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Volumn 15, Issue 2, 2006, Pages 273-285

Mutant huntingtin alters MAPK signaling pathways in PC12 and striatal cells: ERK1/2 protects against mutant huntingtin-associated toxicity

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; CASPASE 3; CEP 11004; HUNTINGTIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MIXED LINEAGE KINASE; MUTANT PROTEIN; NEUROPROTECTIVE AGENT; POLYGLUTAMINE; PROTEIN KINASE INHIBITOR; STRESS ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 31144472414     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddi443     Document Type: Article
Times cited : (125)

References (64)
  • 1
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross, C.A. (2002) Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron, 35, 819-822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 2
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H.Y. and Orr, H.T. (2000) Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci., 23, 217-247.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 4
    • 3142640821 scopus 로고    scopus 로고
    • Huntington's disease: New paths to pathogenesis
    • Ross, C.A. (2004) Huntington's disease: New paths to pathogenesis. Cell, 118, 4-7.
    • (2004) Cell , vol.118 , pp. 4-7
    • Ross, C.A.1
  • 5
    • 0034571171 scopus 로고    scopus 로고
    • Huntington's disease: The challenge for cell biologists
    • Tobin, A.J. and Signer, E.R. (2000) Huntington's disease: The challenge for cell biologists. Trends Cell Biol., 10, 531-536.
    • (2000) Trends Cell Biol. , vol.10 , pp. 531-536
    • Tobin, A.J.1    Signer, E.R.2
  • 6
    • 0141891215 scopus 로고    scopus 로고
    • Pathogenesis of polyglutamine disorders: Aggregation revisited
    • Michalik, A. and Van Broeckhoven, C. (2003) Pathogenesis of polyglutamine disorders: Aggregation revisited. Hum. Mol. Genet., 12, R173-R186.
    • (2003) Hum. Mol. Genet. , vol.12
    • Michalik, A.1    Van Broeckhoven, C.2
  • 7
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates, G. (2003) Huntingtin aggregation and toxicity in Huntington's disease. Lancet, 361, 1642-1644.
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 8
    • 0028823892 scopus 로고
    • Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast
    • Waskiewicz, A.J. and Cooper, J.A. (1995) Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast. Curr. Opin. Cell Biol., 7, 798-805.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 798-805
    • Waskiewicz, A.J.1    Cooper, J.A.2
  • 9
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways
    • Tibbles, L.A. and Woodgett, J.R. (1999) The stress-activated protein kinase pathways. Cell. Mol. Life Sci., 55, 1230-1254.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1230-1254
    • Tibbles, L.A.1    Woodgett, J.R.2
  • 10
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • Seger, R. and Krebs, E.G. (1995) The MAPK signaling cascade. FASEB J., 9, 726-735.
    • (1995) FASEB J. , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 11
    • 0000790724 scopus 로고    scopus 로고
    • SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes
    • Liu, Y.F., Deth, R.C. and Devys, D. (1997) SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes. J. Biol. Chem., 272, 8121-8124.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8121-8124
    • Liu, Y.F.1    Deth, R.C.2    Devys, D.3
  • 12
    • 0037155198 scopus 로고    scopus 로고
    • Expression of full-length polyglutamine-expanded Huntingtin disrupts growth factor receptor signaling in rat pheochromocytoma (PC12) cells
    • Song, C., Perides, G. and Liu, Y.F. (2002) Expression of full-length polyglutamine-expanded Huntingtin disrupts growth factor receptor signaling in rat pheochromocytoma (PC12) cells. J. Biol. Chem., 277, 6703-6707.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6703-6707
    • Song, C.1    Perides, G.2    Liu, Y.F.3
  • 13
    • 0033168302 scopus 로고    scopus 로고
    • Cellular defects and altered gene expression in PC12 cells stably expressing mutant huntingtin
    • Li, S.H., Cheng, A.L., Li, H. and Li, X.J. (1999) Cellular defects and altered gene expression in PC12 cells stably expressing mutant huntingtin. J. Neurosci., 19, 5159-5172.
    • (1999) J. Neurosci. , vol.19 , pp. 5159-5172
    • Li, S.H.1    Cheng, A.L.2    Li, H.3    Li, X.J.4
  • 14
    • 14644430451 scopus 로고    scopus 로고
    • Expanded polyglutamine peptides disrupt EGF receptor signaling and glutamate transporter expression in Drosophila
    • Lievens, J.C., Rival, T., Iche, M., Chneiweiss, H. and Birman, S. (2005) Expanded polyglutamine peptides disrupt EGF receptor signaling and glutamate transporter expression in Drosophila. Hum. Mol. Genet., 14, 713-724.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 713-724
    • Lievens, J.C.1    Rival, T.2    Iche, M.3    Chneiweiss, H.4    Birman, S.5
  • 17
    • 0034703874 scopus 로고    scopus 로고
    • Intranuclear huntingtin increases the expression of caspase-1 and induces apoptosis
    • Li, S.H., Lam, S., Cheng, A.L. and Li, X.J. (2000) Intranuclear huntingtin increases the expression of caspase-1 and induces apoptosis. Hum. Mol. Genet., 9, 2859-2867.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2859-2867
    • Li, S.H.1    Lam, S.2    Cheng, A.L.3    Li, X.J.4
  • 19
    • 0242551370 scopus 로고    scopus 로고
    • Chronic activation of ERK and neurodegenerative diseases
    • Colucci-D'Amato, L., Perrone-Capano, C. and di Porzio, U. (2003) Chronic activation of ERK and neurodegenerative diseases. Bioessays, 25, 1085-1095.
    • (2003) Bioessays , vol.25 , pp. 1085-1095
    • Colucci-D'Amato, L.1    Perrone-Capano, C.2    di Porzio, U.3
  • 21
    • 1842608937 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 aids survival of neurites on neurons derived from pheochromocytoma. (PC-12) cells
    • Soeda, S., Imatoh, T., Ochiai, T., Koyanagi, S. and Shimeno, H. (2004) Plasminogen activator inhibitor-1 aids survival of neurites on neurons derived from pheochromocytoma. (PC-12) cells. Neuroreport, 15, 855-858.
    • (2004) Neuroreport , vol.15 , pp. 855-858
    • Soeda, S.1    Imatoh, T.2    Ochiai, T.3    Koyanagi, S.4    Shimeno, H.5
  • 23
    • 0033674628 scopus 로고    scopus 로고
    • Nuclear factor I/CCAAT box transcription factor trans-activating domain is a negative sensor of cellular stress
    • Morel, Y., Coumoul, X., Nalpas, A. and Barouki, R. (2000) Nuclear factor I/CCAAT box transcription factor trans-activating domain is a negative sensor of cellular stress. Mol. Pharmacol., 58, 1239-1246.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1239-1246
    • Morel, Y.1    Coumoul, X.2    Nalpas, A.3    Barouki, R.4
  • 27
    • 3242723420 scopus 로고    scopus 로고
    • A cell-based screen for drugs to treat Huntington's disease
    • Aiken, C.T., Tobin, A.J. and Schweitzer, E.S. (2004) A cell-based screen for drugs to treat Huntington's disease. Neurobiol. Dis., 16, 546-555.
    • (2004) Neurobiol. Dis. , vol.16 , pp. 546-555
    • Aiken, C.T.1    Tobin, A.J.2    Schweitzer, E.S.3
  • 28
    • 0035805504 scopus 로고    scopus 로고
    • Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing
    • Rigamonti, D., Sipione, S., Goffredo, D., Zuccato, C., Fossale, E. and Cattaneo, E. (2001) Huntingtin's neuroprotective activity occurs via inhibition of procaspase-9 processing. J. Biol. Chem., 276, 14545-14548.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14545-14548
    • Rigamonti, D.1    Sipione, S.2    Goffredo, D.3    Zuccato, C.4    Fossale, E.5    Cattaneo, E.6
  • 30
    • 2342562556 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in apoptosis regulation
    • Wada, T. and Penninger, J.M. (2004) Mitogen-activated protein kinases in apoptosis regulation. Oncogene, 23, 2838-2849.
    • (2004) Oncogene , vol.23 , pp. 2838-2849
    • Wada, T.1    Penninger, J.M.2
  • 31
    • 0036181363 scopus 로고    scopus 로고
    • Regulation of stress-activated protein kinase signaling pathways by protein phosphatases
    • Tamura, S., Hanada, M., Ohnishi, M., Katsura, K., Sasaki, M. and Kobayashi, T. (2002) Regulation of stress-activated protein kinase signaling pathways by protein phosphatases. Eur. J. Biochem., 269, 1060-1066.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1060-1066
    • Tamura, S.1    Hanada, M.2    Ohnishi, M.3    Katsura, K.4    Sasaki, M.5    Kobayashi, T.6
  • 33
    • 0035880474 scopus 로고    scopus 로고
    • Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease
    • Wyttenbach, A., Swartz, J., Kita, H., Thykjaer, T., Carmichael, J., Bradley, J., Brown, R., Maxwell, M., Schapira, A., Orntoft, T.F. et al. (2001) Polyglutamine expansions cause decreased CRE-mediated transcription and early gene expression changes prior to cell death in an inducible cell model of Huntington's disease. Hum. Mol. Genet., 10, 1829-1845.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1829-1845
    • Wyttenbach, A.1    Swartz, J.2    Kita, H.3    Thykjaer, T.4    Carmichael, J.5    Bradley, J.6    Brown, R.7    Maxwell, M.8    Schapira, A.9    Orntoft, T.F.10
  • 34
    • 0035182221 scopus 로고    scopus 로고
    • Stress management - Heat shock protein-70 and the regulation of apoptosis
    • Beere, H.M. and Green, D.R. (2001) Stress management - heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol., 11, 6-10.
    • (2001) Trends Cell Biol. , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 35
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick, J.M., Chan, H.Y., Gray-Board, G.L., Chai, Y., Paulson, H.L. and Bonini, N.M. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet., 23, 425-428.
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 36
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi, Y., Kume, A., Li, M., Doyu, M., Hata, M., Ohtsuka, K. and Sobue, G. (2000) Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J. Biol. Chem., 275, 8772-8778.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 37
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana, N.R., Tanaka, M., Wang, G. and Nukina, N. (2000) Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet., 9, 2009-2018.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 38
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila
    • Chan, H.Y., Warrick, J.M., Gray-Board, G.L., Paulson, H.L. and Bonini, N.M. (2000) Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila. Hum. Mol. Genet., 9, 2811-2820.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2811-2820
    • Chan, H.Y.1    Warrick, J.M.2    Gray-Board, G.L.3    Paulson, H.L.4    Bonini, N.M.5
  • 39
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings, C.J., Sun, Y., Opal, P., Antalffy, B., Mestril, R., Orr, H.T., Dillmann, W.H. and Zoghbi, H.Y. (2001) Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet., 10, 1511-1518.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 40
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi, H., Katsuno, M., Minamiyama, M., Sang, C., Pagoulatos, G., Angelidis, C., Kusakabe, M., Yoshiki, A., Kobayashi, Y., Doyu, M. et al. (2003) Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J. Neurosci., 23, 2203-2211.
    • (2003) J. Neurosci. , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5    Angelidis, C.6    Kusakabe, M.7    Yoshiki, A.8    Kobayashi, Y.9    Doyu, M.10
  • 41
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira, H., Breuer, P., Hayer-Hartl, M.K. and Hartl, F.U. (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Natl Acad. Sci. USA, 99 (Suppl. 4), 16412-16418.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.SUPPL. 4 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 42
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • Zhou, H., Li, S.H. and Li, X.J. (2001) Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J. Biol. Chem., 276, 48417-48424.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.H.2    Li, X.J.3
  • 44
    • 0037147130 scopus 로고    scopus 로고
    • K252a and CEP1347 are neuroprotective compounds that inhibit mixed-lineage kinase-3 and induce activation of Akt and ERK
    • Roux, P.P., Dorval, G., Boudreau, M., Angers-Loustau, A., Morris, S.J., Makkerh, J. and Barker, P.A. (2002) K252a and CEP1347 are neuroprotective compounds that inhibit mixed-lineage kinase-3 and induce activation of Akt and ERK. J. Biol. Chem., 277, 49473-49480.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49473-49480
    • Roux, P.P.1    Dorval, G.2    Boudreau, M.3    Angers-Loustau, A.4    Morris, S.J.5    Makkerh, J.6    Barker, P.A.7
  • 45
    • 1342344813 scopus 로고    scopus 로고
    • Mixed-lineage kinases: A target for the prevention of neurodegeneration
    • Wang, L.H., Besirli, C.G. and Johnson, E.M., Jr. (2004) Mixed-lineage kinases: A target for the prevention of neurodegeneration. Annu. Rev. Pharmacol. Toxicol., 44, 451-474.
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 451-474
    • Wang, L.H.1    Besirli, C.G.2    Johnson Jr., E.M.3
  • 46
    • 4143112468 scopus 로고    scopus 로고
    • Expanded huntingtin activates the c-Jun terminal kinase/c-Jun pathway prior to aggregate formation in striatal neurons in culture
    • Garcia, M., Charvin, D. and Caboche, J. (2004) Expanded huntingtin activates the c-Jun terminal kinase/c-Jun pathway prior to aggregate formation in striatal neurons in culture. Neuroscience, 127, 859-870.
    • (2004) Neuroscience , vol.127 , pp. 859-870
    • Garcia, M.1    Charvin, D.2    Caboche, J.3
  • 47
    • 0001388128 scopus 로고    scopus 로고
    • Expression of polyglutamine-expanded Huntingtin activates the SEK1-JNK pathway and induces apoptosis in a hippocampal neuronal cell line
    • Liu, Y.F. (1998) Expression of polyglutamine-expanded Huntingtin activates the SEK1-JNK pathway and induces apoptosis in a hippocampal neuronal cell line. J. Biol. Chem., 273, 28873-28877.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28873-28877
    • Liu, Y.F.1
  • 48
    • 0001583878 scopus 로고    scopus 로고
    • Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin
    • Liu, Y.F., Dorow, D. and Marshall, J. (2000) Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin. J. Biol. Chem., 275, 19035-19040.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19035-19040
    • Liu, Y.F.1    Dorow, D.2    Marshall, J.3
  • 49
    • 0038039288 scopus 로고    scopus 로고
    • Polyglutamine protein aggregation and toxicity are linked to the cellular stress response
    • Cowan, K.J., Diamond, M.I. and Welch, W.J. (2003) Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Hum. Mol. Genet., 12, 1377-1391.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1377-1391
    • Cowan, K.J.1    Diamond, M.I.2    Welch, W.J.3
  • 52
    • 15244352198 scopus 로고    scopus 로고
    • Emerging role for ERK as a key regulator of neuronal apoptosis
    • Cheung, E.C. and Slack, R.S. (2004) Emerging role for ERK as a key regulator of neuronal apoptosis. Sci. STKE, 2004, PE45.
    • (2004) Sci. STKE , vol.2004
    • Cheung, E.C.1    Slack, R.S.2
  • 54
    • 0037113879 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases are up-regulated and participate in cell death induced by polyglutamine expansion
    • Wu, Z.L., O'Kane, T.M., Scott, R.W., Savage, M.J. and Bozyczko-Coyne, D. (2002) Protein tyrosine phosphatases are up-regulated and participate in cell death induced by polyglutamine expansion. J. Biol. Chem., 277, 44208-44213.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44208-44213
    • Wu, Z.L.1    O'Kane, T.M.2    Scott, R.W.3    Savage, M.J.4    Bozyczko-Coyne, D.5
  • 55
    • 2942605831 scopus 로고    scopus 로고
    • Role of extracellular signal regulated kinases 1 and 2 in neuronal survival
    • Hetman, M. and Gozdz, A. (2004) Role of extracellular signal regulated kinases 1 and 2 in neuronal survival. Eur. J. Biochem., 271, 2050-2055.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2050-2055
    • Hetman, M.1    Gozdz, A.2
  • 56
    • 0033118665 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons
    • Singer, C.A., Figueroa-Masot, X.A., Batchelor, R.H. and Dorsa, D.M. (1999) The mitogen-activated protein kinase pathway mediates estrogen neuroprotection after glutamate toxicity in primary cortical neurons. J. Neurosci., 19, 2455-2463.
    • (1999) J. Neurosci. , vol.19 , pp. 2455-2463
    • Singer, C.A.1    Figueroa-Masot, X.A.2    Batchelor, R.H.3    Dorsa, D.M.4
  • 57
    • 16244392082 scopus 로고    scopus 로고
    • Deficits in experience-dependent cortical plasticity and sensory-discrimination learning in presymptomatic Huntington's disease mice
    • Mazarakis, N.K., Cybulska-Klosowicz, A., Grote, H., Pang, T., Van Dellen, A., Kossut, M., Blakemore, C. and Hannan, A.J. (2005) Deficits in experience-dependent cortical plasticity and sensory-discrimination learning in presymptomatic Huntington's disease mice. J. Neurosci., 25, 3059-3066.
    • (2005) J. Neurosci. , vol.25 , pp. 3059-3066
    • Mazarakis, N.K.1    Cybulska-Klosowicz, A.2    Grote, H.3    Pang, T.4    Van Dellen, A.5    Kossut, M.6    Blakemore, C.7    Hannan, A.J.8
  • 58
    • 0036382909 scopus 로고    scopus 로고
    • Abnormal phosphorylation of synapsin I predicts a neuronal transmission impairment in the R6/2 Huntington's disease transgenic mice
    • Lievens, J.C., Woodman, B., Mahal, A. and Bates, G.P. (2002) Abnormal phosphorylation of synapsin I predicts a neuronal transmission impairment in the R6/2 Huntington's disease transgenic mice. Mol. Cell. Neurosci., 20, 638-648.
    • (2002) Mol. Cell. Neurosci. , vol.20 , pp. 638-648
    • Lievens, J.C.1    Woodman, B.2    Mahal, A.3    Bates, G.P.4
  • 60
    • 23844494402 scopus 로고    scopus 로고
    • The duration, magnitude and compartmentalization of ERK MAP kinase activity: Mechanisms for providing signaling specificity
    • Ebisuya, M., Kondoh, K. and Nishida, E. (2005) The duration, magnitude and compartmentalization of ERK MAP kinase activity: Mechanisms for providing signaling specificity. J. Cell. Sci., 118, 2997-3002.
    • (2005) J. Cell. Sci. , vol.118 , pp. 2997-3002
    • Ebisuya, M.1    Kondoh, K.2    Nishida, E.3
  • 61
    • 0032527592 scopus 로고    scopus 로고
    • Generation and characterization of embryonic striatal conditionally immortalized ST14A cells
    • Cattaneo, E. and Conti, L. (1998) Generation and characterization of embryonic striatal conditionally immortalized ST14A cells. J. Neurosci. Res., 53, 223-234.
    • (1998) J. Neurosci. Res. , vol.53 , pp. 223-234
    • Cattaneo, E.1    Conti, L.2
  • 62
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A.P. and Vogelstein, B. (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem., 132, 6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 63
    • 10744223572 scopus 로고    scopus 로고
    • Complex alteration of NMDA receptors in transgenic Huntington's disease mouse brain: Analysis of mRNA and protein expression, plasma membrane association, interacting proteins, and phosphorylation
    • Luthi-Carter, R., Apostol, B.L., Dunah, A.W., DeJohn, M.M., Farrell, L.A., Bates, G.P., Young, A.B., Standaert, D.G., Thompson, L.M. and Cha, J.H. (2003) Complex alteration of NMDA receptors in transgenic Huntington's disease mouse brain: Analysis of mRNA and protein expression, plasma membrane association, interacting proteins, and phosphorylation. Neurobiol. Dis., 14, 624-636.
    • (2003) Neurobiol. Dis. , vol.14 , pp. 624-636
    • Luthi-Carter, R.1    Apostol, B.L.2    Dunah, A.W.3    DeJohn, M.M.4    Farrell, L.A.5    Bates, G.P.6    Young, A.B.7    Standaert, D.G.8    Thompson, L.M.9    Cha, J.H.10
  • 64
    • 0028329630 scopus 로고
    • Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues
    • Zheng, C.F. and Guan, K.L. (1994) Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues. EMBO J., 13, 1123-1131.
    • (1994) EMBO J. , vol.13 , pp. 1123-1131
    • Zheng, C.F.1    Guan, K.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.