메뉴 건너뛰기




Volumn 10, Issue , 2013, Pages

The absence of myelin basic protein promotes neuroinflammation and reduces amyloid β-protein accumulation in Tg-5xFAD mice

Author keywords

Alzheimer's disease; Amyloid protein; Astrocyte; Chaperone molecules; Matrix metalloproteinases; Microglia; Myelin basic protein; Transgenic mice

Indexed keywords

ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; GELATINASE B; MYELIN BASIC PROTEIN;

EID: 84887126975     PISSN: None     EISSN: 17422094     Source Type: Journal    
DOI: 10.1186/1742-2094-10-134     Document Type: Article
Times cited : (28)

References (79)
  • 4
    • 84857642949 scopus 로고    scopus 로고
    • The toxic aβ oligomer and Alzheimer's disease: an emperor in need of clothes
    • 10.1038/nn.3028, 22286176
    • Benilova I, Karran E, De Strooper B. The toxic aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci 2012, 15:349-357. 10.1038/nn.3028, 22286176.
    • (2012) Nat Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 5
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
    • 10.1038/nrm2101, 17245412
    • Haass C, Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 2007, 8:101-112. 10.1038/nrm2101, 17245412.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 6
    • 44549087765 scopus 로고    scopus 로고
    • Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
    • 10.1016/j.bbr.2008.02.016, 2601528, 18359102
    • Selkoe DJ. Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior. Behav Brain Res 2008, 192:106-113. 10.1016/j.bbr.2008.02.016, 2601528, 18359102.
    • (2008) Behav Brain Res , vol.192 , pp. 106-113
    • Selkoe, D.J.1
  • 7
    • 0037195163 scopus 로고    scopus 로고
    • Neurotoxic effects of thioflavin S-positive amyloid deposits in transgenic mice and Alzheimer's disease
    • 10.1073/pnas.222433299, 137824, 12374847
    • Urbanc B, Cruz L, Le R, Sanders J, Ashe KH, Duff K, Stanley HE, Irizarry MC, Hyman BT. Neurotoxic effects of thioflavin S-positive amyloid deposits in transgenic mice and Alzheimer's disease. Proc Natl Acad Sci USA 2002, 99:13990-13995. 10.1073/pnas.222433299, 137824, 12374847.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13990-13995
    • Urbanc, B.1    Cruz, L.2    Le, R.3    Sanders, J.4    Ashe, K.H.5    Duff, K.6    Stanley, H.E.7    Irizarry, M.C.8    Hyman, B.T.9
  • 8
    • 0037444553 scopus 로고    scopus 로고
    • In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy
    • McLellan ME, Kajdasz ST, Hyman BT, Bacskai BJ. In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy. J Neurosci 2003, 23:2212-2217.
    • (2003) J Neurosci , vol.23 , pp. 2212-2217
    • McLellan, M.E.1    Kajdasz, S.T.2    Hyman, B.T.3    Bacskai, B.J.4
  • 9
    • 0027407565 scopus 로고
    • Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
    • 10.1073/pnas.90.5.1977, 46003, 8446617
    • Strittmatter WJ, Saunders AM, Schmechel D, Pericak-Vance M, Enghild J, Salvesen GS, Roses AD. Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc Natl Acad Sci USA 1993, 90:1977-1981. 10.1073/pnas.90.5.1977, 46003, 8446617.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1977-1981
    • Strittmatter, W.J.1    Saunders, A.M.2    Schmechel, D.3    Pericak-Vance, M.4    Enghild, J.5    Salvesen, G.S.6    Roses, A.D.7
  • 11
    • 0034746840 scopus 로고    scopus 로고
    • Role of apoE/Aβ interactions in the pathogenesis of Alzheimer's disease and cerebral amyloid angiopathy
    • 10.1385/JMN:17:2:147, 11816788
    • Holtzman DM. Role of apoE/Aβ interactions in the pathogenesis of Alzheimer's disease and cerebral amyloid angiopathy. J Mol Neurosci 2001, 17:147-155. 10.1385/JMN:17:2:147, 11816788.
    • (2001) J Mol Neurosci , vol.17 , pp. 147-155
    • Holtzman, D.M.1
  • 12
    • 0028921915 scopus 로고
    • Characterization of apolipoprotein J-Alzheimer's Aβ interaction
    • 10.1074/jbc.270.13.7563, 7706304
    • Matsubara E, Frangione B, Ghiso J. Characterization of apolipoprotein J-Alzheimer's Aβ interaction. J Biol Chem 1995, 270:7563-7567. 10.1074/jbc.270.13.7563, 7706304.
    • (1995) J Biol Chem , vol.270 , pp. 7563-7567
    • Matsubara, E.1    Frangione, B.2    Ghiso, J.3
  • 14
    • 1242274389 scopus 로고    scopus 로고
    • Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed β-amyloid in neurons
    • 10.1523/JNEUROSCI.4330-03.2004, 14973234
    • Magrane J, Smith RC, Walsh K, Querfurth HW. Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed β-amyloid in neurons. J Neurosci 2004, 24:1700-1706. 10.1523/JNEUROSCI.4330-03.2004, 14973234.
    • (2004) J Neurosci , vol.24 , pp. 1700-1706
    • Magrane, J.1    Smith, R.C.2    Walsh, K.3    Querfurth, H.W.4
  • 15
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro
    • 10.1074/jbc.M606192200, 16973602
    • Evans CG, Wisen S, Gestwicki JE. Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro. J Biol Chem 2006, 281:33182-33191. 10.1074/jbc.M606192200, 16973602.
    • (2006) J Biol Chem , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisen, S.2    Gestwicki, J.E.3
  • 16
    • 16344382167 scopus 로고    scopus 로고
    • Assembly of hereditary amyloid β-protein variants in the presence of favorable gangliosides
    • 10.1016/j.febslet.2005.03.013, 15811339
    • Yamamoto N, Hirabayashi Y, Amari M, Yamaguchi H, Romanov G, Van Nostrand WE, Yanagisawa K. Assembly of hereditary amyloid β-protein variants in the presence of favorable gangliosides. FEBS Lett 2005, 579:2185-2190. 10.1016/j.febslet.2005.03.013, 15811339.
    • (2005) FEBS Lett , vol.579 , pp. 2185-2190
    • Yamamoto, N.1    Hirabayashi, Y.2    Amari, M.3    Yamaguchi, H.4    Romanov, G.5    Van Nostrand, W.E.6    Yanagisawa, K.7
  • 17
    • 0030329641 scopus 로고    scopus 로고
    • Interaction of transthyretin with amyloid β-protein: binding and inhibition of amyloid formation
    • discussion 160-144
    • Schwarzman AL, Goldgaber D. Interaction of transthyretin with amyloid β-protein: binding and inhibition of amyloid formation. Ciba Found Symp 1996, 199:146-160. discussion 160-144.
    • (1996) Ciba Found Symp , vol.199 , pp. 146-160
    • Schwarzman, A.L.1    Goldgaber, D.2
  • 18
  • 19
    • 0038376613 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans in Alzheimer's disease and amyloid-related disorders
    • 10.1016/S1474-4422(03)00484-8, 12878436
    • van Horssen J, Wesseling P, van den Heuvel LP, de Waal RM, Verbeek MM. Heparan sulphate proteoglycans in Alzheimer's disease and amyloid-related disorders. Lancet Neurol 2003, 2:482-492. 10.1016/S1474-4422(03)00484-8, 12878436.
    • (2003) Lancet Neurol , vol.2 , pp. 482-492
    • van Horssen, J.1    Wesseling, P.2    van den Heuvel, L.P.3    de Waal, R.M.4    Verbeek, M.M.5
  • 20
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease
    • 10.1038/nm1095-1062, 7489364
    • Yanagisawa K, Odaka A, Suzuki N, Ihara Y. GM1 ganglioside-bound amyloid β-protein (Aβ): a possible form of preamyloid in Alzheimer's disease. Nat Med 1995, 1:1062-1066. 10.1038/nm1095-1062, 7489364.
    • (1995) Nat Med , vol.1 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 21
    • 33847076858 scopus 로고    scopus 로고
    • Ganglioside G(M1)-mediated amyloid-beta fibrillogenesis and membrane disruption
    • 10.1021/bi062177x, 17256880
    • Chi EY, Frey SL, Lee KY. Ganglioside G(M1)-mediated amyloid-beta fibrillogenesis and membrane disruption. Biochemistry 2007, 46:1913-1924. 10.1021/bi062177x, 17256880.
    • (2007) Biochemistry , vol.46 , pp. 1913-1924
    • Chi, E.Y.1    Frey, S.L.2    Lee, K.Y.3
  • 22
    • 34248151111 scopus 로고    scopus 로고
    • Inhibition of familial cerebral amyloid angiopathy mutant amyloid β-protein fibril assembly by myelin basic protein
    • 10.1074/jbc.M603494200, 17259179
    • Hoos MD, Ahmed M, Smith SO, Van Nostrand WE. Inhibition of familial cerebral amyloid angiopathy mutant amyloid β-protein fibril assembly by myelin basic protein. J Biol Chem 2007, 282:9952-9961. 10.1074/jbc.M603494200, 17259179.
    • (2007) J Biol Chem , vol.282 , pp. 9952-9961
    • Hoos, M.D.1    Ahmed, M.2    Smith, S.O.3    Van Nostrand, W.E.4
  • 23
    • 33748487414 scopus 로고    scopus 로고
    • Myelin basic protein: a multifunctional protein
    • 10.1007/s00018-006-6094-7, 16794783
    • Boggs JM. Myelin basic protein: a multifunctional protein. Cell Mol Life Sci 2006, 63:1945-1961. 10.1007/s00018-006-6094-7, 16794783.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1945-1961
    • Boggs, J.M.1
  • 24
    • 0027418817 scopus 로고
    • Structure and developmental regulation of Golli-mbp, a 105-kilobase gene that encompasses the myelin basic protein gene and is expressed in cells in the oligodendrocyte lineage in the brain
    • Campagnoni AT, Pribyl TM, Campagnoni CW, Kampf K, Amur-Umarjee S, Landry CF, Handley VW, Newman SL, Garbay B, Kitamura K. Structure and developmental regulation of Golli-mbp, a 105-kilobase gene that encompasses the myelin basic protein gene and is expressed in cells in the oligodendrocyte lineage in the brain. J Biol Chem 1993, 268:4930-4938.
    • (1993) J Biol Chem , vol.268 , pp. 4930-4938
    • Campagnoni, A.T.1    Pribyl, T.M.2    Campagnoni, C.W.3    Kampf, K.4    Amur-Umarjee, S.5    Landry, C.F.6    Handley, V.W.7    Newman, S.L.8    Garbay, B.9    Kitamura, K.10
  • 25
    • 0010987830 scopus 로고
    • Identification of three forms of human myelin basic protein by cDNA cloning
    • 10.1073/pnas.83.13.4962, 323864, 2425357
    • Kamholz J, de Ferra F, Puckett C, Lazzarini R. Identification of three forms of human myelin basic protein by cDNA cloning. Proc Natl Acad Sci USA 1986, 83:4962-4966. 10.1073/pnas.83.13.4962, 323864, 2425357.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4962-4966
    • Kamholz, J.1    de Ferra, F.2    Puckett, C.3    Lazzarini, R.4
  • 26
    • 0023188062 scopus 로고
    • Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning
    • 10.1002/jnr.490170402, 2442403
    • Roth HJ, Kronquist KE, Kerlero De Rosbo N, Crandall BF, Campagnoni AT. Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning. J Neurosci Res 1987, 17:321-328. 10.1002/jnr.490170402, 2442403.
    • (1987) J Neurosci Res , vol.17 , pp. 321-328
    • Roth, H.J.1    Kronquist, K.E.2    Kerlero De Rosbo, N.3    Crandall, B.F.4    Campagnoni, A.T.5
  • 27
    • 3042553626 scopus 로고    scopus 로고
    • Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis
    • 10.1016/j.micron.2004.04.005, 15219899
    • Harauz G, Ishiyama N, Hill CM, Bates IR, Libich DS, Fares C. Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis. Micron 2004, 35:503-542. 10.1016/j.micron.2004.04.005, 15219899.
    • (2004) Micron , vol.35 , pp. 503-542
    • Harauz, G.1    Ishiyama, N.2    Hill, C.M.3    Bates, I.R.4    Libich, D.S.5    Fares, C.6
  • 28
    • 0022336444 scopus 로고
    • Alternative splicing accounts for the four forms of myelin basic protein
    • 10.1016/0092-8674(85)90245-4, 2416470
    • de Ferra F, Engh H, Hudson L, Kamholz J, Puckett C, Molineaux S, Lazzarini RA. Alternative splicing accounts for the four forms of myelin basic protein. Cell 1985, 43:721-727. 10.1016/0092-8674(85)90245-4, 2416470.
    • (1985) Cell , vol.43 , pp. 721-727
    • de Ferra, F.1    Engh, H.2    Hudson, L.3    Kamholz, J.4    Puckett, C.5    Molineaux, S.6    Lazzarini, R.A.7
  • 29
    • 66649118037 scopus 로고    scopus 로고
    • Myelin basic protein binds to and inhibits the fibrillar assembly of Aβ42 in vitro
    • 10.1021/bi900037s, 19385666
    • Hoos MD, Ahmed M, Smith SO, Van Nostrand WE. Myelin basic protein binds to and inhibits the fibrillar assembly of Aβ42 in vitro. Biochemistry 2009, 48:4720-4727. 10.1021/bi900037s, 19385666.
    • (2009) Biochemistry , vol.48 , pp. 4720-4727
    • Hoos, M.D.1    Ahmed, M.2    Smith, S.O.3    Van Nostrand, W.E.4
  • 30
    • 29844448115 scopus 로고    scopus 로고
    • Apolipoprotein E genotype and age-related myelin breakdown in healthy individuals: implications for cognitive decline and dementia
    • 10.1001/archpsyc.63.1.63, 16389198
    • Bartzokis G, Lu PH, Geschwind DH, Edwards N, Mintz J, Cummings JL. Apolipoprotein E genotype and age-related myelin breakdown in healthy individuals: implications for cognitive decline and dementia. Arch Gen Psychiatry 2006, 63:63-72. 10.1001/archpsyc.63.1.63, 16389198.
    • (2006) Arch Gen Psychiatry , vol.63 , pp. 63-72
    • Bartzokis, G.1    Lu, P.H.2    Geschwind, D.H.3    Edwards, N.4    Mintz, J.5    Cummings, J.L.6
  • 31
    • 33745924689 scopus 로고    scopus 로고
    • Extensive degradation of myelin basic protein isoforms by calpain following traumatic brain injury
    • 10.1111/j.1471-4159.2006.03882.x, 16893416
    • Liu MC, Akle V, Zheng W, Kitlen J, O'Steen B, Larner SF, Dave JR, Tortella FC, Hayes RL, Wang KK. Extensive degradation of myelin basic protein isoforms by calpain following traumatic brain injury. J Neurochem 2006, 98:700-712. 10.1111/j.1471-4159.2006.03882.x, 16893416.
    • (2006) J Neurochem , vol.98 , pp. 700-712
    • Liu, M.C.1    Akle, V.2    Zheng, W.3    Kitlen, J.4    O'Steen, B.5    Larner, S.F.6    Dave, J.R.7    Tortella, F.C.8    Hayes, R.L.9    Wang, K.K.10
  • 32
    • 36549071668 scopus 로고    scopus 로고
    • Apolipoprotein E affects both myelin breakdown and cognition: implications for age-related trajectories of decline into dementia
    • 10.1016/j.biopsych.2007.03.024, 17659264
    • Bartzokis G, Lu PH, Geschwind DH, Tingus K, Huang D, Mendez MF, Edwards N, Mintz J. Apolipoprotein E affects both myelin breakdown and cognition: implications for age-related trajectories of decline into dementia. Biol Psychiatry 2007, 62:1380-1387. 10.1016/j.biopsych.2007.03.024, 17659264.
    • (2007) Biol Psychiatry , vol.62 , pp. 1380-1387
    • Bartzokis, G.1    Lu, P.H.2    Geschwind, D.H.3    Tingus, K.4    Huang, D.5    Mendez, M.F.6    Edwards, N.7    Mintz, J.8
  • 33
    • 3042662696 scopus 로고    scopus 로고
    • Heterogeneous age-related breakdown of white matter structural integrity: implications for cortical 'disconnection' in aging and Alzheimer's disease
    • 10.1016/j.neurobiolaging.2003.09.005, 15212838
    • Bartzokis G, Sultzer D, Lu PH, Nuechterlein KH, Mintz J, Cummings JL. Heterogeneous age-related breakdown of white matter structural integrity: implications for cortical 'disconnection' in aging and Alzheimer's disease. Neurobiol Aging 2004, 25:843-851. 10.1016/j.neurobiolaging.2003.09.005, 15212838.
    • (2004) Neurobiol Aging , vol.25 , pp. 843-851
    • Bartzokis, G.1    Sultzer, D.2    Lu, P.H.3    Nuechterlein, K.H.4    Mintz, J.5    Cummings, J.L.6
  • 34
    • 0038467307 scopus 로고    scopus 로고
    • Marked loss of myelinated nerve fibers in the human brain with age
    • 10.1002/cne.10714, 12794739
    • Marner L, Nyengaard JR, Tang Y, Pakkenberg B. Marked loss of myelinated nerve fibers in the human brain with age. J Comp Neurol 2003, 462:144-152. 10.1002/cne.10714, 12794739.
    • (2003) J Comp Neurol , vol.462 , pp. 144-152
    • Marner, L.1    Nyengaard, J.R.2    Tang, Y.3    Pakkenberg, B.4
  • 37
    • 1842356008 scopus 로고
    • Recombination within the myelin basic protein gene created the dysmyelinating shiverer mouse mutation
    • 10.1073/pnas.83.19.7542, 386755, 2429310
    • Molineaux SM, Engh H, de Ferra F, Hudson L, Lazzarini RA. Recombination within the myelin basic protein gene created the dysmyelinating shiverer mouse mutation. Proc Natl Acad Sci USA 1986, 83:7542-7546. 10.1073/pnas.83.19.7542, 386755, 2429310.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7542-7546
    • Molineaux, S.M.1    Engh, H.2    de Ferra, F.3    Hudson, L.4    Lazzarini, R.A.5
  • 38
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal β-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation
    • 10.1523/JNEUROSCI.1202-06.2006, 17021169
    • Oakley H, Cole SL, Logan S, Maus E, Shao P, Craft J, Guillozet-Bongaarts A, Ohno M, Disterhoft J, Van Eldik L, Berry R, Vassar R. Intraneuronal β-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J Neurosci 2006, 26:10129-10140. 10.1523/JNEUROSCI.1202-06.2006, 17021169.
    • (2006) J Neurosci , vol.26 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3    Maus, E.4    Shao, P.5    Craft, J.6    Guillozet-Bongaarts, A.7    Ohno, M.8    Disterhoft, J.9    Van Eldik, L.10    Berry, R.11    Vassar, R.12
  • 39
    • 80055104131 scopus 로고    scopus 로고
    • A technique for serial collection of cerebrospinal fluid from the cisterna magna in mouse
    • 2762909, 19066529
    • Liu L, Duff K. A technique for serial collection of cerebrospinal fluid from the cisterna magna in mouse. J Vis Exp 2008, 21:960. 2762909, 19066529.
    • (2008) J Vis Exp , vol.21 , pp. 960
    • Liu, L.1    Duff, K.2
  • 40
    • 2442594971 scopus 로고    scopus 로고
    • Early-onset and robust cerebral microvascular accumulation of amyloid β-protein in transgenic mice expressing low levels of a vasculotropic Dutch/Iowa mutant form of amyloid β-protein precursor
    • 10.1074/jbc.M312946200, 14985348
    • Davis J, Xu F, Deane R, Romanov G, Previti ML, Zeigler K, Zlokovic BV, Van Nostrand WE. Early-onset and robust cerebral microvascular accumulation of amyloid β-protein in transgenic mice expressing low levels of a vasculotropic Dutch/Iowa mutant form of amyloid β-protein precursor. J Biol Chem 2004, 279:20296-20306. 10.1074/jbc.M312946200, 14985348.
    • (2004) J Biol Chem , vol.279 , pp. 20296-20306
    • Davis, J.1    Xu, F.2    Deane, R.3    Romanov, G.4    Previti, M.L.5    Zeigler, K.6    Zlokovic, B.V.7    Van Nostrand, W.E.8
  • 41
    • 0036319503 scopus 로고    scopus 로고
    • Plaque-associated disruption of CSF and plasma amyloid-β (Aβ) equilibrium in a mouse model of Alzheimer's disease
    • 10.1046/j.1471-4159.2002.00889.x, 12064470
    • DeMattos RB, Bales KR, Parsadanian M, O'Dell MA, Foss EM, Paul SM, Holtzman DM. Plaque-associated disruption of CSF and plasma amyloid-β (Aβ) equilibrium in a mouse model of Alzheimer's disease. J Neurochem 2002, 81:229-236. 10.1046/j.1471-4159.2002.00889.x, 12064470.
    • (2002) J Neurochem , vol.81 , pp. 229-236
    • DeMattos, R.B.1    Bales, K.R.2    Parsadanian, M.3    O'Dell, M.A.4    Foss, E.M.5    Paul, S.M.6    Holtzman, D.M.7
  • 42
    • 78149255950 scopus 로고    scopus 로고
    • N-terminal domain of myelin basic protein inhibits amyloid β-protein fibril assembly
    • 10.1074/jbc.M110.169599, 2975183, 20807757
    • Liao MC, Hoos MD, Aucoin D, Ahmed M, Davis J, Smith SO, Van Nostrand WE. N-terminal domain of myelin basic protein inhibits amyloid β-protein fibril assembly. J Biol Chem 2010, 285:35590-35598. 10.1074/jbc.M110.169599, 2975183, 20807757.
    • (2010) J Biol Chem , vol.285 , pp. 35590-35598
    • Liao, M.C.1    Hoos, M.D.2    Aucoin, D.3    Ahmed, M.4    Davis, J.5    Smith, S.O.6    Van Nostrand, W.E.7
  • 43
    • 4043167747 scopus 로고    scopus 로고
    • Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • 10.1016/j.neuron.2004.07.003, 15294141
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM. Aβ immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 2004, 43:321-332. 10.1016/j.neuron.2004.07.003, 15294141.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 45
    • 0035933279 scopus 로고    scopus 로고
    • Intraneuronal aβ accumulation precedes plaque formation in β-amyloid precursor protein and presenilin-1 double-transgenic mice
    • 10.1016/S0304-3940(01)01876-6, 11403971
    • Wirths O, Multhaup G, Czech C, Blanchard V, Moussaoui S, Tremp G, Pradier L, Beyreuther K, Bayer TA. Intraneuronal aβ accumulation precedes plaque formation in β-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci Lett 2001, 306:116-120. 10.1016/S0304-3940(01)01876-6, 11403971.
    • (2001) Neurosci Lett , vol.306 , pp. 116-120
    • Wirths, O.1    Multhaup, G.2    Czech, C.3    Blanchard, V.4    Moussaoui, S.5    Tremp, G.6    Pradier, L.7    Beyreuther, K.8    Bayer, T.A.9
  • 46
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • 10.1186/1750-1326-2-18, 2100048, 17897471
    • Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, Necula M, Margol L, Wu J, Breydo L, Thompson JL, Rasool S, Gurlo T, Butler P, Glabe CG. Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Mol Neurodegener 2007, 2:18. 10.1186/1750-1326-2-18, 2100048, 17897471.
    • (2007) Mol Neurodegener , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5    Necula, M.6    Margol, L.7    Wu, J.8    Breydo, L.9    Thompson, J.L.10    Rasool, S.11    Gurlo, T.12    Butler, P.13    Glabe, C.G.14
  • 48
    • 0038038284 scopus 로고    scopus 로고
    • Alzheimer's disease, normal-pressure hydrocephalus, and senescent changes in CSF circulatory physiology: a hypothesis
    • 10.1016/S1474-4422(03)00487-3, 12878439
    • Silverberg GD, Mayo M, Saul T, Rubenstein E, McGuire D. Alzheimer's disease, normal-pressure hydrocephalus, and senescent changes in CSF circulatory physiology: a hypothesis. Lancet Neurol 2003, 2:506-511. 10.1016/S1474-4422(03)00487-3, 12878439.
    • (2003) Lancet Neurol , vol.2 , pp. 506-511
    • Silverberg, G.D.1    Mayo, M.2    Saul, T.3    Rubenstein, E.4    McGuire, D.5
  • 49
    • 2542475986 scopus 로고    scopus 로고
    • Clearing amyloid through the blood-brain barrier
    • 10.1111/j.1471-4159.2004.02385.x, 15140180
    • Zlokovic BV. Clearing amyloid through the blood-brain barrier. J Neurochem 2004, 89:807-811. 10.1111/j.1471-4159.2004.02385.x, 15140180.
    • (2004) J Neurochem , vol.89 , pp. 807-811
    • Zlokovic, B.V.1
  • 50
    • 0018333258 scopus 로고
    • Absence of the major dense line in myelin of the mutant mouse 'shiverer'
    • 10.1016/0304-3940(79)91489-7, 460693
    • Privat A, Jacque C, Bourre JM, Dupouey P, Baumann N. Absence of the major dense line in myelin of the mutant mouse 'shiverer'. Neurosci Lett 1979, 12:107-112. 10.1016/0304-3940(79)91489-7, 460693.
    • (1979) Neurosci Lett , vol.12 , pp. 107-112
    • Privat, A.1    Jacque, C.2    Bourre, J.M.3    Dupouey, P.4    Baumann, N.5
  • 51
    • 0020466562 scopus 로고
    • Dysmyelination of shiverer mutant mice in vivo and in vitro
    • 10.1111/j.1471-4159.1982.tb12560.x, 6750046
    • Nagaike K, Mikoshiba K, Tsukada Y. Dysmyelination of shiverer mutant mice in vivo and in vitro. J Neurochem 1982, 39:1235-1241. 10.1111/j.1471-4159.1982.tb12560.x, 6750046.
    • (1982) J Neurochem , vol.39 , pp. 1235-1241
    • Nagaike, K.1    Mikoshiba, K.2    Tsukada, Y.3
  • 52
    • 0028834682 scopus 로고
    • Increased production of gelatinase B (matrix metalloproteinase-9) and interleukin-6 by activated rat microglia in culture
    • 10.1002/jnr.490420307, 8583501
    • Gottschall PE, Yu X, Bing B. Increased production of gelatinase B (matrix metalloproteinase-9) and interleukin-6 by activated rat microglia in culture. J Neurosci Res 1995, 42:335-342. 10.1002/jnr.490420307, 8583501.
    • (1995) J Neurosci Res , vol.42 , pp. 335-342
    • Gottschall, P.E.1    Yu, X.2    Bing, B.3
  • 55
    • 0037266280 scopus 로고    scopus 로고
    • Serum- and CSF-concentrations of brain specific proteins in hydrocephalus
    • 10.1007/s00701-002-1019-1, 12545260
    • Beems T, Simons KS, Van Geel WJ, De Reus HP, Vos PE, Verbeek MM. Serum- and CSF-concentrations of brain specific proteins in hydrocephalus. Acta Neurochir (Wien) 2003, 145:37-43. 10.1007/s00701-002-1019-1, 12545260.
    • (2003) Acta Neurochir (Wien) , vol.145 , pp. 37-43
    • Beems, T.1    Simons, K.S.2    Van Geel, W.J.3    De Reus, H.P.4    Vos, P.E.5    Verbeek, M.M.6
  • 56
    • 33747033693 scopus 로고    scopus 로고
    • CSF analysis differentiates multiple-system atrophy from idiopathic late-onset cerebellar ataxia
    • 10.1212/01.wnl.0000227891.25592.8c, 16894110
    • Abdo WF, van de Warrenburg BP, Munneke M, van Geel WJ, Bloem BR, Kremer HP, Verbeek MM. CSF analysis differentiates multiple-system atrophy from idiopathic late-onset cerebellar ataxia. Neurology 2006, 67:474-479. 10.1212/01.wnl.0000227891.25592.8c, 16894110.
    • (2006) Neurology , vol.67 , pp. 474-479
    • Abdo, W.F.1    van de Warrenburg, B.P.2    Munneke, M.3    van Geel, W.J.4    Bloem, B.R.5    Kremer, H.P.6    Verbeek, M.M.7
  • 58
    • 0031661556 scopus 로고    scopus 로고
    • Myelin basic protein in CSF as indicator of disease activity in multiple sclerosis
    • Lamers KJ, de Reus HP, Jongen PJ. Myelin basic protein in CSF as indicator of disease activity in multiple sclerosis. Mult Scler 1998, 4:124-126.
    • (1998) Mult Scler , vol.4 , pp. 124-126
    • Lamers, K.J.1    de Reus, H.P.2    Jongen, P.J.3
  • 59
    • 0029881927 scopus 로고    scopus 로고
    • Myelin basic protein gene expression in neurons: developmental and regional changes in protein targeting within neuronal nuclei, cell bodies, and processes
    • Landry CF, Ellison JA, Pribyl TM, Campagnoni C, Kampf K, Campagnoni AT. Myelin basic protein gene expression in neurons: developmental and regional changes in protein targeting within neuronal nuclei, cell bodies, and processes. J Neurosci 1996, 16:2452-2462.
    • (1996) J Neurosci , vol.16 , pp. 2452-2462
    • Landry, C.F.1    Ellison, J.A.2    Pribyl, T.M.3    Campagnoni, C.4    Kampf, K.5    Campagnoni, A.T.6
  • 60
    • 0032531096 scopus 로고    scopus 로고
    • Embryonic expression of the myelin basic protein gene: identification of a promoter region that targets transgene expression to pioneer neurons
    • Landry CF, Pribyl TM, Ellison JA, Givogri MI, Kampf K, Campagnoni CW, Campagnoni AT. Embryonic expression of the myelin basic protein gene: identification of a promoter region that targets transgene expression to pioneer neurons. J Neurosci 1998, 18:7315-7327.
    • (1998) J Neurosci , vol.18 , pp. 7315-7327
    • Landry, C.F.1    Pribyl, T.M.2    Ellison, J.A.3    Givogri, M.I.4    Kampf, K.5    Campagnoni, C.W.6    Campagnoni, A.T.7
  • 61
    • 25144503844 scopus 로고    scopus 로고
    • Interaction between microglia and oligodendrocyte cell progenitors involves Golli proteins
    • 10.1196/annals.1342.015, 16154930
    • Filipovic R, Zecevic N. Interaction between microglia and oligodendrocyte cell progenitors involves Golli proteins. Ann N Y Acad Sci 2005, 1048:166-174. 10.1196/annals.1342.015, 16154930.
    • (2005) Ann N Y Acad Sci , vol.1048 , pp. 166-174
    • Filipovic, R.1    Zecevic, N.2
  • 62
    • 69249091013 scopus 로고    scopus 로고
    • Structural polymorphism and multifunctionality of myelin basic protein
    • 10.1021/bi901005f, 19642704
    • Harauz G, Ladizhansky V, Boggs JM. Structural polymorphism and multifunctionality of myelin basic protein. Biochemistry 2009, 48:8094-8104. 10.1021/bi901005f, 19642704.
    • (2009) Biochemistry , vol.48 , pp. 8094-8104
    • Harauz, G.1    Ladizhansky, V.2    Boggs, J.M.3
  • 63
    • 0019828169 scopus 로고
    • Shiverer: an autosomal recessive mutant mouse with myelin deficiency
    • Chernoff GF. Shiverer: an autosomal recessive mutant mouse with myelin deficiency. J Hered 1981, 72:128.
    • (1981) J Hered , vol.72 , pp. 128
    • Chernoff, G.F.1
  • 64
  • 66
    • 41149149615 scopus 로고    scopus 로고
    • Aβ-degrading enzymes in Alzheimer's disease
    • 10.1111/j.1750-3639.2008.00132.x, 18363935
    • Miners JS, Baig S, Palmer J, Palmer LE, Kehoe PG, Love S. Aβ-degrading enzymes in Alzheimer's disease. Brain Pathol 2008, 18:240-252. 10.1111/j.1750-3639.2008.00132.x, 18363935.
    • (2008) Brain Pathol , vol.18 , pp. 240-252
    • Miners, J.S.1    Baig, S.2    Palmer, J.3    Palmer, L.E.4    Kehoe, P.G.5    Love, S.6
  • 67
    • 0019833114 scopus 로고
    • Chronological study of oligodendroglial alterations and myelination in quaking mice
    • 10.1111/j.1365-2990.1981.tb00083.x, 7231641
    • Nagara H, Suzuki K. Chronological study of oligodendroglial alterations and myelination in quaking mice. Neuropathol Appl Neurobiol 1981, 7:135-149. 10.1111/j.1365-2990.1981.tb00083.x, 7231641.
    • (1981) Neuropathol Appl Neurobiol , vol.7 , pp. 135-149
    • Nagara, H.1    Suzuki, K.2
  • 68
    • 0023940954 scopus 로고
    • Astroglial plasticity in hemizygous and heterozygous jimpy mice
    • 10.1016/0736-5748(88)90027-5, 3213569
    • Best TT, Skoff RP, Bartlett WP. Astroglial plasticity in hemizygous and heterozygous jimpy mice. Int J Dev Neurosci 1988, 6:39-57. 10.1016/0736-5748(88)90027-5, 3213569.
    • (1988) Int J Dev Neurosci , vol.6 , pp. 39-57
    • Best, T.T.1    Skoff, R.P.2    Bartlett, W.P.3
  • 69
    • 0034193266 scopus 로고    scopus 로고
    • GFAP-positive and myelin marker-positive glia in normal and pathologic environments
    • 10.1002/(SICI)1097-4547(20000501)60:3<412::AID-JNR16>3.0.CO;2-E, 10797544
    • Dyer CA, Kendler A, Jean-Guillaume D, Awatramani R, Lee A, Mason LM, Kamholz J. GFAP-positive and myelin marker-positive glia in normal and pathologic environments. J Neurosci Res 2000, 60:412-426. 10.1002/(SICI)1097-4547(20000501)60:3<412::AID-JNR16>3.0.CO;2-E, 10797544.
    • (2000) J Neurosci Res , vol.60 , pp. 412-426
    • Dyer, C.A.1    Kendler, A.2    Jean-Guillaume, D.3    Awatramani, R.4    Lee, A.5    Mason, L.M.6    Kamholz, J.7
  • 70
    • 0029867128 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the normal human central nervous system, microglial nodules, and multiple sclerosis lesions
    • 10.1097/00005072-199603000-00005, 8786388
    • Maeda A, Sobel RA. Matrix metalloproteinases in the normal human central nervous system, microglial nodules, and multiple sclerosis lesions. J Neuropathol Exp Neurol 1996, 55:300-309. 10.1097/00005072-199603000-00005, 8786388.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 300-309
    • Maeda, A.1    Sobel, R.A.2
  • 71
    • 3042694846 scopus 로고    scopus 로고
    • Interferon-beta inhibits the expression of metalloproteinases in rat glial cell cultures: implications for multiple sclerosis pathogenesis and treatment
    • 10.1191/1352458504ms1016oa, 15222694
    • Liuzzi GM, Latronico T, Fasano A, Carlone G, Riccio P. Interferon-beta inhibits the expression of metalloproteinases in rat glial cell cultures: implications for multiple sclerosis pathogenesis and treatment. Mult Scler 2004, 10:290-297. 10.1191/1352458504ms1016oa, 15222694.
    • (2004) Mult Scler , vol.10 , pp. 290-297
    • Liuzzi, G.M.1    Latronico, T.2    Fasano, A.3    Carlone, G.4    Riccio, P.5
  • 72
    • 33846591479 scopus 로고    scopus 로고
    • Microglial activation and matrix protease generation during focal cerebral ischemia
    • 10.1161/01.STR.0000254477.34231.cb, 17261708
    • del Zoppo GJ, Milner R, Mabuchi T, Hung S, Wang X, Berg GI, Koziol JA. Microglial activation and matrix protease generation during focal cerebral ischemia. Stroke 2007, 38:646-651. 10.1161/01.STR.0000254477.34231.cb, 17261708.
    • (2007) Stroke , vol.38 , pp. 646-651
    • del Zoppo, G.J.1    Milner, R.2    Mabuchi, T.3    Hung, S.4    Wang, X.5    Berg, G.I.6    Koziol, J.A.7
  • 75
    • 0029852887 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1-40)
    • Backstrom JR, Lim GP, Cullen MJ, Tokes ZA. Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1-40). J Neurosci 1996, 16:7910-7919.
    • (1996) J Neurosci , vol.16 , pp. 7910-7919
    • Backstrom, J.R.1    Lim, G.P.2    Cullen, M.J.3    Tokes, Z.A.4
  • 79
    • 84876275084 scopus 로고    scopus 로고
    • Fine mapping of the amyloid ss-protein binding site on myelin basic protein
    • 10.1021/bi4001936, 23510371
    • Kotarba AE, Aucoin DS, Hoos MD, Smith SO, Van Nostrand WE. Fine mapping of the amyloid ss-protein binding site on myelin basic protein. Biochemistry 2013, 52(15):2565-2573. 10.1021/bi4001936, 23510371.
    • (2013) Biochemistry , vol.52 , Issue.15 , pp. 2565-2573
    • Kotarba, A.E.1    Aucoin, D.S.2    Hoos, M.D.3    Smith, S.O.4    Van Nostrand, W.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.