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Volumn 51, Issue 43, 2012, Pages 8597-8607

FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions

Author keywords

[No Author keywords available]

Indexed keywords

DIFFERENT EFFECTS; DIFFERENTIAL EFFECT; DISEASE PROGRESSION; FILAMENT MORPHOLOGY; FRONTOTEMPORAL DEMENTIAS; HYPERPHOSPHORYLATION; IN-VITRO; MICROTUBULE ASSEMBLY; MICROTUBULE ASSOCIATED PROTEIN; MICROTUBULES; MODEL SYSTEM; SECONDARY STRUCTURES; TAUOPATHIES; TO EFFECT; WILD TYPES;

EID: 84868104221     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3010818     Document Type: Article
Times cited : (61)

References (61)
  • 3
    • 0344505849 scopus 로고    scopus 로고
    • Tau interacts with src-family non-receptor tyrosine kinases
    • Lee, G., Newman, S. T., Gard, D. L., Band, H., and Panchamoorthy, G. (1998) Tau interacts with src-family non-receptor tyrosine kinases J. Cell Sci. 111, 3167-3177
    • (1998) J. Cell Sci. , vol.111 , pp. 3167-3177
    • Lee, G.1    Newman, S.T.2    Gard, D.L.3    Band, H.4    Panchamoorthy, G.5
  • 4
    • 0026729767 scopus 로고
    • Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons
    • Chen, J., Kanai, Y., Cowan, N. J., and Hirokawa, N. (1992) Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons Nature 360, 674-677
    • (1992) Nature , vol.360 , pp. 674-677
    • Chen, J.1    Kanai, Y.2    Cowan, N.J.3    Hirokawa, N.4
  • 5
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt, R., Leger, J., and Lee, G. (1995) Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain J. Cell Biol. 131, 1327-1340
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 6
    • 0024387161 scopus 로고
    • Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain
    • Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., and Crowther, R. A. (1989) Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain EMBO J. 8, 393-399
    • (1989) EMBO J. , vol.8 , pp. 393-399
    • Goedert, M.1    Spillantini, M.G.2    Potier, M.C.3    Ulrich, J.4    Crowther, R.A.5
  • 7
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler, A., Drechsel, D., Kirschner, M. W., and Martin, D. W., Jr. (1989) Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains Mol. Cell. Biol. 9, 1381-1388
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin Jr., D.W.4
  • 8
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • Goode, B. L. and Feinstein, S. C. (1994) Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau J. Cell Biol. 124, 769-782
    • (1994) J. Cell Biol. , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 10
    • 0347594304 scopus 로고    scopus 로고
    • Modeling tau polymerization in vitro: A review and synthesis
    • Gamblin, T. C., Berry, R. W., and Binder, L. I. (2003) Modeling tau polymerization in vitro: A review and synthesis Biochemistry 42, 15009-15017
    • (2003) Biochemistry , vol.42 , pp. 15009-15017
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 11
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming β structure
    • von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., and Mandelkow, E. (2000) Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming β structure Proc. Natl. Acad. Sci. U.S.A. 97, 5129-5134
    • (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.5
  • 12
    • 0034494233 scopus 로고    scopus 로고
    • Fibers of tau fragments, but not full length tau, exhibit a cross β-structure: Implications for the formation of paired helical filaments
    • Giannetti, A. M., Lindwall, G., Chau, M. F., Radeke, M. J., Feinstein, S. C., and Kohlstaedt, L. A. (2000) Fibers of tau fragments, but not full length tau, exhibit a cross β-structure: Implications for the formation of paired helical filaments Protein Sci. 9, 2427-2435
    • (2000) Protein Sci. , vol.9 , pp. 2427-2435
    • Giannetti, A.M.1    Lindwall, G.2    Chau, M.F.3    Radeke, M.J.4    Feinstein, S.C.5    Kohlstaedt, L.A.6
  • 13
    • 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
    • (2002) J. Biol. Chem. , vol.277 , pp. 41390-41400
    • Li, L.1    Von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 16
    • 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
    • (1999) Biochemistry , vol.38 , pp. 14851-14859
    • King, M.E.1    Ahuja, V.2    Binder, L.I.3    Kuret, J.4
  • 17
    • 46649101161 scopus 로고    scopus 로고
    • Nucleation-dependent tau filament formation: The importance of dimerization and an estimation of elementary rate constants
    • Congdon, E. E., Kim, S., Bonchak, J., Songrug, T., Matzavinos, A., and Kuret, J. (2008) Nucleation-dependent tau filament formation: The importance of dimerization and an estimation of elementary rate constants J. Biol. Chem. 283, 13806-13816
    • (2008) J. Biol. Chem. , vol.283 , pp. 13806-13816
    • Congdon, E.E.1    Kim, S.2    Bonchak, J.3    Songrug, T.4    Matzavinos, A.5    Kuret, J.6
  • 19
    • 10944223484 scopus 로고    scopus 로고
    • Tau protein as a differential biomarker of tauopathies
    • Sergeant, N., Delacourte, A., and Buee, L. (2005) Tau protein as a differential biomarker of tauopathies Biochim. Biophys. Acta 1739, 179-197
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 179-197
    • Sergeant, N.1    Delacourte, A.2    Buee, L.3
  • 22
    • 0345561533 scopus 로고    scopus 로고
    • Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations
    • Arrasate, M., Perez, M., Armas-Portela, R., and Avila, J. (1999) Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations FEBS Lett. 446, 199-202
    • (1999) FEBS Lett. , vol.446 , pp. 199-202
    • Arrasate, M.1    Perez, M.2    Armas-Portela, R.3    Avila, J.4
  • 23
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S., Zheng-Fischhofer, Q., Ackmann, M., Biernat, J., von Bergen, M., Mandelkow, E. M., and Mandelkow, E. (2000) Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias Biochemistry 39, 11714-11721
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1    Zheng-Fischhofer, Q.2    Ackmann, M.3    Biernat, J.4    Von Bergen, M.5    Mandelkow, E.M.6    Mandelkow, E.7
  • 25
    • 0034705192 scopus 로고    scopus 로고
    • In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants
    • Gamblin, T. C., King, M. E., Dawson, H., Vitek, M. P., Kuret, J., Berry, R. W., and Binder, L. I. (2000) In vitro polymerization of tau protein monitored by laser light scattering: Method and application to the study of FTDP-17 mutants Biochemistry 39, 6136-6144
    • (2000) Biochemistry , vol.39 , pp. 6136-6144
    • Gamblin, T.C.1    King, M.E.2    Dawson, H.3    Vitek, M.P.4    Kuret, J.5    Berry, R.W.6    Binder, L.I.7
  • 26
    • 0033011181 scopus 로고    scopus 로고
    • Accelerated filament formation from tau protein with specific FTDP-17 missense mutations
    • Nacharaju, P., Lewis, J., Easson, C., Yen, S., Hackett, J., Hutton, M., and Yen, S. H. (1999) Accelerated filament formation from tau protein with specific FTDP-17 missense mutations FEBS Lett. 447, 195-199
    • (1999) FEBS Lett. , vol.447 , pp. 195-199
    • Nacharaju, P.1    Lewis, J.2    Easson, C.3    Yen, S.4    Hackett, J.5    Hutton, M.6    Yen, S.H.7
  • 27
    • 0035254160 scopus 로고    scopus 로고
    • Mutated tau binds less avidly to microtubules than wildtype tau in living cells
    • Nagiec, E. W., Sampson, K. E., and Abraham, I. (2001) Mutated tau binds less avidly to microtubules than wildtype tau in living cells J. Neurosci. Res. 63, 268-275
    • (2001) J. Neurosci. Res. , vol.63 , pp. 268-275
    • Nagiec, E.W.1    Sampson, K.E.2    Abraham, I.3
  • 28
    • 0034193290 scopus 로고    scopus 로고
    • Missense point mutations of tau to segregate with FTDP-17 exhibit site-specific effects on microtubule structure in COS cells: A novel action of R406W mutation
    • Sahara, N., Tomiyama, T., and Mori, H. (2000) Missense point mutations of tau to segregate with FTDP-17 exhibit site-specific effects on microtubule structure in COS cells: A novel action of R406W mutation J. Neurosci. Res. 60, 380-387
    • (2000) J. Neurosci. Res. , vol.60 , pp. 380-387
    • Sahara, N.1    Tomiyama, T.2    Mori, H.3
  • 29
    • 0033638377 scopus 로고    scopus 로고
    • Distinct FTDP-17 missense mutations in tau produce tau aggregates and other pathological phenotypes in transfected CHO cells
    • Vogelsberg-Ragaglia, V., Bruce, J., Richter-Landsberg, C., Zhang, B., Hong, M., Trojanowski, J. Q., and Lee, V. M. (2000) Distinct FTDP-17 missense mutations in tau produce tau aggregates and other pathological phenotypes in transfected CHO cells Mol. Biol. Cell 11, 4093-4104
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4093-4104
    • Vogelsberg-Ragaglia, V.1    Bruce, J.2    Richter-Landsberg, C.3    Zhang, B.4    Hong, M.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 30
    • 0032885930 scopus 로고    scopus 로고
    • Fibrillogenesis of tau: Insights from tau missense mutations in FTDP-17
    • Yen, S. H., Hutton, M., DeTure, M., Ko, L. W., and Nacharaju, P. (1999) Fibrillogenesis of tau: Insights from tau missense mutations in FTDP-17 Brain Pathol. 9, 695-705
    • (1999) Brain Pathol. , vol.9 , pp. 695-705
    • Yen, S.H.1    Hutton, M.2    Deture, M.3    Ko, L.W.4    Nacharaju, P.5
  • 31
    • 4844219627 scopus 로고    scopus 로고
    • Promotion of hyperphosphorylation by frontotemporal dementia tau mutations
    • Alonso Adel, C., Mederlyova, A., Novak, M., Grundke-Iqbal, I., and Iqbal, K. (2004) Promotion of hyperphosphorylation by frontotemporal dementia tau mutations J. Biol. Chem. 279, 34873-34881
    • (2004) J. Biol. Chem. , vol.279 , pp. 34873-34881
    • Alonso Adel, C.1    Mederlyova, A.2    Novak, M.3    Grundke-Iqbal, I.4    Iqbal, K.5
  • 33
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman, J. M. and Feany, M. B. (2003) Genetic modifiers of tauopathy in Drosophila Genetics 165, 1233-1242
    • (2003) Genetics , vol.165 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 37
    • 49149100053 scopus 로고    scopus 로고
    • Assessing the toxicity of tau aggregation
    • Rankin, C. A. and Gamblin, T. C. (2008) Assessing the toxicity of tau aggregation J. Alzheimer's Dis. 14, 411-416
    • (2008) J. Alzheimer's Dis. , vol.14 , pp. 411-416
    • Rankin, C.A.1    Gamblin, T.C.2
  • 38
    • 0037465354 scopus 로고    scopus 로고
    • Tau polymerization: Role of the amino terminus
    • Gamblin, T. C., Berry, R. W., and Binder, L. I. (2003) Tau polymerization: Role of the amino terminus Biochemistry 42, 2252-2257
    • (2003) Biochemistry , vol.42 , pp. 2252-2257
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 39
    • 11144258263 scopus 로고    scopus 로고
    • Mutations causing neurodegenerative tauopathies
    • Goedert, M. and Jakes, R. (2005) Mutations causing neurodegenerative tauopathies Biochim. Biophys. Acta 1739, 240-250
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 240-250
    • Goedert, M.1    Jakes, R.2
  • 40
    • 0032561415 scopus 로고    scopus 로고
    • Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly
    • Hasegawa, M., Smith, M. J., and Goedert, M. (1998) Tau proteins with FTDP-17 mutations have a reduced ability to promote microtubule assembly FEBS Lett. 437, 207-210
    • (1998) FEBS Lett. , vol.437 , pp. 207-210
    • Hasegawa, M.1    Smith, M.J.2    Goedert, M.3
  • 41
    • 30944470033 scopus 로고    scopus 로고
    • Frontotemporal dementia and parkinsonism linked to chromosome 17
    • Wszolek, Z. K., Slowinski, J., Golan, M., and Dickson, D. W. (2005) Frontotemporal dementia and parkinsonism linked to chromosome 17 Folia Neuropathol. 43, 258-270
    • (2005) Folia Neuropathol. , vol.43 , pp. 258-270
    • Wszolek, Z.K.1    Slowinski, J.2    Golan, M.3    Dickson, D.W.4
  • 42
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 43
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • Chou, P. Y. and Fasman, G. D. (1974) Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins Biochemistry 13, 211-222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 44
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti, F., Stefani, M., Taddei, N., Ramponi, G., and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates Nature 424, 805-808
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 45
    • 22744459527 scopus 로고    scopus 로고
    • Pseudo-phosphorylation of tau at Ser202 and Thr205 affects tau filament formation
    • Rankin, C. A., Sun, Q., and Gamblin, T. C. (2005) Pseudo-phosphorylation of tau at Ser202 and Thr205 affects tau filament formation Brain Res. Mol. Brain Res. 138, 84-93
    • (2005) Brain Res. Mol. Brain Res. , vol.138 , pp. 84-93
    • Rankin, C.A.1    Sun, Q.2    Gamblin, T.C.3
  • 46
    • 39749112546 scopus 로고    scopus 로고
    • Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
    • Morris, A. M., Watzky, M. A., Agar, J. N., and Finke, R. G. (2008) Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth Biochemistry 47, 2413-2427
    • (2008) Biochemistry , vol.47 , pp. 2413-2427
    • Morris, A.M.1    Watzky, M.A.2    Agar, J.N.3    Finke, R.G.4
  • 47
    • 67649622427 scopus 로고    scopus 로고
    • Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization
    • Sun, Q. and Gamblin, T. C. (2009) Pseudohyperphosphorylation causing AD-like changes in tau has significant effects on its polymerization Biochemistry 48, 6002-6011
    • (2009) Biochemistry , vol.48 , pp. 6002-6011
    • Sun, Q.1    Gamblin, T.C.2
  • 48
    • 80155166000 scopus 로고    scopus 로고
    • Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms
    • Combs, B., Voss, K., and Gamblin, T. C. (2011) Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms Biochemistry 50, 9446-9456
    • (2011) Biochemistry , vol.50 , pp. 9446-9456
    • Combs, B.1    Voss, K.2    Gamblin, T.C.3
  • 50
    • 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
    • (1998) Biochemistry , vol.37 , pp. 10223-10230
    • Friedhoff, P.1    Schneider, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 51
    • 33845926113 scopus 로고    scopus 로고
    • Characterization of two VQIXXK motifs for tau fibrillization in vitro
    • Li, W. and Lee, V. M. (2006) Characterization of two VQIXXK motifs for tau fibrillization in vitro Biochemistry 45, 15692-15701
    • (2006) Biochemistry , vol.45 , pp. 15692-15701
    • Li, W.1    Lee, V.M.2
  • 52
    • 0035930625 scopus 로고    scopus 로고
    • Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local β-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 β-structure J. Biol. Chem. 276, 48165-48174
    • (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
  • 53
    • 57649129018 scopus 로고    scopus 로고
    • Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation
    • Jeganathan, S., Hascher, A., Chinnathambi, S., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (2008) Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation J. Biol. Chem. 283, 32066-32076
    • (2008) J. Biol. Chem. , vol.283 , pp. 32066-32076
    • Jeganathan, S.1    Hascher, A.2    Chinnathambi, S.3    Biernat, J.4    Mandelkow, E.M.5    Mandelkow, E.6
  • 56
    • 48249148310 scopus 로고    scopus 로고
    • Tau exon 10 alternative splicing and tauopathies
    • Liu, F. and Gong, C. X. (2008) Tau exon 10 alternative splicing and tauopathies Mol. Neurodegener. 3, 8
    • (2008) Mol. Neurodegener. , vol.3 , pp. 8
    • Liu, F.1    Gong, C.X.2
  • 57
    • 61349120799 scopus 로고    scopus 로고
    • FTDP-17 mutations in Tau alter the regulation of microtubule dynamics: An "alternative core" model for normal and pathological Tau action
    • LeBoeuf, A. C., Levy, S. F., Gaylord, M., Bhattacharya, A., Singh, A. K., Jordan, M. A., Wilson, L., and Feinstein, S. C. (2008) FTDP-17 mutations in Tau alter the regulation of microtubule dynamics: An "alternative core" model for normal and pathological Tau action J. Biol. Chem. 283, 36406-36415
    • (2008) J. Biol. Chem. , vol.283 , pp. 36406-36415
    • Leboeuf, A.C.1    Levy, S.F.2    Gaylord, M.3    Bhattacharya, A.4    Singh, A.K.5    Jordan, M.A.6    Wilson, L.7    Feinstein, S.C.8
  • 59
    • 0034718571 scopus 로고    scopus 로고
    • Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias
    • Barghorn, S., Zheng-Fischhofer, Q., Ackmann, M., Biernat, J., von Bergen, M., and Mandelkow, E. (2000) Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias Biochemistry 39, 11714-11721
    • (2000) Biochemistry , vol.39 , pp. 11714-11721
    • Barghorn, S.1    Zheng-Fischhofer, Q.2    Ackmann, M.3    Biernat, J.4    Von Bergen, M.5    Mandelkow, E.6
  • 60
    • 0037134098 scopus 로고    scopus 로고
    • Effects on splicing and protein function of three mutations in codon N296 of tau in vitro
    • Grover, A., DeTure, M., Yen, S. H., and Hutton, M. (2002) Effects on splicing and protein function of three mutations in codon N296 of tau in vitro Neurosci. Lett. 323, 33-36
    • (2002) Neurosci. Lett. , vol.323 , pp. 33-36
    • Grover, A.1    Deture, M.2    Yen, S.H.3    Hutton, M.4


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