메뉴 건너뛰기




Volumn , Issue , 2005, Pages 167-193

Prion protein, prion protein-like protein, and neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords


EID: 58149471049     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/0-387-23923-5_7     Document Type: Chapter
Times cited : (2)

References (77)
  • 1
    • 0029993449 scopus 로고    scopus 로고
    • Know your neighbors: Three phenotypes in null mutants of the myogenic bHLH gene MRF4
    • E. N. Olson, H. H. Arnold, P. W. Rigby, and B. J. Wold, Know your neighbors: three phenotypes in null mutants of the myogenic bHLH gene MRF4. Cell 85, 1-4 (1996).
    • (1996) Cell , vol.85 , pp. 1-4
    • Olson, E.N.1    Arnold, H.H.2    Rigby, P.W.3    Wold, B.J.4
  • 3
    • 0033942010 scopus 로고    scopus 로고
    • Identification of a novel gene encoding a PrP-like protein expressed as chimeric transcripts fused to PrP exon 1/2 in ataxic mouse line with a disrupted PrP gene
    • A. Li, S. Sakaguchi, R. Atarashi, B. C. Roy, R. Nakaoke, K. Arima, N. Okimura, J. Kopacek, and K. Shigematsu, Identification of a novel gene encoding a PrP-like protein expressed as chimeric transcripts fused to PrP exon 1/2 in ataxic mouse line with a disrupted PrP gene. Cell Mol Neurobiol 20, 553-67 (2000).
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 553-567
    • Li, A.1    Sakaguchi, S.2    Atarashi, R.3    Roy, B.C.4    Nakaoke, R.5    Arima, K.6    Okimura, N.7    Kopacek, J.8    Shigematsu, K.9
  • 5
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • S. B. Prusiner, Molecular biology of prion diseases. Science 252, 1515-22 (1991).
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 9
    • 0028703452 scopus 로고
    • PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology
    • J. C. Manson, A. R. Clarke, P. A. McBride, I. McConnell, and J. Hope, PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 3, 331-40 (1994).
    • (1994) Neurodegeneration , vol.3 , pp. 331-340
    • Manson, J.C.1    Clarke, A.R.2    McBride, P.A.3    McConnell, I.4    Hope, J.5
  • 10
    • 0027372297 scopus 로고
    • Kinetics of infectivity are dissociated from PrP accumulation in salivary glands of Creutzfeldt-Jakob disease agent-inoculated mice
    • S. Sakaguchi, S. Katamine, K. Yamanouchi, M. Kishikawa, R. Moriuchi, N. Yasukawa, T. Doi, and T. Miyamoto, Kinetics of infectivity are dissociated from PrP accumulation in salivary glands of Creutzfeldt-Jakob disease agent-inoculated mice. J Gen Virol 74(Pt 10), 2117-23 (1993).
    • (1993) J Gen Virol , vol.74 , Issue.PART 10 , pp. 2117-2123
    • Sakaguchi, S.1    Katamine, S.2    Yamanouchi, K.3    Kishikawa, M.4    Moriuchi, R.5    Yasukawa, N.6    Doi, T.7    Miyamoto, T.8
  • 12
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • J. C. Manson, A. R. Clarke, M. L. Hooper, L. Aitchison, I. McConnell, and J. Hope, 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 8, 121-7 (1994).
    • (1994) Mol Neurobiol , vol.8 , pp. 121-127
    • Manson, J.C.1    Clarke, A.R.2    Hooper, M.L.3    Aitchison, L.4    McConnell, I.5    Hope, J.6
  • 14
    • 0028820122 scopus 로고
    • Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent
    • S. Sakaguchi, S. Katamine, K. Shigematsu, A. Nakatani, R. Moriuchi, N. Nishida, K. Kurokawa, R. Nakaoke, H. Sato, K. Jishage, and et al., Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent. J Virol 69, 7586-92 (1995).
    • (1995) J Virol , vol.69 , pp. 7586-7592
    • Sakaguchi, S.1    Katamine, S.2    Shigematsu, K.3    Nakatani, A.4    Moriuchi, R.5    Nishida, N.6    Kurokawa, K.7    Nakaoke, R.8    Sato, H.9    Jishage, K.10
  • 15
    • 0035865398 scopus 로고    scopus 로고
    • Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain
    • D. Rossi, A. Cozzio, E. Flechsig, M. A. Klein, T. Rulicke, A. Aguzzi, and C. Weissmann, Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. Embo J 20, 694-702 (2001).
    • (2001) Embo J , vol.20 , pp. 694-702
    • Rossi, D.1    Cozzio, A.2    Flechsig, E.3    Klein, M.A.4    Rulicke, T.5    Aguzzi, A.6    Weissmann, C.7
  • 18
    • 0021173996 scopus 로고
    • Developments of a water-maze procedure for studying spatial learning in the rat
    • R. Morris, Developments of a water-maze procedure for studying spatial learning in the rat. J Neurosci Methods 11, 47-60 (1984).
    • (1984) J Neurosci Methods , vol.11 , pp. 47-60
    • Morris, R.1
  • 19
    • 0032926449 scopus 로고    scopus 로고
    • No hippocampal neuron or synaptic bouton loss in learningimpaired aged beta-amyloid precursor protein-null mice
    • A. L. Phinney, M. E. Calhoun, D. P. Wolfer, H. P. Lipp, and H. Zheng, No hippocampal neuron or synaptic bouton loss in learningimpaired aged beta-amyloid precursor protein-null mice. Neuroscience 90, 1207-1216 (1999).
    • (1999) Neuroscience , vol.90 , pp. 1207-1216
    • Phinney, A.L.1    Calhoun, M.E.2    Wolfer, D.P.3    Lipp, H.P.4    Zheng, H.5
  • 20
    • 0026338819 scopus 로고
    • A computer-controlled Y-maze for the analysis of vibrissotactile discrimination learning in mice
    • H. P. Lipp, and H. Van der Loos, A computer-controlled Y-maze for the analysis of vibrissotactile discrimination learning in mice. Behav Brain Res 45, 135-145 (1991).
    • (1991) Behav Brain Res , vol.45 , pp. 135-145
    • Lipp, H.P.1    Van Der Loos, H.2
  • 22
    • 0020576940 scopus 로고
    • Vasopressin potentiation in the performance of a learned appetitive task: Reversal by a pressor antagonist analog of vasopressin
    • A. Ettenberg, M. L. Moal, G. F. Koob, and F. E. Bloom, Vasopressin potentiation in the performance of a learned appetitive task: Reversal by a pressor antagonist analog of vasopressin. Pharmacol Biochem Behav 18, 645-647 (1983).
    • (1983) Pharmacol Biochem Behav , vol.18 , pp. 645-647
    • Ettenberg, A.1    Moal, M.L.2    Koob, G.F.3    Bloom, F.E.4
  • 23
    • 0023931486 scopus 로고
    • Infrapyramidal mossy fibers and two-way avoidance learning: Developmental modification of hippocampal circuitry and adult behavior of rats and mice
    • H. P. Lipp, H. Schwegler, B. Heimrich, and P. Driscoll, Infrapyramidal mossy fibers and two-way avoidance learning: Developmental modification of hippocampal circuitry and adult behavior of rats and mice. J Neurosci 8, 1905-1921 (1988).
    • (1988) J Neurosci , vol.8 , pp. 1905-1921
    • Lipp, H.P.1    Schwegler, H.2    Heimrich, B.3    Driscoll, P.4
  • 27
    • 0028793453 scopus 로고
    • Patch-clamp analysis of synaptic transmission to cerebellar purkinje cells of prion protein knockout mice
    • J. W. Herms, H. A. Kretzchmar, S. Titz, and B. U. Keller, Patch-clamp analysis of synaptic transmission to cerebellar purkinje cells of prion protein knockout mice. Eur J Neurosci 7, 2508-12 (1995).
    • (1995) Eur J Neurosci , vol.7 , pp. 2508-2512
    • Herms, J.W.1    Kretzchmar, H.A.2    Titz, S.3    Keller, B.U.4
  • 28
    • 0029916617 scopus 로고    scopus 로고
    • Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus
    • P. M. Lledo, P. Tremblay, S. J. DeArmond, S. B. Prusiner, and R. A. Nicoll, Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc Natl Acad Sci U S A 93, 2403-7 (1996).
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 2403-2407
    • Lledo, P.M.1    Tremblay, P.2    DeArmond, S.J.3    Prusiner, S.B.4    Nicoll, R.A.5
  • 31
    • 0028356488 scopus 로고
    • Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous systems
    • D. R. Borchelt, V. E. Koliatsos, M. Guarnieri, C. A. Pardo, S. S. Sisodia, and D. L. Price, Rapid anterograde axonal transport of the cellular prion glycoprotein in the peripheral and central nervous systems. J Biol Chem 269, 14711-4 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 14711-14714
    • Borchelt, D.R.1    Koliatsos, V.E.2    Guarnieri, M.3    Pardo, C.A.4    Sisodia, S.S.5    Price, D.L.6
  • 32
    • 0035716992 scopus 로고    scopus 로고
    • Abnormal activation of glial cells in the brains of prion protein-deficient mice ectopically expressing prion protein-like protein, PrPLP/Dpl
    • R. Atarashi, S. Sakaguchi, K. Shigematsu, K. Arima, N. Okimura, N. Yamaguchi, A. Li, J. Kopacek, and S. Katamine, Abnormal activation of glial cells in the brains of prion protein-deficient mice ectopically expressing prion protein-like protein, PrPLP/Dpl. Mol Med 7, 803-9 (2001).
    • (2001) Mol Med , vol.7 , pp. 803-809
    • Atarashi, R.1    Sakaguchi, S.2    Shigematsu, K.3    Arima, K.4    Okimura, N.5    Yamaguchi, N.6    Li, A.7    Kopacek, J.8    Katamine, S.9
  • 33
    • 0028902465 scopus 로고
    • Developmental expression of the prion protein gene in glial cells
    • M. Moser, R. J. Colello, U. Pott, and B. Oesch, Developmental expression of the prion protein gene in glial cells. Neuron 14, 509-17 (1995).
    • (1995) Neuron , vol.14 , pp. 509-517
    • Moser, M.1    Colello, R.J.2    Pott, U.3    Oesch, B.4
  • 36
    • 0030728698 scopus 로고    scopus 로고
    • Pre-mRNA processing and the CTD of RNA polymerase II: The tail that wags the dog
    • E. J. Steinmetz, Pre-mRNA processing and the CTD of RNA polymerase II: The tail that wags the dog. Cell 89, 491-494 (1997).
    • (1997) Cell , vol.89 , pp. 491-494
    • Steinmetz, E.J.1
  • 38
    • 0033678443 scopus 로고    scopus 로고
    • Physiological expression of the gene for PrP-like protein, PrPLP/Dpl, by brain endothelial cells and its ectopic expression in neurons of PrP-deficient mice ataxic due to Purkinje cell degeneration
    • A. Li, S. Sakaguchi, K. Shigematsu, R. Atarashi, B. C. Roy, R. Nakaoke, K. Arima, N. Okimura, J. Kopacek, and S. Katamine, Physiological expression of the gene for PrP-like protein, PrPLP/Dpl, by brain endothelial cells and its ectopic expression in neurons of PrP-deficient mice ataxic due to Purkinje cell degeneration. Am J Pathol 157, 1447-52 (2000).
    • (2000) Am J Pathol , vol.157 , pp. 1447-1452
    • Li, A.1    Sakaguchi, S.2    Shigematsu, K.3    Atarashi, R.4    Roy, B.C.5    Nakaoke, R.6    Arima, K.7    Okimura, N.8    Kopacek, J.9    Katamine, S.10
  • 39
    • 0034282872 scopus 로고    scopus 로고
    • Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic productioninthe brainsof Prnp (0/0) mice predisposedtoPurkinje cell loss
    • G. L. Silverman, K. Qin, R. C. Moore, Y. Yang, P. Mastrangelo, P. Tremblay, S. B. Prusiner, F. E. Cohen, and D. Westaway, Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic productioninthe brainsof Prnp (0/0) mice predisposedtoPurkinje cell loss. J Biol Chem 275, 26834-41 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 26834-26841
    • Silverman, G.L.1    Qin, K.2    Moore, R.C.3    Yang, Y.4    Mastrangelo, P.5    Tremblay, P.6    Prusiner, S.B.7    Cohen, F.E.8    Westaway, D.9
  • 41
    • 0037163874 scopus 로고    scopus 로고
    • Doppel and PrP (C) do not share the same membrane microenvironment
    • Y. Shaked, N. Hijazi, and R. Gabizon, Doppel and PrP (C) do not share the same membrane microenvironment. FEBS Lett 530, 85-8 (2002).
    • (2002) FEBS Lett , vol.530 , pp. 85-88
    • Shaked, Y.1    Hijazi, N.2    Gabizon, R.3
  • 45
    • 1542618236 scopus 로고    scopus 로고
    • Transgenedriven expression of the Doppel protein in Purkinje cells causes Purkinje cell degeneration and motor impairment
    • L. Anderson, D. Rossi, J. Linehan, S. Brandner, and C. Weissmann, Transgenedriven expression of the Doppel protein in Purkinje cells causes Purkinje cell degeneration and motor impairment. Proc Natl Acad Sci U S A 101, 3644-3649 (2004).
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3644-3649
    • Anderson, L.1    Rossi, D.2    Linehan, J.3    Brandner, S.4    Weissmann, C.5
  • 46
    • 0043208949 scopus 로고    scopus 로고
    • Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration
    • R. Atarashi, N. Nishida, K. Shigematsu, S. Goto, T. Kondo, S. Sakaguchi, and S. Katamine, Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/doppel-induced Neurodegeneration. J Biol Chem 278, 28944-9 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 28944-28949
    • Atarashi, R.1    Nishida, N.2    Shigematsu, K.3    Goto, S.4    Kondo, T.5    Sakaguchi, S.6    Katamine, S.7
  • 47
    • 0034721767 scopus 로고    scopus 로고
    • Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases
    • Y. Zhang, W. Swietnicki, M. G. Zagorski, W. K. Surewicz, and F. D. Sonnichsen, Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J Biol Chem 275, 33650-4 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 33650-33654
    • Zhang, Y.1    Swietnicki, W.2    Zagorski, M.G.3    Surewicz, W.K.4    Sonnichsen, F.D.5
  • 50
    • 0033615415 scopus 로고    scopus 로고
    • Perspectives: Neurobiology. PrP's double causes trouble
    • C. Weissmann, and A. Aguzzi, Perspectives: neurobiology. PrP's double causes trouble. Science 286, 914-5 (1999).
    • (1999) Science , vol.286 , pp. 914-915
    • Weissmann, C.1    Aguzzi, A.2
  • 51
    • 0034950034 scopus 로고    scopus 로고
    • Electron paramagnetic resonance evidence for binding of Cu (2+) to the C-terminal domain of the murine prion protein
    • G. M. Cereghetti, A. Schweiger, R. Glockshuber, and S. Van Doorslaer, Electron paramagnetic resonance evidence for binding of Cu (2+) to the C-terminal domain of the murine prion protein. Biophys J 81, 516-25 (2001).
    • (2001) Biophys J , vol.81 , pp. 516-525
    • Cereghetti, G.M.1    Schweiger, A.2    Glockshuber, R.3    Van Doorslaer, S.4
  • 54
    • 0030811015 scopus 로고    scopus 로고
    • Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix
    • T. Muramoto, S. J. DeArmond, M. Scott, G. C. Telling, F. E. Cohen, and S. B. Prusiner, Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix. Nat Med 3, 750-5 (1997).
    • (1997) Nat Med , vol.3 , pp. 750-755
    • Muramoto, T.1    DeArmond, S.J.2    Scott, M.3    Telling, G.C.4    Cohen, F.E.5    Prusiner, S.B.6
  • 56
    • 0037166240 scopus 로고    scopus 로고
    • Identification of the heparan sulfate binding sites inthe cellular prion protein
    • R. G. Warner, C. Hundt, S. Weiss, and J. E. Turnbull, Identification of the heparan sulfate binding sites inthe cellular prion protein. J Biol Chem 277, 18421-30 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 18421-18430
    • Warner, R.G.1    Hundt, C.2    Weiss, S.3    Turnbull, J.E.4
  • 60
    • 0037080043 scopus 로고    scopus 로고
    • Lack of prion protein expression results in a neuronal phenotype sensitive to stress
    • D. R. Brown, R. S. Nicholas, and L. Canevari, Lack of prion protein expression results in a neuronal phenotype sensitive to stress. J Neurosci Res 67, 211-24 (2002).
    • (2002) J Neurosci Res , vol.67 , pp. 211-224
    • Brown, D.R.1    Nicholas, R.S.2    Canevari, L.3
  • 62
    • 0035914410 scopus 로고    scopus 로고
    • Prion protein protects human neurons against Bax-mediated apoptosis
    • Y. Bounhar, Y. Zhang, C. G. Goodyer, and A. LeBlanc, Prion protein protects human neurons against Bax-mediated apoptosis. J Biol Chem 276, 39145-9 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 39145-39149
    • Bounhar, Y.1    Zhang, Y.2    Goodyer, C.G.3    LeBlanc, A.4
  • 63
    • 0028922696 scopus 로고
    • Etiology and pathogenesis of prion diseases
    • S. J. DeArmond, and S. B. Prusiner, Etiology and pathogenesis of prion diseases. Am J Pathol 146, 785-811 (1995).
    • (1995) Am J Pathol , vol.146 , pp. 785-811
    • DeArmond, S.J.1    Prusiner, S.B.2
  • 64
    • 0035815709 scopus 로고    scopus 로고
    • In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodies
    • T. Yokoyama, K. M. Kimura, Y. Ushiki, S. Yamada, A. Morooka, T. Nakashiba, T. Sassa, and S. Itohara, In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodies. J Biol Chem 276, 11265-71 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 11265-11271
    • Yokoyama, T.1    Kimura, K.M.2    Ushiki, Y.3    Yamada, S.4    Morooka, A.5    Nakashiba, T.6    Sassa, T.7    Itohara, S.8
  • 67
    • 0026703146 scopus 로고
    • Demyelinating peripheral neuropathy in Creutzfeldt-Jakob disease
    • M. Y. Neufeld, J. Josiphov, and A. D. Korczyn, Demyelinating peripheral neuropathy in Creutzfeldt-Jakob disease. Muscle Nerve 15, 1234-9 (1992).
    • (1992) Muscle Nerve , vol.15 , pp. 1234-1239
    • Neufeld, M.Y.1    Josiphov, J.2    Korczyn, A.D.3
  • 68
    • 0036184716 scopus 로고    scopus 로고
    • Expression of doppel in the CNS of mice does not modulate transmissible spongiform encephalopathy disease
    • N. L. Tuzi, E. Gall, D. Melton, and J. C. Manson, Expression of doppel in the CNS of mice does not modulate transmissible spongiform encephalopathy disease. J Gen Virol 83, 705-11 (2002).
    • (2002) J Gen Virol , vol.83 , pp. 705-711
    • Tuzi, N.L.1    Gall, E.2    Melton, D.3    Manson, J.C.4
  • 70
    • 0033009241 scopus 로고    scopus 로고
    • Activitydependent regulation of alternative splicing patterns in the rat brain
    • R. Daoud, M. Da Penha Berzaghi, F. Siedler, M. Hubener, and S. Stamm, Activitydependent regulation of alternative splicing patterns in the rat brain. Eur J Neurosci 11, 788-802 (1999).
    • (1999) Eur J Neurosci , vol.11 , pp. 788-802
    • Daoud, R.1    Da Penha Berzaghi, M.2    Siedler, F.3    Hubener, M.4    Stamm, S.5
  • 71
    • 0037101633 scopus 로고    scopus 로고
    • Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain
    • R. Daoud, G. Mies, A. Smialowska, L. Olah, K. A. Hossmann, and S. Stamm, Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain. J Neurosci 22, 5889-99 (2002).
    • (2002) J Neurosci , vol.22 , pp. 5889-5899
    • Daoud, R.1    Mies, G.2    Smialowska, A.3    Olah, L.4    Hossmann, K.A.5    Stamm, S.6
  • 72
    • 0033568704 scopus 로고    scopus 로고
    • Structural roles of acetylcholinesterase variants in biology and pathology
    • D. Grisaru, M. Sternfeld, A. Eldor, D. Glick, and H. Soreq, Structural roles of acetylcholinesterase variants in biology and pathology. Eur J Biochem 264, 672-86 (1999).
    • (1999) Eur J Biochem , vol.264 , pp. 672-686
    • Grisaru, D.1    Sternfeld, M.2    Eldor, A.3    Glick, D.4    Soreq, H.5
  • 73
    • 0031882856 scopus 로고    scopus 로고
    • Cloning of a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation
    • Y. Imai, N. Matsuo, S. Ogawa, M. Tohyama, and T. Takagi, Cloning of a gene, YT521, for a novel RNA splicing-related protein induced by hypoxia/reoxygenation. Brain Res Mol Brain Res 53, 33-40 (1998).
    • (1998) Brain Res Mol Brain Res , vol.53 , pp. 33-40
    • Imai, Y.1    Matsuo, N.2    Ogawa, S.3    Tohyama, M.4    Takagi, T.5
  • 74
    • 0034967218 scopus 로고    scopus 로고
    • Bax kappa, a novel Bax splice variant from ischemic rat brain lacking an ART domain, promotes neuronal cell death
    • K. L. Jin, S. H. Graham, X. O. Mao, X. He, T. Nagayama, R. P. Simon, and D. A. Greenberg, Bax kappa, a novel Bax splice variant from ischemic rat brain lacking an ART domain, promotes neuronal cell death. J Neurochem 77, 1508-19 (2001).
    • (2001) J Neurochem , vol.77 , pp. 1508-1519
    • Jin, K.L.1    Graham, S.H.2    Mao, X.O.3    He, X.4    Nagayama, T.5    Simon, R.P.6    Greenberg, D.A.7
  • 75
    • 0032574973 scopus 로고    scopus 로고
    • Acute stress facilitates longlasting changes in cholinergic gene expression
    • D. Kaufer, A. Friedman, S. Seidman, and H. Soreq, Acute stress facilitates longlasting changes in cholinergic gene expression. Nature 393, 373-7 (1998).
    • (1998) Nature , vol.393 , pp. 373-377
    • Kaufer, D.1    Friedman, A.2    Seidman, S.3    Soreq, H.4
  • 76
    • 0035912224 scopus 로고    scopus 로고
    • A CaMK IV responsive RNA element mediates depolarizationinduced alternative splicing of ion channels
    • J. Xie, and D. L. Black, A CaMK IV responsive RNA element mediates depolarizationinduced alternative splicing of ion channels. Nature 410, 936-9 (2001).
    • (2001) Nature , vol.410 , pp. 936-939
    • Xie, J.1    Black, D.L.2
  • 77
    • 0141887509 scopus 로고    scopus 로고
    • Patterned Purkinje cell death in the cerebellum
    • J. R. Sarna, and R. Hawkes, Patterned Purkinje cell death in the cerebellum. Prog Neurobiol 70, 473-507 (2003).
    • (2003) Prog Neurobiol , vol.70 , pp. 473-507
    • Sarna, J.R.1    Hawkes, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.