheimer-like filaments from full-length tau protein FEBS Lett. 337, 135-138 10.1016/0014-5793(94)80260-2
    • (1994) FEBS Lett. , vol.337 , pp. 135-138
    • Crowther, R.A.1    Olesen, O.F.2    Smith, M.J.3    Jakes, R.4    Goedert, M.5
  • 29
    • 0027308924 scopus 로고
    • Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding
    • Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., and Lee, V. M. (1993) Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding Neuron 10, 1089-1099 10.1016/0896-6273(93)90057-X
    • (1993) Neuron , vol.10 , pp. 1089-1099
    • Bramblett, G.T.1    Goedert, M.2    Jakes, R.3    Merrick, S.E.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 30
    • 0027338266 scopus 로고
    • Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding
    • Biernat, J., Gustke, N., Drewes, G., Mandelkow, E. M., and Mandelkow, E. (1993) Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding Neuron 11, 153-163 10.1016/0896-6273(93)90279-Z
    • (1993) Neuron , vol.11 , pp. 153-163
    • Biernat, J.1    Gustke, N.2    Drewes, G.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 31
    • 0036830506 scopus 로고    scopus 로고
    • Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis
    • Li, L., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2002) Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis J. Biol. Chem. 277, 41390-41400 10.1074/jbc.M206334200
    • (2002) J. Biol. Chem. , vol.277 , pp. 41390-41400
    • Li, L.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 32
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick, G. N., Zukerberg, L., Nikolic, M., de la Monte, S., Dikkes, P., and Tsai, L. H. (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration Nature 402, 615-622 10.1038/45159
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    De La Monte, S.4    Dikkes, P.5    Tsai, L.H.6
  • 33
    • 0031045396 scopus 로고    scopus 로고
    • Sequestration of RNA in Alzheimer's disease neurofibrillary tangles and senile plaques
    • Ginsberg, S. D., Crino, P. B., Lee, V. M., Eberwine, J. H., and Trojanowski, J. Q. (1997) Sequestration of RNA in Alzheimer's disease neurofibrillary tangles and senile plaques Ann. Neurol. 41, 200-209 10.1002/ana.410410211
    • (1997) Ann. Neurol. , vol.41 , pp. 200-209
    • Ginsberg, S.D.1    Crino, P.B.2    Lee, V.M.3    Eberwine, J.H.4    Trojanowski, J.Q.5
  • 35
    • 78549275132 scopus 로고    scopus 로고
    • Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease
    • Siddiqua, A. and Margittai, M. (2010) Three- and four-repeat Tau coassemble into heterogeneous filaments: an implication for Alzheimer disease J. Biol. Chem. 285, 37920-37926 10.1074/jbc.M110.185728
    • (2010) J. Biol. Chem. , vol.285 , pp. 37920-37926
    • Siddiqua, A.1    Margittai, M.2
  • 36
    • 79956223051 scopus 로고    scopus 로고
    • Variations in Filament Conformation Dictate Seeding Barrier between Three- and Four-Repeat Tau
    • Dinkel, P. D., Siddiqua, A., Huynh, H., Shah, M., and Margittai, M. (2011) Variations in Filament Conformation Dictate Seeding Barrier between Three- and Four-Repeat Tau Biochemistry 50, 4330-4336 10.1021/bi2004685
    • (2011) Biochemistry , vol.50 , pp. 4330-4336
    • Dinkel, P.D.1    Siddiqua, A.2    Huynh, H.3    Shah, M.4    Margittai, M.5
  • 38
    • 80655128134 scopus 로고    scopus 로고
    • Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein
    • Ramachandran, G. and Udgaonkar, J. B. (2011) Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein J. Biol. Chem. 286, 38948-38959 10.1074/jbc.M111.271874
    • (2011) J. Biol. Chem. , vol.286 , pp. 38948-38959
    • Ramachandran, G.1    Udgaonkar, J.B.2
  • 39
    • 84863983902 scopus 로고    scopus 로고
    • Evidence for the existence of a secondary pathway for fibril growth during the aggregation of tau
    • Ramachandran, G. and Udgaonkar, J. B. (2012) Evidence for the existence of a secondary pathway for fibril growth during the aggregation of tau J. Mol. Biol. 421, 296-314 10.1016/j.jmb.2012.01.007
    • (2012) J. Mol. Biol. , vol.421 , pp. 296-314
    • Ramachandran, G.1    Udgaonkar, J.B.2
  • 40
    • 24144459823 scopus 로고    scopus 로고
    • Evaluating triggers and enhancers of tau fibrillization
    • Kuret, J., Congdon, E. E., Li, G., Yin, H., Yu, X., and Zhong, Q. (2005) Evaluating triggers and enhancers of tau fibrillization Microsc. Res. Tech. 67, 141-155 10.1002/jemt.20187
    • (2005) Microsc. Res. Tech. , vol.67 , pp. 141-155
    • Kuret, J.1    Congdon, E.E.2    Li, G.3    Yin, H.4    Yu, X.5    Zhong, Q.6
  • 41
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai, M. and Langen, R. (2004) Template-assisted filament growth by parallel stacking of tau Proc. Natl. Acad. Sci. U. S. A. 101, 10278-10283 10.1073/pnas.0401911101
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 42
    • 0020482581 scopus 로고
    • A novel reversible thiol-specific spin label: papain active site labeling and inhibition
    • Berliner, L. J., Grunwald, J., Hankovszky, H. O., and Hideg, K. (1982) A novel reversible thiol-specific spin label: papain active site labeling and inhibition Anal. Biochem. 119, 450-455 10.1016/0003-2697(82)90612-1
    • (1982) Anal. Biochem. , vol.119 , pp. 450-455
    • Berliner, L.J.1    Grunwald, J.2    Hankovszky, H.O.3    Hideg, K.4
  • 43
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure
    • von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E. M., and Mandelkow, E. (2000) Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure Proc. Natl. Acad. Sci. U. S. A. 97, 5129-5134 10.1073/pnas.97.10.5129
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5129-5134
    • Von Bergen, M.1    Friedhoff, P.2    Biernat, J.3    Heberle, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 44
    • 57649128935 scopus 로고    scopus 로고
    • Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy
    • Margittai, M. and Langen, R. (2008) Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy Q. Rev. Biophys. 41, 265-297 10.1017/S0033583508004733
    • (2008) Q. Rev. Biophys. , vol.41 , pp. 265-297
    • Margittai, M.1    Langen, R.2
  • 46
    • 0032516493 scopus 로고    scopus 로고
    • Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution
    • Friedhoff, P., Schneider, A., Mandelkow, E. M., and Mandelkow, E. (1998) Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution Biochemistry 37, 10223-10230 10.1021/bi980537d
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 47
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type Tau fibrils specified by templated conformation change
    • Frost, B., Ollesch, J., Wille, H., and Diamond, M. I. (2009) Conformational diversity of wild-type Tau fibrils specified by templated conformation change J. Biol. Chem. 284, 3546-3551 10.1074/jbc.M805627200
    • (2009) J. Biol. Chem. , vol.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 48
    • 84860380323 scopus 로고    scopus 로고
    • Cross-seeding and conformational selection between three- and four-repeat human Tau proteins
    • Yu, X., Luo, Y., Dinkel, P., Zheng, J., Wei, G., Margittai, M., Nussinov, R., and Ma, B. (2012) Cross-seeding and conformational selection between three- and four-repeat human Tau proteins J. Biol. Chem. 287, 14950-14959 10.1074/jbc.M112.340794
    • (2012) J. Biol. Chem. , vol.287 , pp. 14950-14959
    • Yu, X.1    Luo, Y.2    Dinkel, P.3    Zheng, J.4    Wei, G.5    Margittai, M.6    Nussinov, R.7    Ma, B.8
  • 49
    • 0030936599 scopus 로고    scopus 로고
    • Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau
    • Jicha, G. A., Bowser, R., Kazam, I. G., and Davies, P. (1997) Alz-50 and MC-1, a new monoclonal antibody raised to paired helical filaments, recognize conformational epitopes on recombinant tau J. Neurosci. Res. 48, 128-132 10.1002/(SICI)1097-4547(19970415)48:2<128::AID-JNR5>3.0.CO;2-E
    • (1997) J. Neurosci. Res. , vol.48 , pp. 128-132
    • Jicha, G.A.1    Bowser, R.2    Kazam, I.G.3    Davies, P.4
  • 51
    • 84867390250 scopus 로고    scopus 로고
    • Identification of an aggregation-prone structure of tau
    • Elbaum-Garfinkle, S. and Rhoades, E. (2012) Identification of an aggregation-prone structure of tau J. Am. Chem. Soc. 134, 16607-16613 10.1021/ja305206m
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16607-16613
    • Elbaum-Garfinkle, S.1    Rhoades, E.2
  • 52
    • 33750045702 scopus 로고    scopus 로고
    • Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopy
    • Sibille, N., Sillen, A., Leroy, A., Wieruszeski, J. M., Mulloy, B., Landrieu, I., and Lippens, G. (2006) Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopy Biochemistry 45, 12560-12572 10.1021/bi060964o
    • (2006) Biochemistry , vol.45 , pp. 12560-12572
    • Sibille, N.1    Sillen, A.2    Leroy, A.3    Wieruszeski, J.M.4    Mulloy, B.5    Landrieu, I.6    Lippens, G.7
  • 53
  • 59
    • 0026548436 scopus 로고
    • Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease
    • Snow, A. D., Mar, H., Nochlin, D., Kresse, H., and Wight, T. N. (1992) Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease J. Histochem. Cytochem. 40, 105-113 10.1177/40.1.1370306
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 105-113
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kresse, H.4    Wight, T.N.5
  • 60
    • 0026468915 scopus 로고
    • Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease
    • Su, J. H., Cummings, B. J., and Cotman, C. W. (1992) Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease Neuroscience 51, 801-813 10.1016/0306-4522(92)90521-3
    • (1992) Neuroscience , vol.51 , pp. 801-813
    • Su, J.H.1    Cummings, B.J.2    Cotman, C.W.3
  • 61
    • 0027209456 scopus 로고
    • Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease
    • DeWitt, D. A., Silver, J., Canning, D. R., and Perry, G. (1993) Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease Exp. Neurol. 121, 149-152 10.1006/exnr.1993.1081
    • (1993) Exp. Neurol. , vol.121 , pp. 149-152
    • Dewitt, D.A.1    Silver, J.2    Canning, D.R.3    Perry, G.4
  • 63
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge, J. and Clarke, A. R. (2007) A general model of prion strains and their pathogenicity Science 318, 930-936 10.1126/science.1138718
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 64
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault, N. R., Lucassen, R. W., and Supattapone, S. (2003) RNA molecules stimulate prion protein conversion Nature 425, 717-720 10.1038/nature01979
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 66
    • 22844438894 scopus 로고    scopus 로고
    • Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • Deleault, N. R., Geoghegan, J. C., Nishina, K., Kascsak, R., Williamson, R. A., and Supattapone, S. (2005) Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions J. Biol. Chem. 280, 26873-26879 10.1074/jbc.M503973200
    • (2005) J. Biol. Chem. , vol.280 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 67
    • 84861848298 scopus 로고    scopus 로고
    • Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids
    • Deleault, N. R., Piro, J. R., Walsh, D. J., Wang, F., Ma, J., Geoghegan, J. C., and Supattapone, S. (2012) Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids Proc. Natl. Acad. Sci. U. S. A. 109, 8546-8551 10.1073/pnas.1204498109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 8546-8551
    • Deleault, N.R.1    Piro, J.R.2    Walsh, D.J.3    Wang, F.4    Ma, J.5    Geoghegan, J.C.6    Supattapone, S.7
  • 69
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang, F., Wang, X., Yuan, C. G., and Ma, J. (2010) Generating a prion with bacterially expressed recombinant prion protein Science 327, 1132-1135 10.1126/science.1183748
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.