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Volumn 123, Issue 12, 2013, Pages 5190-5202

Antibodies against low-Density lipoprotein receptor-Related protein 4 induce myasthenia gravis

Author keywords

[No Author keywords available]

Indexed keywords

AGRIN; CHOLINERGIC RECEPTOR; IMMUNOGLOBULIN G; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN 4; MUSK PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 84890113189     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI66039     Document Type: Article
Times cited : (175)

References (80)
  • 1
    • 0036779688 scopus 로고    scopus 로고
    • Unravelling the pathogenesis of myasthenia gravis
    • Vincent A. Unravelling the pathogenesis of myasthenia gravis. Nat Rev Immunol. 2002;2(10):797-804.
    • (2002) Nat Rev Immunol , vol.2 , Issue.10 , pp. 797-804
    • Vincent, A.1
  • 2
    • 77953633370 scopus 로고    scopus 로고
    • A systematic review of population based epidemiological studies in myasthenia gravis
    • Carr AS, Cardwell CR, McCarron PO, McConville J. A systematic review of population based epidemiological studies in Myasthenia Gravis. BMC Neurol. 2010;10:46.
    • (2010) BMC Neurol , vol.10 , pp. 46
    • Carr, A.S.1    Cardwell, C.R.2    McCarron, P.O.3    McConville, J.4
  • 3
    • 0141839026 scopus 로고    scopus 로고
    • The epidemiology of myasthenia gravis
    • Phillips LH 2nd. The epidemiology of myasthenia gravis. Ann N Y Acad Sci. 2003;998:407-412.
    • (2003) Ann N Y Acad Sci , vol.998 , pp. 407-412
    • Phillips II, L.H.1
  • 4
    • 0022373590 scopus 로고
    • Acetylcholine receptor antibody as a diagnostic test for myasthenia gravis: Results in 153 validated cases and 2967 diagnostic assays
    • Vincent A, Newsom-Davis J. Acetylcholine receptor antibody as a diagnostic test for myasthenia gravis: results in 153 validated cases and 2967 diagnostic assays. J Neurol Neurosurg Psychiatry. 1985; 48(12):1246-1252.
    • (1985) J Neurol Neurosurg Psychiatry , vol.48 , Issue.12 , pp. 1246-1252
    • Vincent, A.1    Newsom-Davis, J.2
  • 5
    • 0017171683 scopus 로고
    • Antibody to acetylcholine receptor in myasthenia gravis. Prevalence, clinical correlates, and diagnostic value
    • Lindstrom JM, Seybold ME, Lennon VA, Whittingham S, Duane DD. Antibody to acetylcholine receptor in myasthenia gravis. Prevalence, clinical correlates, and diagnostic value. Neurology. 1976; 26(11):1054-1059.
    • (1976) Neurology , vol.26 , Issue.11 , pp. 1054-1059
    • Lindstrom, J.M.1    Seybold, M.E.2    Lennon, V.A.3    Whittingham, S.4    Duane, D.D.5
  • 6
    • 0015935638 scopus 로고
    • Autoimmune response to acetylcholine receptor
    • Patrick J, Lindstrom J. Autoimmune response to acetylcholine receptor. Science. 1973; 180(4088):871-872.
    • (1973) Science , vol.180 , Issue.4088 , pp. 871-872
    • Patrick, J.1    Lindstrom, J.2
  • 7
    • 0017582747 scopus 로고
    • Myasthenic immunoglobulin accelerates acetylcholine receptor degradation
    • Kao I, Drachman DB. Myasthenic immunoglobulin accelerates acetylcholine receptor degradation. Science. 1977;196(4289):527-529.
    • (1977) Science , vol.196 , Issue.4289 , pp. 527-529
    • Kao, I.1    Drachman, D.B.2
  • 8
    • 0017224904 scopus 로고
    • Reduced muscle acetylcholine sensitivity in rats immunised with acetylcholine receptor
    • Bevan S, Heinemann S, Lennon VA, Lindstrom J. Reduced muscle acetylcholine sensitivity in rats immunised with acetylcholine receptor. Nature. 1976; 260(5550):438-439.
    • (1976) Nature , vol.260 , Issue.5550 , pp. 438-439
    • Bevan, S.1    Heinemann, S.2    Lennon, V.A.3    Lindstrom, J.4
  • 9
    • 0016914842 scopus 로고
    • End-Plate potentials in experimental autoimmune myasthenia gravis in rats
    • Lambert EH, Lindstrom JM, Lennon VA. End-plate potentials in experimental autoimmune myasthenia gravis in rats. Ann N Y Acad Sci. 1976;274:300-318.
    • (1976) Ann N Y Acad Sci , vol.274 , pp. 300-318
    • Lambert, E.H.1    Lindstrom, J.M.2    Lennon, V.A.3
  • 10
    • 0017332896 scopus 로고
    • Myasthenia gravis. Study of humoral immune mechanisms by passive transfer to mice
    • Toyka KV, et al. Myasthenia gravis. Study of humoral immune mechanisms by passive transfer to mice. N Engl J Med. 1977;296(3):125-131.
    • (1977) N Engl J Med , vol.296 , Issue.3 , pp. 125-131
    • Toyka, K.V.1
  • 11
    • 0016756372 scopus 로고
    • Neuromuscular transmission after immunization against acetylcholine receptors
    • Green DP, Miledi R, Vincent A. Neuromuscular transmission after immunization against acetylcholine receptors. Proc R Soc Lond B Biol Sci. 1975; 189(1094):57-68.
    • (1975) Proc R Soc Lond B Biol Sci. , vol.189 , Issue.1094 , pp. 57-68
    • Green, D.P.1    Miledi, R.2    Vincent, A.3
  • 12
    • 0016910996 scopus 로고
    • The motor end plate in myasthenia gravis and in experimental autoimmune myasthenia gravis. A quantitative ultrastructural study
    • Engel AG, Tsujihata M, Lindstrom JM, Lennon VA. The motor end plate in myasthenia gravis and in experimental autoimmune myasthenia gravis. A quantitative ultrastructural study. Ann N Y Acad Sci. 1976;274:60-79.
    • (1976) Ann N Y Acad Sci , vol.274 , pp. 60-79
    • Engel, A.G.1    Tsujihata, M.2    Lindstrom, J.M.3    Lennon, V.A.4
  • 13
    • 0016796265 scopus 로고
    • Experimental autoimmune myasthenia: A model of myasthenia gravis in rats and guinea pigs
    • Lennon VA, Lindstrom JM, Seybold ME. Experimental autoimmune myasthenia: A model of myasthenia gravis in rats and guinea pigs. J Exp Med. 1975;141(6):1365-1375.
    • (1975) J Exp Med , vol.141 , Issue.6 , pp. 1365-1375
    • Lennon, V.A.1    Lindstrom, J.M.2    Seybold, M.E.3
  • 14
    • 0019195070 scopus 로고
    • Myasthenia gravis induced by monoclonal antibodies to acetylcholine receptors
    • Lennon VA, Lambert EH. Myasthenia gravis induced by monoclonal antibodies to acetylcholine receptors. Nature. 1980;285(5762):238-240.
    • (1980) Nature , vol.285 , Issue.5762 , pp. 238-240
    • Lennon, V.A.1    Lambert, E.H.2
  • 15
    • 0019201756 scopus 로고
    • Monoclonal anti-Acetylcholine receptor antibodies can cause experimental myasthenia
    • Richman DP, Gomez CM, Berman PW, Burres SA, Fitch FW, Arnason BG. Monoclonal anti-acetylcholine receptor antibodies can cause experimental myasthenia. Nature. 1980;286(5774):738-739.
    • (1980) Nature , vol.286 , Issue.5774 , pp. 738-739
    • Richman, D.P.1    Gomez, C.M.2    Berman, P.W.3    Burres, S.A.4    Fitch, F.W.5    Arnason, B.G.6
  • 16
    • 0016683636 scopus 로고
    • Immunological relationship between acetylcholine receptor and thymus: A possible significance in myasthenia gravis
    • Aharonov A, Tarrab-Hazdai R, Abramsky O, Fuchs S. Immunological relationship between acetylcholine receptor and thymus: a possible significance in myasthenia gravis. Proc Natl Acad Sci U S A. 1975;72(4):1456-1459.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , Issue.4 , pp. 1456-1459
    • Aharonov, A.1    Tarrab-Hazdai, R.2    Abramsky, O.3    Fuchs, S.4
  • 17
    • 0023625137 scopus 로고
    • The membrane attack complex of complement at the endplate in myasthenia gravis
    • Engel AG, Arahata K. The membrane attack complex of complement at the endplate in myasthenia gravis. Ann N Y Acad Sci. 1987;505:326-332.
    • (1987) Ann N Y Acad Sci , vol.505 , pp. 326-332
    • Engel, A.G.1    Arahata, K.2
  • 18
    • 0017755136 scopus 로고
    • Immune complexes (IgG and C3) at the motor end-Plate in myasthenia gravis: Ultrastructural and light microscopic localization and electrophysiologic correlations
    • Engel AG, Lambert EH, Howard FM. Immune complexes (IgG and C3) at the motor end-plate in myasthenia gravis: ultrastructural and light microscopic localization and electrophysiologic correlations. Mayo Clin Proc. 1977;52(5):267-280.
    • (1977) Mayo Clin Proc , vol.52 , Issue.5 , pp. 267-280
    • Engel, A.G.1    Lambert, E.H.2    Howard, F.M.3
  • 20
    • 55049092996 scopus 로고    scopus 로고
    • Lrp4 is a receptor for Agrin and forms a complex with MuSK
    • Kim N, et al. Lrp4 is a receptor for Agrin and forms a complex with MuSK. Cell. 2008;135(2):334-342.
    • (2008) Cell , vol.135 , Issue.2 , pp. 334-342
    • Kim, N.1
  • 22
    • 77950462859 scopus 로고    scopus 로고
    • To build a synapse: Signaling pathways in neuromuscular junction assembly
    • Wu H, Xiong WC, Mei L. To build a synapse: signaling pathways in neuromuscular junction assembly. Development. 2010;137(7):1017-1033.
    • (2010) Development , vol.137 , Issue.7 , pp. 1017-1033
    • Wu, H.1    Xiong, W.C.2    Mei, L.3
  • 23
    • 23344453327 scopus 로고    scopus 로고
    • Agrin promotes synaptic differentiation by counteracting an inhibitory effect of neurotransmitter
    • Misgeld T, Kummer TT, Lichtman JW, Sanes Jr. Agrin promotes synaptic differentiation by counteracting an inhibitory effect of neurotransmitter. Proc Natl Acad Sci U S A. 2005;102(31):11088-11093.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.31 , pp. 11088-11093
    • Misgeld, T.1    Kummer, T.T.2    Lichtman, J.W.3    Sanes, J.R.4
  • 24
    • 33846155569 scopus 로고    scopus 로고
    • LDL-Receptor-related protein 4 is crucial for formation of the neuromuscular junction
    • Weatherbee SD, Anderson KV, Niswander LA. LDL-receptor-related protein 4 is crucial for formation of the neuromuscular junction. Development. 2006;133(24):4993-5000.
    • (2006) Development , vol.133 , Issue.24 , pp. 4993-5000
    • Weatherbee, S.D.1    Anderson, K.V.2    Niswander, L.A.3
  • 25
    • 84863011431 scopus 로고    scopus 로고
    • Structural basis of agrin-Lrp4-Musk signaling
    • Zong Y, et al. Structural basis of agrin-LRP4-MuSK signaling. Genes Dev. 2012;26(3):247-258.
    • (2012) Genes Dev , vol.26 , Issue.3 , pp. 247-258
    • Zong, Y.1
  • 26
    • 15844417385 scopus 로고    scopus 로고
    • The receptor tyrosine kinase musk is required for neuromuscular junction formation in vivo
    • DeChiara TM, et al. The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo. Cell. 1996;85(4):501-512.
    • (1996) Cell , vol.85 , Issue.4 , pp. 501-512
    • DeChiara, T.M.1
  • 27
    • 15844380040 scopus 로고    scopus 로고
    • Agrin acts via a musk receptor complex
    • Glass DJ, et al. Agrin acts via a MuSK receptor complex. Cell. 1996;85(4):513-523.
    • (1996) Cell , vol.85 , Issue.4 , pp. 513-523
    • Glass, D.J.1
  • 28
    • 0035105784 scopus 로고    scopus 로고
    • Auto-Antibodies to the receptor tyrosine kinase musk in patients with myasthenia gravis without acetylcholine receptor antibodies
    • Hoch W, McConville J, Helms S, Newsom-Davis J, Melms A, Vincent A. Auto-antibodies to the receptor tyrosine kinase MuSK in patients with myasthenia gravis without acetylcholine receptor antibodies. Nat Med. 2001;7(3):365-368.
    • (2001) Nat Med , vol.7 , Issue.3 , pp. 365-368
    • Hoch, W.1    McConville, J.2    Helms, S.3    Newsom-Davis, J.4    Melms, A.5    Vincent, A.6
  • 30
    • 1642348179 scopus 로고    scopus 로고
    • Detection and characterization of musk antibodies in seronegative myasthenia gravis
    • McConville J, et al. Detection and characterization of MuSK antibodies in seronegative myasthenia gravis. Ann Neurol. 2004;55(4):580-584.
    • (2004) Ann Neurol , vol.55 , Issue.4 , pp. 580-584
    • McConville, J.1
  • 31
    • 33645521800 scopus 로고    scopus 로고
    • Induction of myasthenia by immunization against muscle-Specific kinase
    • Shigemoto K, et al. Induction of myasthenia by immunization against muscle-specific kinase. J Clin Invest. 2006;116(4):1016-1024.
    • (2006) J Clin Invest , vol.116 , Issue.4 , pp. 1016-1024
    • Shigemoto, K.1
  • 32
    • 45249083240 scopus 로고    scopus 로고
    • Myasthenia gravis experimentally induced with muscle-Specific kinase
    • Shigemoto K, et al. Myasthenia gravis experimentally induced with muscle-specific kinase. Ann N Y Acad Sci. 2008;1132:93-98.
    • (2008) Ann N Y Acad Sci , vol.1132 , pp. 93-98
    • Shigemoto, K.1
  • 33
    • 33646780233 scopus 로고    scopus 로고
    • Myasthenia gravis induced in mice by immunization with the recombinant extracellular domain of rat muscle-Specific kinase (musk)
    • Jha S, et al. Myasthenia gravis induced in mice by immunization with the recombinant extracellular domain of rat muscle-specific kinase (MuSK). J Neuroimmunol. 2006;175(1-2):107-117.
    • (2006) J Neuroimmunol , vol.175 , Issue.1-2 , pp. 107-117
    • Jha, S.1
  • 34
    • 33750969338 scopus 로고    scopus 로고
    • Delayed synapsing muscles are more severely affected in an experimental model of musk-Induced myasthenia gravis
    • Xu K, Jha S, Hoch W, Dryer SE. Delayed synapsing muscles are more severely affected in an experimental model of MuSK-induced myasthenia gravis. Neuroscience. 2006;143(3):655-659.
    • (2006) Neuroscience , vol.143 , Issue.3 , pp. 655-659
    • Xu, K.1    Jha, S.2    Hoch, W.3    Dryer, S.E.4
  • 35
    • 79958743273 scopus 로고    scopus 로고
    • Muscle-Selective synaptic disassembly and reorganization in musk antibody positive mg mice
    • Punga AR, Lin S, Oliveri F, Meinen S, Rügg MA. Muscle-selective synaptic disassembly and reorganization in MuSK antibody positive MG mice. Exp Neurol. 2011;230(2):207-217.
    • (2011) Exp Neurol , vol.230 , Issue.2 , pp. 207-217
    • Punga, A.R.1    Lin, S.2    Oliveri, F.3    Meinen, S.4    Rüegg, M.A.5
  • 36
    • 84856022505 scopus 로고    scopus 로고
    • Antibodies against muscle-Specific kinase impair both presynaptic and postsynaptic functions in a murine model of myasthenia gravis
    • Mori S, et al. Antibodies against muscle-specific kinase impair both presynaptic and postsynaptic functions in a murine model of myasthenia gravis. Am J Pathol. 2012;180(2):798-810.
    • (2012) Am J Pathol , vol.180 , Issue.2 , pp. 798-810
    • Mori, S.1
  • 37
    • 46749148845 scopus 로고    scopus 로고
    • Anti-MuSK patient antibodies disrupt the mouse neuromuscular junction
    • Cole RN, Reddel SW, Gervásio OL, Phillips WD. Anti-MuSK patient antibodies disrupt the mouse neuromuscular junction. Ann Neurol. 2008; 63(6):782-789.
    • (2008) Ann Neurol. , vol.63 , Issue.6 , pp. 782-789
    • Cole, R.N.1    Reddel, S.W.2    Gervásio, O.L.3    Phillips, W.D.4
  • 38
    • 77956275172 scopus 로고    scopus 로고
    • Patient autoantibodies deplete postsynaptic muscle-Specific kinase leading to disassembly of the ach receptor scaffold and myasthenia gravis in mice
    • Cole RN, Ghazanfari N, Ngo ST, Gervásio OL, Reddel SW, Phillips WD. Patient autoantibodies deplete postsynaptic muscle-specific kinase leading to disassembly of the ACh receptor scaffold and myasthenia gravis in mice. J Physiol. 2010; 588(pt 17):3217-3229.
    • J Physiol. , vol.2010 , Issue.588 PART 17 , pp. 3217-3229
    • Cole, R.N.1    Ghazanfari, N.2    Ngo, S.T.3    Gervásio, O.L.4    Reddel, S.W.5    Phillips, W.D.6
  • 39
    • 73549091486 scopus 로고    scopus 로고
    • The effect of plasma from muscle-Specific tyrosine kinase myasthenia patientson regenerating endplates
    • ter Beek WP, et al. The effect of plasma from muscle- specific tyrosine kinase myasthenia patientson regenerating endplates. Am J Pathol. 2009; 175(4):1536-1544.
    • (2009) Am J Pathol , vol.175 , Issue.4 , pp. 1536-1544
    • Ter Beek, W.P.1
  • 40
    • 84860155499 scopus 로고    scopus 로고
    • Muscle-Specific kinase myasthenia gravis igg4 autoantibodies cause severe neuromuscular junction dysfunction in mice
    • Klooster R, et al. Muscle-specific kinase myasthenia gravis IgG4 autoantibodies cause severe neuromuscular junction dysfunction in mice. Brain. 2012; 135(pt 4):1081-1101.
    • (2012) Brain , vol.135 , Issue.PART 4 , pp. 1081-1101
    • Klooster, R.1
  • 41
    • 84859978028 scopus 로고    scopus 로고
    • Acute severe animal model of antimuscle-Specific kinase myasthenia: Combined postsynaptic and presynaptic changes
    • Richman DP, et al. Acute severe animal model of antimuscle- specific kinase myasthenia: combined postsynaptic and presynaptic changes. Arch Neurol. 2012; 69(4):453-460.
    • (2012) Arch Neurol , vol.69 , Issue.4 , pp. 453-460
    • Richman, D.P.1
  • 42
    • 35248837870 scopus 로고    scopus 로고
    • A role for lrp4 in neuronal cell viability is related to apoe-Binding
    • Lu Y, Tian QB, Endo S, Suzuki T. A role for LRP4 in neuronal cell viability is related to apoE-binding. Brain Res. 2007;1177:19-28.
    • (2007) Brain Res , vol.1177 , pp. 19-28
    • Lu, Y.1    Tian, Q.B.2    Endo, S.3    Suzuki, T.4
  • 43
    • 27944471018 scopus 로고    scopus 로고
    • Abnormal development of the apical ectodermal ridge and polysyndactyly in megf7-Deficient mice
    • Johnson EB, Hammer RE, Herz J. Abnormal development of the apical ectodermal ridge and polysyndactyly in Megf7-deficient mice. Hum Mol Genet. 2005; 14(22):3523-3538.
    • (2005) Hum Mol Genet , vol.14 , Issue.22 , pp. 3523-3538
    • Johnson, E.B.1    Hammer, R.E.2    Herz, J.3
  • 44
    • 33646770321 scopus 로고    scopus 로고
    • Expression of low density lipoprotein receptor-Related protein 4 (Lrp4) gene in the mouse germ cells
    • Yamaguchi YL, Tanaka SS, Kasa M, Yasuda K, Tam PP, Matsui Y. Expression of low density lipoprotein receptor-related protein 4 (Lrp4) gene in the mouse germ cells. Gene Expr Patterns. 2006;6(6):607-612.
    • (2006) Gene Expr Patterns , vol.6 , Issue.6 , pp. 607-612
    • Yamaguchi, Y.L.1    Tanaka, S.S.2    Kasa, M.3    Yasuda, K.4    Tam, P.P.5    Matsui, Y.6
  • 45
    • 33745071526 scopus 로고    scopus 로고
    • Interaction of ldl receptor-Related protein 4 (lrp4) with postsynaptic scaffold proteins via its c-Terminal pdz domain-Binding motif, and its regulation by ca/calmodulin-Dependent protein kinase II
    • Tian QB, et al. Interaction of LDL receptor-related protein 4 (LRP4) with postsynaptic scaffold proteins via its C-terminal PDZ domain-binding motif, and its regulation by Ca/calmodulin-dependent protein kinase II. Eur J Neurosci. 2006;23(11):2864-2876.
    • (2006) Eur J Neurosci , vol.23 , Issue.11 , pp. 2864-2876
    • Tian, Q.B.1
  • 46
    • 84863011431 scopus 로고    scopus 로고
    • Structural basis of agrin-lrp4-Musk signaling
    • Zong Y, et al. Structural basis of agrin-LRP4-MuSK signaling. Genes Dev. 2012;26(3):247-258.
    • (2012) Genes Dev , vol.26 , Issue.3 , pp. 247-258
    • Zong, Y.1
  • 47
    • 84861855230 scopus 로고    scopus 로고
    • Anti-Lrp4 autoantibodies in achr-And musk-Antibody-Negative myasthenia gravis
    • Pevzner A, et al. Anti-LRP4 autoantibodies in AChR- and MuSK-antibody-negative myasthenia gravis. J Neurol. 2012;259(3):427-435.
    • (2012) J Neurol , vol.259 , Issue.3 , pp. 427-435
    • Pevzner, A.1
  • 48
    • 84859939384 scopus 로고    scopus 로고
    • Autoantibodies to lipoproteinrelated protein 4 in patients with double-Seronegative myasthenia gravis
    • Zhang B, et al. Autoantibodies to lipoproteinrelated protein 4 in patients with double-seronegative myasthenia gravis. Arch Neurol. 2012; 69(4):445-451.
    • (2012) Arch Neurol , vol.69 , Issue.4 , pp. 445-451
    • Zhang, B.1
  • 49
    • 79952513213 scopus 로고    scopus 로고
    • Autoantibodies to low-Density lipoprotein receptorrelated protein 4 in myasthenia gravis
    • Higuchi O, Hamuro J, Motomura M, Yamanashi Y. Autoantibodies to low-density lipoprotein receptorrelated protein 4 in myasthenia gravis. Ann Neurol. 2011;69(2):418-422.
    • (2011) Ann Neurol , vol.69 , Issue.2 , pp. 418-422
    • Higuchi, O.1    Hamuro, J.2    Motomura, M.3    Yamanashi, Y.4
  • 50
    • 0030001471 scopus 로고    scopus 로고
    • Expression of neurofilaments and of a titin epitope in thymic epithelial tumors. Implications for the pathogenesis of myasthenia gravis
    • Marx A, et al. Expression of neurofilaments and of a titin epitope in thymic epithelial tumors. Implications for the pathogenesis of myasthenia gravis. Am J Pathol. 1996;148(6):1839-1850.
    • (1996) Am J Pathol , vol.148 , Issue.6 , pp. 1839-1850
    • Marx, A.1
  • 51
    • 0031903545 scopus 로고    scopus 로고
    • Anti-Titin and antiryanodine receptor antibodies in myasthenia gravis patients with thymoma
    • Baggi F, et al. Anti-titin and antiryanodine receptor antibodies in myasthenia gravis patients with thymoma. Ann N Y Acad Sci. 1998;841:538-541.
    • (1998) Ann N Y Acad Sci , vol.841 , pp. 538-541
    • Baggi, F.1
  • 52
    • 0034970401 scopus 로고    scopus 로고
    • Anti-Titin antibodies in myasthenia gravis: Tight association with thymoma and heterogeneity of nonthymoma patients
    • Yamamoto AM, et al. Anti-titin antibodies in myasthenia gravis: tight association with thymoma and heterogeneity of nonthymoma patients. Arch Neurol. 2001; 58(6):885-890.
    • (2001) Arch Neurol , vol.58 , Issue.6 , pp. 885-890
    • Yamamoto, A.M.1
  • 53
    • 0035856431 scopus 로고    scopus 로고
    • Linkage of hla to myasthenia gravis and genetic heterogeneity depending on antititin antibodies
    • Giraud M, et al. Linkage of HLA to myasthenia gravis and genetic heterogeneity depending on antititin antibodies. Neurology. 2001;57(9):1555- 1560.
    • (2001) Neurology , vol.57 , Issue.9 , pp. 1555-1560
    • Giraud, M.1
  • 54
    • 0034717830 scopus 로고    scopus 로고
    • Suppression of experimental myasthenia gravis by monoclonal antibodies against mhc peptide region involved in presentation of a pathogenic t-Cell epitope
    • Nakayashiki N, Oshima M, Deitiker PR, Ashizawa T, Atassi MZ. Suppression of experimental myasthenia gravis by monoclonal antibodies against MHC peptide region involved in presentation of a pathogenic T-cell epitope. J Neuroimmunol. 2000; 105(2):131-144.
    • (2000) J Neuroimmunol , vol.105 , Issue.2 , pp. 131-144
    • Nakayashiki, N.1    Oshima, M.2    Deitiker, P.R.3    Ashizawa, T.4    Atassi, M.Z.5
  • 55
    • 0019519330 scopus 로고
    • No direct correlation between serum antiacetylcholine receptor antibody levels and clinical state of individual patients with myasthenia gravis
    • Roses AD, Olanow CW, McAdams MW, Lane RJ. No direct correlation between serum antiacetylcholine receptor antibody levels and clinical state of individual patients with myasthenia gravis. Neurology. 1981;31(2):220-224.
    • (1981) Neurology , vol.31 , Issue.2 , pp. 220-224
    • Roses, A.D.1    Olanow, C.W.2    McAdams, M.W.3    Lane, R.J.4
  • 56
    • 0020682914 scopus 로고
    • The relation of clinical disease to antibody titre, proliferative response and neurophysiology in murine experimental autoimmune myasthenia gravis
    • Pachner AR, Kantor FS. The relation of clinical disease to antibody titre, proliferative response and neurophysiology in murine experimental autoimmune myasthenia gravis. Clin Exp Immunol. 1983; 51(3):543-550.
    • (1983) Clin Exp Immunol , vol.51 , Issue.3 , pp. 543-550
    • Pachner, A.R.1    Kantor, F.S.2
  • 57
    • 84865963074 scopus 로고    scopus 로고
    • Distinct roles of muscle and motoneuron LRP4 in neuromuscular junction formation
    • Wu H, et al. Distinct roles of muscle and motoneuron LRP4 in neuromuscular junction formation. Neuron. 2012;75(1):94-107.
    • (2012) Neuron , vol.75 , Issue.1 , pp. 94-107
    • Wu, H.1
  • 58
    • 0022648662 scopus 로고
    • Antigenic modulation of human myotube acetylcholine receptor by myasthenic sera. Serum titer determines receptor internalization rate
    • Tzartos SJ, Sophianos D, Zimmerman K, Starzinski- Powitz A. Antigenic modulation of human myotube acetylcholine receptor by myasthenic sera. Serum titer determines receptor internalization rate. J Immunol. 1986;136(9):3231- 3238.
    • (1986) J Immunol , vol.136 , Issue.9 , pp. 3231-3238
    • Tzartos, S.J.1    Sophianos, D.2    Zimmerman, K.3    Starzinski-Powitz, A.4
  • 59
    • 84877131867 scopus 로고    scopus 로고
    • The role of MuSK in synapse formation and neuromuscular disease
    • Burden SJ, Yumoto N, Zhang W. The role of MuSK in synapse formation and neuromuscular disease. Cold Spring Harb Perspect Biol. 2013;5(5):a009167.
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , Issue.5
    • Burden, S.J.1    Yumoto, N.2    Zhang, W.3
  • 60
    • 84872062607 scopus 로고    scopus 로고
    • Lrp4 and wise interplay controls the formation and patterning of mammary and other skin appendage placodes by modulating wnt signaling
    • Ahn Y, Sims C, Logue JM, Weatherbee SD, Krumlauf R. Lrp4 and Wise interplay controls the formation and patterning of mammary and other skin appendage placodes by modulating Wnt signaling. Development. 2013;140(3):583-593.
    • (2013) Development , vol.140 , Issue.3 , pp. 583-593
    • Ahn, Y.1    Sims, C.2    Logue, J.M.3    Weatherbee, S.D.4    Krumlauf, R.5
  • 61
    • 34249795451 scopus 로고    scopus 로고
    • Rapid synapse elimination after postsynaptic protein synthesis inhibition in vivo
    • McCann CM, Nguyen QT, Santo Neto H, Lichtman JW. Rapid synapse elimination after postsynaptic protein synthesis inhibition in vivo. J Neurosci. 2007; 27(22):6064-6067.
    • (2007) J Neurosci , vol.27 , Issue.22 , pp. 6064-6067
    • McCann, C.M.1    Nguyen, Q.T.2    Santo Neto, H.3    Lichtman, J.W.4
  • 62
    • 1642487117 scopus 로고    scopus 로고
    • Inhibition of synapse assembly in mammalian muscle in vivo by RNA interference
    • Kong XC, Barzaghi P, Ruegg MA. Inhibition of synapse assembly in mammalian muscle in vivo by RNA interference. EMBO Rep. 2004;5(2):183-188.
    • (2004) EMBO Rep , vol.5 , Issue.2 , pp. 183-188
    • Kong, X.C.1    Barzaghi, P.2    Ruegg, M.A.3
  • 63
    • 33644844430 scopus 로고    scopus 로고
    • Synapse disassembly and formation of new synapses in postnatal muscle upon conditional inactivation of musk
    • Hesser BA, Henschel O, Witzemann V. Synapse disassembly and formation of new synapses in postnatal muscle upon conditional inactivation of MuSK. Mol Cell Neurosci. 2006;31(3):470-480.
    • (2006) Mol Cell Neurosci , vol.31 , Issue.3 , pp. 470-480
    • Hesser, B.A.1    Henschel, O.2    Witzemann, V.3
  • 64
    • 0018612959 scopus 로고
    • Activation of mouse complement by different classes of mouse antibody
    • Klaus GG, Pepys MB, Kitajima K, Askonas BA. Activation of mouse complement by different classes of mouse antibody. Immunology. 1979; 38(4):687-695.
    • (1979) Immunology , vol.38 , Issue.4 , pp. 687-695
    • Klaus, G.G.1    Pepys, M.B.2    Kitajima, K.3    Askonas, B.A.4
  • 65
    • 0019848470 scopus 로고
    • Activation of mouse complement by monoclonal mouse antibodies
    • Neuberger MS, Rajewsky K. Activation of mouse complement by monoclonal mouse antibodies. Eur J Immunol. 1981;11(12):1012-1016.
    • (1981) Eur J Immunol , vol.11 , Issue.12 , pp. 1012-1016
    • Neuberger, M.S.1    Rajewsky, K.2
  • 66
    • 2442622616 scopus 로고    scopus 로고
    • Anti-Ganglioside antibody-Mediated neuronal cytotoxicity and its protection by intravenous immunoglobulin: Implications for immune neuropathies
    • Zhang G, et al. Anti-ganglioside antibody-mediated neuronal cytotoxicity and its protection by intravenous immunoglobulin: implications for immune neuropathies. Brain. 2004;127(pt 5):1085-1100.
    • (2004) Brain , vol.127 , Issue.PART 5 , pp. 1085-1100
    • Zhang, G.1
  • 67
    • 77449144352 scopus 로고    scopus 로고
    • Antibody purification: Ammonium sulfate fractionation or gel filtration
    • Grodzki AC, Berenstein E. Antibody purification: ammonium sulfate fractionation or gel filtration. Methods Mol Biol. 2010;588:15-26.
    • (2010) Methods Mol Biol , vol.588 , pp. 15-26
    • Grodzki, A.C.1    Berenstein, E.2
  • 68
    • 0016755254 scopus 로고
    • Myasthenia gravis: Passive transfer from man to mouse
    • Toyka KV, Brachman DB, Pestronk A, Kao I. Myasthenia gravis: passive transfer from man to mouse. Science. 1975;190(4212):397-399.
    • (1975) Science , vol.190 , Issue.4212 , pp. 397-399
    • Toyka, K.V.1    Brachman, D.B.2    Pestronk, A.3    Kao, I.4
  • 69
    • 0032513058 scopus 로고    scopus 로고
    • Dimerization of the musclespecific kinase induces tyrosine phosphorylation of acetylcholine receptors and their aggregation on the surface of myotubes
    • Hopf C, Hoch W. Dimerization of the musclespecific kinase induces tyrosine phosphorylation of acetylcholine receptors and their aggregation on the surface of myotubes. J Biol Chem. 1998; 273(11):6467-6473.
    • (1998) J Biol Chem , vol.273 , Issue.11 , pp. 6467-6473
    • Hopf, C.1    Hoch, W.2
  • 70
    • 80855153205 scopus 로고    scopus 로고
    • Agrin binds to the N-Terminal region of lrp4 protein and stimulates association between lrp4 and the first immunoglobulin-Like domain in muscle-Specific kinase (MuSK)
    • Zhang W, Coldefy AS, Hubbard SR, Burden SJ. Agrin binds to the N-terminal region of Lrp4 protein and stimulates association between Lrp4 and the first immunoglobulin-like domain in muscle-specific kinase (MuSK). J Biol Chem. 2011; 286(47):40624-40630.
    • (2011) J Biol Chem , vol.286 , Issue.47 , pp. 40624-40630
    • Zhang, W.1    Coldefy, A.S.2    Hubbard, S.R.3    Burden, S.J.4
  • 71
    • 0032125483 scopus 로고    scopus 로고
    • Axon withdrawal during synapse elimination at the neuromuscular junction is accompanied by disassembly of the postsynaptic specialization and withdrawal of Schwann cell processes
    • Culican SM, Nelson CC, Lichtman JW. Axon withdrawal during synapse elimination at the neuromuscular junction is accompanied by disassembly of the postsynaptic specialization and withdrawal of Schwann cell processes. J Neurosci. 1998; 18(13):4953-4965.
    • (1998) J Neurosci , vol.18 , Issue.13 , pp. 4953-4965
    • Culican, S.M.1    Nelson, C.C.2    Lichtman, J.W.3
  • 72
    • 84858155813 scopus 로고    scopus 로고
    • Passive and active immunization models of musk-Ab positive myasthenia: Electrophysiological evidence for pre and postsynaptic defects
    • Viegas S, et al. Passive and active immunization models of MuSK-Ab positive myasthenia: electrophysiological evidence for pre and postsynaptic defects. Exp Neurol. 2012;234(2):506-512.
    • (2012) Exp Neurol , vol.234 , Issue.2 , pp. 506-512
    • Viegas, S.1
  • 73
    • 77956414899 scopus 로고    scopus 로고
    • Lrp4 regulates initiation of ureteric budding and is crucial for kidney formation - A mouse model for cenani-Lenz syndrome
    • Karner CM, et al. Lrp4 regulates initiation of ureteric budding and is crucial for kidney formation - a mouse model for Cenani-Lenz syndrome. PLoS One. 2010;5(4):e10418.
    • (2010) PLoS One , vol.5 , Issue.4
    • Karner, C.M.1
  • 74
    • 28444440976 scopus 로고    scopus 로고
    • Genetics of autoimmune myasthenia gravis: The multifaceted contribution of the HLA complex
    • Vandiedonck C, Giraud M, Garchon HJ. Genetics of autoimmune myasthenia gravis: the multifaceted contribution of the HLA complex. J Autoimmun. 2005; 25(suppl):6-11.
    • (2005) J Autoimmun , vol.25 , Issue.SUPPL.1 , pp. 6-11
    • Vandiedonck, C.1    Giraud, M.2    Garchon, H.J.3
  • 75
    • 33745645882 scopus 로고    scopus 로고
    • Strong association of MuSK antibodypositive myasthenia gravis and HLA-DR14-DQ5
    • Niks EH, et al. Strong association of MuSK antibodypositive myasthenia gravis and HLA-DR14-DQ5. Neurology. 2006;66(11):1772-1774.
    • (2006) Neurology , vol.66 , Issue.11 , pp. 1772-1774
    • Niks, E.H.1
  • 76
    • 33845873304 scopus 로고    scopus 로고
    • Neuromuscular development in the absence of programmed cell death: Phenotypic alteration of motoneurons and muscle
    • Buss RR, et al. Neuromuscular development in the absence of programmed cell death: phenotypic alteration of motoneurons and muscle. J Neurosci. 2006; 26(52):13413-13427.
    • (2006) J Neurosci , vol.26 , Issue.52 , pp. 13413-13427
    • Buss, R.R.1
  • 77
    • 84856563661 scopus 로고    scopus 로고
    • Wnt proteins regulate acetylcholine receptor clustering in muscle cells
    • Zhang B, Liang C, Bates R, Yin Y, Xiong WC, Mei L. Wnt proteins regulate acetylcholine receptor clustering in muscle cells. Mol Brain. 2012;5:7.
    • (2012) Mol Brain , vol.5 , pp. 7
    • Zhang, B.1    Liang, C.2    Bates, R.3    Yin, Y.4    Xiong, W.C.5    Mei, L.6
  • 78
    • 53049109653 scopus 로고    scopus 로고
    • HSP90β regulates rapsyn turnover and subsequent AChR cluster formation and maintenance
    • Luo S, et al. HSP90β regulates rapsyn turnover and subsequent AChR cluster formation and maintenance. Neuron. 2008;60(1):97-110.
    • (2008) Neuron , vol.60 , Issue.1 , pp. 97-110
    • Luo, S.1
  • 79
    • 84861991275 scopus 로고    scopus 로고
    • β-Catenin gain of function in muscles impairs neuromuscular junction formation
    • Wu H, et al. β-Catenin gain of function in muscles impairs neuromuscular junction formation. Development. 2012;139(13):2392-2404.
    • (2012) Development , vol.139 , Issue.13 , pp. 2392-2404
    • Wu, H.1
  • 80
    • 13444252597 scopus 로고    scopus 로고
    • Neuregulin- Induced expression of the acetylcholine receptor requires endocytosis of ErbB receptors
    • Yang XL, Huang YZ, Xiong WC, Mei L. Neuregulin- induced expression of the acetylcholine receptor requires endocytosis of ErbB receptors. Mol Cell Neurosci. 2005;28(2):335-346.
    • (2005) Mol Cell Neurosci , vol.28 , Issue.2 , pp. 335-346
    • Yang, X.L.1    Huang, Y.Z.2    Xiong, W.C.3    Mei, L.4


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