메뉴 건너뛰기




Volumn 12, Issue 4, 2012, Pages 586-599

Structure-oriented review of 14-3-3 protein isoforms in geriatric neuroscience

Author keywords

14 3 3 proteins; Alzheimer's disease; Atherosclerosis; Cerebral infarction; Neurogenesis; Polyglutamine disease

Indexed keywords

ALPHA SYNUCLEIN; APOPTOSIS SIGNAL REGULATING KINASE 1; ATAXIN 1; BREAKPOINT CLUSTER REGION PROTEIN; ISOPROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; POLYGLUTAMINE; PROTEIN 14 3 3; PROTEIN BAD; PROTEIN BCL 2; PROTEIN KINASE B; RAF PROTEIN; TAU PROTEIN; TRANSCRIPTION FACTOR FKHR; TRYPTOPHAN HYDROXYLASE;

EID: 84866758053     PISSN: 14441586     EISSN: 14470594     Source Type: Journal    
DOI: 10.1111/j.1447-0594.2012.00860.x     Document Type: Review
Times cited : (11)

References (88)
  • 1
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: a historic overview
    • Aitken A. 14-3-3 proteins: a historic overview. Semin Cancer Biol 2006; 16: 162-172.
    • (2006) Semin Cancer Biol , vol.16 , pp. 162-172
    • Aitken, A.1
  • 2
    • 0026494876 scopus 로고
    • 14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins
    • Aitken A, Collinge DB, van Heusden BP etal. 14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins. Trends Biochem Sci 1992; 17: 498-501.
    • (1992) Trends Biochem Sci , vol.17 , pp. 498-501
    • Aitken, A.1    Collinge, D.B.2    van Heusden, B.P.3
  • 3
    • 33846149648 scopus 로고    scopus 로고
    • DISC1 regulates the transport of the NUDEL/LIS1/14-3-3epsilon complex through kinesin-1
    • Taya S, Shinoda T, Tsuboi D etal. DISC1 regulates the transport of the NUDEL/LIS1/14-3-3epsilon complex through kinesin-1. J Neurosci 2007; 27: 15-26.
    • (2007) J Neurosci , vol.27 , pp. 15-26
    • Taya, S.1    Shinoda, T.2    Tsuboi, D.3
  • 4
    • 80455154960 scopus 로고    scopus 로고
    • Structural basis of 14-3-3 protein functions
    • Obsil T, Obsilova V. Structural basis of 14-3-3 protein functions. Semin Cell Dev Biol 2011; 22: 663-672.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 663-672
    • Obsil, T.1    Obsilova, V.2
  • 5
    • 0141722623 scopus 로고    scopus 로고
    • 14-3-3 proteins in the nervous system
    • Berg D, Holzmann C, Riess O. 14-3-3 proteins in the nervous system. Nat Rev Neurosci 2003; 4: 752-762.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 752-762
    • Berg, D.1    Holzmann, C.2    Riess, O.3
  • 6
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 1996; 87: 619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 7
    • 0037726598 scopus 로고    scopus 로고
    • Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1
    • Chen HK, Fernandez-Funez P, Acevedo SF etal. Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1. Cell 2003; 113: 457-468.
    • (2003) Cell , vol.113 , pp. 457-468
    • Chen, H.K.1    Fernandez-Funez, P.2    Acevedo, S.F.3
  • 8
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty MK, Morrison DK. Unlocking the code of 14-3-3. J Cell Sci 2004; 117: 1875-1884.
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 9
    • 24344460521 scopus 로고    scopus 로고
    • 14-3-3 proteins - an update
    • Mhawech P. 14-3-3 proteins - an update. Cell Res 2005; 15: 228-236.
    • (2005) Cell Res , vol.15 , pp. 228-236
    • Mhawech, P.1
  • 10
    • 15544385930 scopus 로고    scopus 로고
    • Differential functions of 14-3-3 isoforms in vertebrate development
    • Muslin AJ, Lau JM. Differential functions of 14-3-3 isoforms in vertebrate development. Curr Top Dev Biol 2005; 65: 211-228.
    • (2005) Curr Top Dev Biol , vol.65 , pp. 211-228
    • Muslin, A.J.1    Lau, J.M.2
  • 11
    • 0031807577 scopus 로고    scopus 로고
    • 14-3-3 proteins in neuronal development and function
    • Skoulakis EM, Davis RL. 14-3-3 proteins in neuronal development and function. Mol Neurobiol 1998; 16: 269-284.
    • (1998) Mol Neurobiol , vol.16 , pp. 269-284
    • Skoulakis, E.M.1    Davis, R.L.2
  • 12
    • 0038724088 scopus 로고    scopus 로고
    • The 14-3-3 proteins: gene, gene expression, and function
    • Takahashi Y. The 14-3-3 proteins: gene, gene expression, and function. Neurochem Res 2003; 28: 1265-1273.
    • (2003) Neurochem Res , vol.28 , pp. 1265-1273
    • Takahashi, Y.1
  • 13
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion G, Avruch J. 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J Biol Chem 2002; 277: 3061-3064.
    • (2002) J Biol Chem , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 14
    • 0035473486 scopus 로고    scopus 로고
    • 14-3-3 proteins; bringing new definitions to scaffolding
    • Tzivion G, Shen YH, Zhu J. 14-3-3 proteins; bringing new definitions to scaffolding. Oncogene 2001; 20: 6331-6338.
    • (2001) Oncogene , vol.20 , pp. 6331-6338
    • Tzivion, G.1    Shen, Y.H.2    Zhu, J.3
  • 15
    • 22944479314 scopus 로고    scopus 로고
    • JNK antagonizes Akt-mediated survival signals by phosphorylating 14-3-3
    • Sunayama J, Tsuruta F, Masuyama N, Gotoh Y. JNK antagonizes Akt-mediated survival signals by phosphorylating 14-3-3. J Cell Biol 2005; 170: 295-304.
    • (2005) J Cell Biol , vol.170 , pp. 295-304
    • Sunayama, J.1    Tsuruta, F.2    Masuyama, N.3    Gotoh, Y.4
  • 17
    • 4844230325 scopus 로고    scopus 로고
    • 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease
    • Umahara T, Uchihara T, Tsuchiya K etal. 14-3-3 proteins and zeta isoform containing neurofibrillary tangles in patients with Alzheimer's disease. Acta Neuropathol 2004; 108: 279-286.
    • (2004) Acta Neuropathol , vol.108 , pp. 279-286
    • Umahara, T.1    Uchihara, T.2    Tsuchiya, K.3
  • 18
    • 7444250839 scopus 로고    scopus 로고
    • Immunolocalization of 14-3-3 isoforms in brains with Pick body disease
    • Umahara T, Uchihara T, Tsuchiya K etal. Immunolocalization of 14-3-3 isoforms in brains with Pick body disease. Neurosci Lett 2004; 371: 215-219.
    • (2004) Neurosci Lett , vol.371 , pp. 215-219
    • Umahara, T.1    Uchihara, T.2    Tsuchiya, K.3
  • 20
    • 0036896686 scopus 로고    scopus 로고
    • Accumulation of 14-3-3 proteins in glial cytoplasmic inclusions in multiple system atrophy
    • Kawamoto Y, Akiguchi I, Nakamura S, Budka H. Accumulation of 14-3-3 proteins in glial cytoplasmic inclusions in multiple system atrophy. Ann Neurol 2002; 52: 722-731.
    • (2002) Ann Neurol , vol.52 , pp. 722-731
    • Kawamoto, Y.1    Akiguchi, I.2    Nakamura, S.3    Budka, H.4
  • 21
    • 77955495045 scopus 로고    scopus 로고
    • 14-3-3 proteins and spinocerebellar ataxia type 1: from molecular interaction to human neuropathology
    • Umahara T, Uchihara T. 14-3-3 proteins and spinocerebellar ataxia type 1: from molecular interaction to human neuropathology. Cerebellum 2010; 9: 183-189.
    • (2010) Cerebellum , vol.9 , pp. 183-189
    • Umahara, T.1    Uchihara, T.2
  • 22
    • 33847064609 scopus 로고    scopus 로고
    • Intranuclear immunolocalization of 14-3-3 protein isoforms in brains with spinocerebellar ataxia type 1
    • Umahara T, Uchihara T, Yagishita S, Nakamura A, Tsuchiya K, Iwamoto T. Intranuclear immunolocalization of 14-3-3 protein isoforms in brains with spinocerebellar ataxia type 1. Neurosci Lett 2007; 414: 130-135.
    • (2007) Neurosci Lett , vol.414 , pp. 130-135
    • Umahara, T.1    Uchihara, T.2    Yagishita, S.3    Nakamura, A.4    Tsuchiya, K.5    Iwamoto, T.6
  • 23
    • 0037142070 scopus 로고    scopus 로고
    • Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth
    • Urano T, Saito T, Tsukui T etal. Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. Nature 2002; 417: 871-875.
    • (2002) Nature , vol.417 , pp. 871-875
    • Urano, T.1    Saito, T.2    Tsukui, T.3
  • 24
    • 2942616864 scopus 로고    scopus 로고
    • 14-3-3sigma is down-regulated in human prostate cancer
    • Urano T, Takahashi S, Suzuki T etal. 14-3-3sigma is down-regulated in human prostate cancer. Biochem Biophys Res Commun 2004; 319: 795-800.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 795-800
    • Urano, T.1    Takahashi, S.2    Suzuki, T.3
  • 25
    • 58249142180 scopus 로고    scopus 로고
    • Isoform-dependent immunolocalization of 14-3-3 proteins in developing rat cerebellum
    • Umahara T, Uchihara T, Nakamura A, Iwamoto T. Isoform-dependent immunolocalization of 14-3-3 proteins in developing rat cerebellum. Brain Res 2009; 1253: 15-26.
    • (2009) Brain Res , vol.1253 , pp. 15-26
    • Umahara, T.1    Uchihara, T.2    Nakamura, A.3    Iwamoto, T.4
  • 26
    • 80052029677 scopus 로고    scopus 로고
    • Differential expression of 14-3-3 protein-isoforms in developing rat hippocampus, cortex, rostral migratory stream, olfactory bulb, and white matter
    • Umahara T, Uchihara T, Nakamura A, Iwamoto T. Differential expression of 14-3-3 protein-isoforms in developing rat hippocampus, cortex, rostral migratory stream, olfactory bulb, and white matter. Brain Res 2011; 1410: 1-11.
    • (2011) Brain Res , vol.1410 , pp. 1-11
    • Umahara, T.1    Uchihara, T.2    Nakamura, A.3    Iwamoto, T.4
  • 27
    • 0038757833 scopus 로고    scopus 로고
    • 14-3-3epsilon is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome
    • Toyo-oka K, Shionoya A, Gambello MJ etal. 14-3-3epsilon is important for neuronal migration by binding to NUDEL: a molecular explanation for Miller-Dieker syndrome. Nat Genet 2003; 34: 274-285.
    • (2003) Nat Genet , vol.34 , pp. 274-285
    • Toyo-oka, K.1    Shionoya, A.2    Gambello, M.J.3
  • 28
    • 0038500794 scopus 로고    scopus 로고
    • Down-regulation of 14-3-3 eta gene expression by IGF-I in mouse cerebellum during postnatal development
    • Zhang J, Popken GJ, Ye P, D'Ercole AJ. Down-regulation of 14-3-3 eta gene expression by IGF-I in mouse cerebellum during postnatal development. Brain Res Dev Brain Res 2003; 143: 199-206.
    • (2003) Brain Res Dev Brain Res , vol.143 , pp. 199-206
    • Zhang, J.1    Popken, G.J.2    Ye, P.3    D'Ercole, A.J.4
  • 29
    • 0037127035 scopus 로고    scopus 로고
    • Immunolocalisation of 14-3-3 isoforms in normal and scrapie-infected murine brain
    • Baxter HC, Liu WG, Forster JL, Aitken A, Fraser JR. Immunolocalisation of 14-3-3 isoforms in normal and scrapie-infected murine brain. Neuroscience 2002; 109: 5-14.
    • (2002) Neuroscience , vol.109 , pp. 5-14
    • Baxter, H.C.1    Liu, W.G.2    Forster, J.L.3    Aitken, A.4    Fraser, J.R.5
  • 30
    • 34547657218 scopus 로고    scopus 로고
    • Intranuclear localization and isoform-dependent translocation of 14-3-3 proteins in human brain with infarction
    • Umahara T, Uchihara T, Tsuchiya K, Nakamura A, Iwamoto T. Intranuclear localization and isoform-dependent translocation of 14-3-3 proteins in human brain with infarction. J Neurol Sci 2007; 260: 159-166.
    • (2007) J Neurol Sci , vol.260 , pp. 159-166
    • Umahara, T.1    Uchihara, T.2    Tsuchiya, K.3    Nakamura, A.4    Iwamoto, T.5
  • 31
    • 58049214009 scopus 로고    scopus 로고
    • Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration
    • Sahara N, Maeda S, Takashima A. Tau oligomerization: a role for tau aggregation intermediates linked to neurodegeneration. Curr Alzheimer Res 2008; 5: 591-598.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 591-598
    • Sahara, N.1    Maeda, S.2    Takashima, A.3
  • 32
    • 0034682667 scopus 로고    scopus 로고
    • 14-3-3zeta is an effector of tau protein phosphorylation
    • Hashiguchi M, Sobue K, Paudel HK. 14-3-3zeta is an effector of tau protein phosphorylation. J Biol Chem 2000; 275: 25247-25254.
    • (2000) J Biol Chem , vol.275 , pp. 25247-25254
    • Hashiguchi, M.1    Sobue, K.2    Paudel, H.K.3
  • 33
    • 0037631324 scopus 로고    scopus 로고
    • 14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex
    • Agarwal-Mawal A, Qureshi HY, Cafferty PW etal. 14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex. J Biol Chem 2003; 278: 12722-12728.
    • (2003) J Biol Chem , vol.278 , pp. 12722-12728
    • Agarwal-Mawal, A.1    Qureshi, H.Y.2    Cafferty, P.W.3
  • 34
    • 2942755865 scopus 로고    scopus 로고
    • 14-3-3 binds to and mediates phosphorylation of microtubule-associated tau protein by Ser9-phosphorylated glycogen synthase kinase 3beta in the brain
    • Yuan Z, Agarwal-Mawal A, Paudel HK. 14-3-3 binds to and mediates phosphorylation of microtubule-associated tau protein by Ser9-phosphorylated glycogen synthase kinase 3beta in the brain. J Biol Chem 2004; 279: 26105-26114.
    • (2004) J Biol Chem , vol.279 , pp. 26105-26114
    • Yuan, Z.1    Agarwal-Mawal, A.2    Paudel, H.K.3
  • 35
    • 20644468811 scopus 로고    scopus 로고
    • 14-3-3Zeta does not increase GSK3beta-mediated tau phosphorylation in cell culture models
    • Matthews TA, Johnson GV. 14-3-3Zeta does not increase GSK3beta-mediated tau phosphorylation in cell culture models. Neurosci Lett 2005; 384: 211-216.
    • (2005) Neurosci Lett , vol.384 , pp. 211-216
    • Matthews, T.A.1    Johnson, G.V.2
  • 36
    • 0033944507 scopus 로고    scopus 로고
    • Tau-positive neurons in corticobasal degeneration and Alzheimer's disease - distinction by thiazin red and silver impregnations
    • Uchihara T, Nakamura A, Yamazaki M, Mori O. Tau-positive neurons in corticobasal degeneration and Alzheimer's disease - distinction by thiazin red and silver impregnations. Acta Neuropathol 2000; 100: 385-389.
    • (2000) Acta Neuropathol , vol.100 , pp. 385-389
    • Uchihara, T.1    Nakamura, A.2    Yamazaki, M.3    Mori, O.4
  • 37
    • 0034920989 scopus 로고    scopus 로고
    • Evolution from pretangle neurons to neurofibrillary tangles monitored by thiazin red combined with Gallyas method and double immunofluorescence
    • Uchihara T, Nakamura A, Yamazaki M, Mori O. Evolution from pretangle neurons to neurofibrillary tangles monitored by thiazin red combined with Gallyas method and double immunofluorescence. Acta Neuropathol 2001; 101: 535-539.
    • (2001) Acta Neuropathol , vol.101 , pp. 535-539
    • Uchihara, T.1    Nakamura, A.2    Yamazaki, M.3    Mori, O.4
  • 38
    • 0034769236 scopus 로고    scopus 로고
    • Different conformation of neuronal tau deposits distinguished by double immunofluorescence with AT8 and thiazin red combined with Gallyas method
    • Uchihara T, Nakamura A, Yamazaki M, Mori O, Ikeda K, Tsuchiya K. Different conformation of neuronal tau deposits distinguished by double immunofluorescence with AT8 and thiazin red combined with Gallyas method. Acta Neuropathol 2001; 102: 462-466.
    • (2001) Acta Neuropathol , vol.102 , pp. 462-466
    • Uchihara, T.1    Nakamura, A.2    Yamazaki, M.3    Mori, O.4    Ikeda, K.5    Tsuchiya, K.6
  • 39
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009; 284: 12845-12852.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 40
    • 57249108291 scopus 로고    scopus 로고
    • Phosphorylation of tau at Ser214 mediates its interaction with 14-3-3 protein: implications for the mechanism of tau aggregation
    • Sadik G, Tanaka T, Kato K etal. Phosphorylation of tau at Ser214 mediates its interaction with 14-3-3 protein: implications for the mechanism of tau aggregation. J Neurochem 2009; 108: 33-43.
    • (2009) J Neurochem , vol.108 , pp. 33-43
    • Sadik, G.1    Tanaka, T.2    Kato, K.3
  • 41
    • 64949087565 scopus 로고    scopus 로고
    • Differential interaction and aggregation of 3-repeat and 4-repeat tau isoforms with 14-3-3zeta protein
    • Sadik G, Tanaka T, Kato K, Yanagi K, Kudo T, Takeda M. Differential interaction and aggregation of 3-repeat and 4-repeat tau isoforms with 14-3-3zeta protein. Biochem Biophys Res Commun 2009; 383: 37-41.
    • (2009) Biochem Biophys Res Commun , vol.383 , pp. 37-41
    • Sadik, G.1    Tanaka, T.2    Kato, K.3    Yanagi, K.4    Kudo, T.5    Takeda, M.6
  • 42
    • 69249212121 scopus 로고    scopus 로고
    • Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta
    • Sluchanko NN, Seit-Nebi AS, Gusev NB. Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta. FEBS Lett 2009; 583: 2739-2742.
    • (2009) FEBS Lett , vol.583 , pp. 2739-2742
    • Sluchanko, N.N.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 43
    • 58949099193 scopus 로고    scopus 로고
    • Effect of phosphorylation on interaction of human tau protein with 14-3-3zeta
    • Sluchanko NN, Seit-Nebi AS, Gusev NB. Effect of phosphorylation on interaction of human tau protein with 14-3-3zeta. Biochem Biophys Res Commun 2009; 379: 990-994.
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 990-994
    • Sluchanko, N.N.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 45
    • 39149104664 scopus 로고    scopus 로고
    • Gene-gene interaction between 14-3-3 zeta and butyrylcholinesterase modulates Alzheimer's disease risk
    • Mateo I, Llorca J, Infante J, Rodriguez-Rodriguez E, Berciano J, Combarros O. Gene-gene interaction between 14-3-3 zeta and butyrylcholinesterase modulates Alzheimer's disease risk. Eur J Neurol 2008; 15: 219-222.
    • (2008) Eur J Neurol , vol.15 , pp. 219-222
    • Mateo, I.1    Llorca, J.2    Infante, J.3    Rodriguez-Rodriguez, E.4    Berciano, J.5    Combarros, O.6
  • 47
  • 48
    • 66049102942 scopus 로고    scopus 로고
    • Neuropathology of Pick body disease
    • Uchihara T, Tsuchiya K. Neuropathology of Pick body disease. Handb Clin Neurol 2008; 89: 415-430.
    • (2008) Handb Clin Neurol , vol.89 , pp. 415-430
    • Uchihara, T.1    Tsuchiya, K.2
  • 49
    • 0006164301 scopus 로고    scopus 로고
    • Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop
    • McKeith IG, Galasko D, Kosaka K etal. Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop. Neurology 1996; 47: 1113-1124.
    • (1996) Neurology , vol.47 , pp. 1113-1124
    • McKeith, I.G.1    Galasko, D.2    Kosaka, K.3
  • 50
    • 0021636665 scopus 로고
    • Diffuse type of Lewy body disease: progressive dementia with abundant cortical Lewy bodies and senile changes of varying degree - a new disease?
    • Kosaka K, Yoshimura M, Ikeda K, Budka H. Diffuse type of Lewy body disease: progressive dementia with abundant cortical Lewy bodies and senile changes of varying degree - a new disease? Clin Neuropathol 1984; 3: 185-192.
    • (1984) Clin Neuropathol , vol.3 , pp. 185-192
    • Kosaka, K.1    Yoshimura, M.2    Ikeda, K.3    Budka, H.4
  • 52
    • 0033565874 scopus 로고    scopus 로고
    • alpha-Synuclein shares physical and functional homology with 14-3-3 proteins
    • Ostrerova N, Petrucelli L, Farrer M etal. alpha-Synuclein shares physical and functional homology with 14-3-3 proteins. J Neurosci 1999; 19: 5782-5791.
    • (1999) J Neurosci , vol.19 , pp. 5782-5791
    • Ostrerova, N.1    Petrucelli, L.2    Farrer, M.3
  • 53
    • 0038462211 scopus 로고    scopus 로고
    • Specification of 14-3-3 proteins in Lewy bodies
    • Berg D, Riess O, Bornemann A. Specification of 14-3-3 proteins in Lewy bodies. Ann Neurol 2003; 54: 135.
    • (2003) Ann Neurol , vol.54 , pp. 135
    • Berg, D.1    Riess, O.2    Bornemann, A.3
  • 54
    • 33750335666 scopus 로고    scopus 로고
    • Ihara M. alpha-Synuclein is colocalized with 14-3-3 and synphilin-1 in A53T transgenic mice
    • Shirakashi Y, Kawamoto Y, Tomimoto H, Takahashi R. Ihara M. alpha-Synuclein is colocalized with 14-3-3 and synphilin-1 in A53T transgenic mice. Acta Neuropathol 2006; 112: 681-689.
    • (2006) Acta Neuropathol , vol.112 , pp. 681-689
    • Shirakashi, Y.1    Kawamoto, Y.2    Tomimoto, H.3    Takahashi, R.4
  • 55
    • 77952216305 scopus 로고    scopus 로고
    • Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson's disease
    • Yacoubian TA, Slone SR, Harrington AJ etal. Differential neuroprotective effects of 14-3-3 proteins in models of Parkinson's disease. Cell Death Dis 2010; 1: e2.
    • (2010) Cell Death Dis , vol.1
    • Yacoubian, T.A.1    Slone, S.R.2    Harrington, A.J.3
  • 56
    • 30444448687 scopus 로고    scopus 로고
    • 14-3-3eta is a novel regulator of parkin ubiquitin ligase
    • Sato S, Chiba T, Sakata E etal. 14-3-3eta is a novel regulator of parkin ubiquitin ligase. EMBO J 2006; 25: 211-221.
    • (2006) EMBO J , vol.25 , pp. 211-221
    • Sato, S.1    Chiba, T.2    Sakata, E.3
  • 57
    • 58149161719 scopus 로고    scopus 로고
    • Late onset Huntington Disease: clinical and genetic characteristics of 34 cases
    • Lipe H, Bird T. Late onset Huntington Disease: clinical and genetic characteristics of 34 cases. J Neurol Sci 2009; 276: 159-162.
    • (2009) J Neurol Sci , vol.276 , pp. 159-162
    • Lipe, H.1    Bird, T.2
  • 58
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter S, Boeddrich A, Lurz R etal. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol Biol Cell 2001; 12: 1393-1407.
    • (2001) Mol Biol Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3
  • 59
    • 38049080224 scopus 로고    scopus 로고
    • 14-3-3zeta is indispensable for aggregate formation of polyglutamine-expanded huntingtin protein
    • Omi K, Hachiya NS, Tanaka M, Tokunaga K, Kaneko K. 14-3-3zeta is indispensable for aggregate formation of polyglutamine-expanded huntingtin protein. Neurosci Lett 2008; 431: 45-50.
    • (2008) Neurosci Lett , vol.431 , pp. 45-50
    • Omi, K.1    Hachiya, N.S.2    Tanaka, M.3    Tokunaga, K.4    Kaneko, K.5
  • 60
    • 59649096550 scopus 로고    scopus 로고
    • Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery
    • Wang Y, Meriin AB, Zaarur N etal. Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 2009; 23: 451-463.
    • (2009) FASEB J , vol.23 , pp. 451-463
    • Wang, Y.1    Meriin, A.B.2    Zaarur, N.3
  • 61
    • 36949002758 scopus 로고    scopus 로고
    • Research into neurodegenerative disease: an entangled web of mice and men
    • Uchihara T, Paulus W. Research into neurodegenerative disease: an entangled web of mice and men. Acta Neuropathol 2008; 115: 1-4.
    • (2008) Acta Neuropathol , vol.115 , pp. 1-4
    • Uchihara, T.1    Paulus, W.2
  • 62
    • 0029840653 scopus 로고    scopus 로고
    • The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies
    • Hsich G, Kenney K, Gibbs CJ, Lee KH, Harrington MG. The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies. N Engl J Med 1996; 335: 924-930.
    • (1996) N Engl J Med , vol.335 , pp. 924-930
    • Hsich, G.1    Kenney, K.2    Gibbs, C.J.3    Lee, K.H.4    Harrington, M.G.5
  • 63
    • 0034649443 scopus 로고    scopus 로고
    • Misleading results with the 14-3-3 assay for the diagnosis of Creutzfeldt-Jakob disease
    • Chapman T, McKeel DW Jr, Morris JC. Misleading results with the 14-3-3 assay for the diagnosis of Creutzfeldt-Jakob disease. Neurology 2000; 55: 1396-1397.
    • (2000) Neurology , vol.55 , pp. 1396-1397
    • Chapman, T.1    McKeel Jr, D.W.2    Morris, J.C.3
  • 64
    • 0038790332 scopus 로고    scopus 로고
    • Immunohistochemical localization of 14.3.3 zeta protein in amyloid plaques in human spongiform encephalopathies
    • Richard M, Biacabe AG, Streichenberger N etal. Immunohistochemical localization of 14.3.3 zeta protein in amyloid plaques in human spongiform encephalopathies. Acta Neuropathol 2003; 105: 296-302.
    • (2003) Acta Neuropathol , vol.105 , pp. 296-302
    • Richard, M.1    Biacabe, A.G.2    Streichenberger, N.3
  • 65
    • 33846811283 scopus 로고    scopus 로고
    • The epsilon isoform of 14-3-3 protein is a component of the prion protein amyloid deposits of Gerstmann-Straussler-Scheinker disease
    • Di Fede G, Giaccone G, Limido L etal. The epsilon isoform of 14-3-3 protein is a component of the prion protein amyloid deposits of Gerstmann-Straussler-Scheinker disease. J Neuropathol Exp Neurol 2007; 66: 124-130.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 124-130
    • Di Fede, G.1    Giaccone, G.2    Limido, L.3
  • 66
    • 26444462510 scopus 로고    scopus 로고
    • The 14-3-3 protein forms a molecular complex with heat shock protein Hsp60 and cellular prion protein
    • Satoh J, Onoue H, Arima K, Yamamura T. The 14-3-3 protein forms a molecular complex with heat shock protein Hsp60 and cellular prion protein. J Neuropathol Exp Neurol 2005; 64: 858-868.
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 858-868
    • Satoh, J.1    Onoue, H.2    Arima, K.3    Yamamura, T.4
  • 67
    • 0032125107 scopus 로고    scopus 로고
    • Ischemic rat brains contain immunoreactivity of 14-3-3 proteins
    • Pirim I. Ischemic rat brains contain immunoreactivity of 14-3-3 proteins. Int J Neurosci 1998; 95: 101-106.
    • (1998) Int J Neurosci , vol.95 , pp. 101-106
    • Pirim, I.1
  • 68
    • 0037335444 scopus 로고    scopus 로고
    • Overexpression of copper/zinc superoxide dismutase in transgenic mice protects against neuronal cell death after transient focal ischemia by blocking activation of the Bad cell death signaling pathway
    • Saito A, Hayashi T, Okuno S, Ferrand-Drake M, Chan PH. Overexpression of copper/zinc superoxide dismutase in transgenic mice protects against neuronal cell death after transient focal ischemia by blocking activation of the Bad cell death signaling pathway. J Neurosci 2003; 23: 1710-1718.
    • (2003) J Neurosci , vol.23 , pp. 1710-1718
    • Saito, A.1    Hayashi, T.2    Okuno, S.3    Ferrand-Drake, M.4    Chan, P.H.5
  • 69
    • 1242274413 scopus 로고    scopus 로고
    • Neuroprotective role of a proline-rich Akt substrate in apoptotic neuronal cell death after stroke: relationships with nerve growth factor
    • Saito A, Narasimhan P, Hayashi T, Okuno S, Ferrand-Drake M, Chan PH. Neuroprotective role of a proline-rich Akt substrate in apoptotic neuronal cell death after stroke: relationships with nerve growth factor. J Neurosci 2004; 24: 1584-1593.
    • (2004) J Neurosci , vol.24 , pp. 1584-1593
    • Saito, A.1    Narasimhan, P.2    Hayashi, T.3    Okuno, S.4    Ferrand-Drake, M.5    Chan, P.H.6
  • 70
    • 47249087218 scopus 로고    scopus 로고
    • Ischemic preconditioning suppresses apoptosis of rabbit spinal neurocytes by inhibiting ASK1-14-3-3 dissociation
    • Yang C, Ren Y, Liu F etal. Ischemic preconditioning suppresses apoptosis of rabbit spinal neurocytes by inhibiting ASK1-14-3-3 dissociation. Neurosci Lett 2008; 441: 267-271.
    • (2008) Neurosci Lett , vol.441 , pp. 267-271
    • Yang, C.1    Ren, Y.2    Liu, F.3
  • 71
    • 62649096776 scopus 로고    scopus 로고
    • Ligand-activated peroxisome proliferator-activated receptor-gamma protects against ischemic cerebral infarction and neuronal apoptosis by 14-3-3 epsilon upregulation
    • Wu JS, Cheung WM, Tsai YS etal. Ligand-activated peroxisome proliferator-activated receptor-gamma protects against ischemic cerebral infarction and neuronal apoptosis by 14-3-3 epsilon upregulation. Circulation 2009; 119: 1124-1134.
    • (2009) Circulation , vol.119 , pp. 1124-1134
    • Wu, J.S.1    Cheung, W.M.2    Tsai, Y.S.3
  • 72
    • 77957960820 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors protect against apoptosis via 14-3-3
    • Wu KK. Peroxisome proliferator-activated receptors protect against apoptosis via 14-3-3. PPAR Res 2010; 2010: 1-7.
    • (2010) PPAR Res , vol.2010 , pp. 1-7
    • Wu, K.K.1
  • 73
    • 0038119829 scopus 로고    scopus 로고
    • 14-3-3gamma is upregulated by in vitro ischemia and binds to protein kinase Raf in primary cultures of astrocytes
    • Chen XQ, Chen JG, Zhang Y, Hsiao WW, Yu AC. 14-3-3gamma is upregulated by in vitro ischemia and binds to protein kinase Raf in primary cultures of astrocytes. Glia 2003; 42: 315-324.
    • (2003) Glia , vol.42 , pp. 315-324
    • Chen, X.Q.1    Chen, J.G.2    Zhang, Y.3    Hsiao, W.W.4    Yu, A.C.5
  • 74
    • 14644391542 scopus 로고    scopus 로고
    • Association of 14-3-3gamma and phosphorylated bad attenuates injury in ischemic astrocytes
    • Chen XQ, Fung YW, Yu AC. Association of 14-3-3gamma and phosphorylated bad attenuates injury in ischemic astrocytes. J Cereb Blood Flow Metab 2005; 25: 338-347.
    • (2005) J Cereb Blood Flow Metab , vol.25 , pp. 338-347
    • Chen, X.Q.1    Fung, Y.W.2    Yu, A.C.3
  • 75
    • 1542328881 scopus 로고    scopus 로고
    • Inducible expression of the signal transduction protein 14-3-3gamma in injured arteries and stimulated human vascular smooth muscle cells
    • Autieri MV. Inducible expression of the signal transduction protein 14-3-3gamma in injured arteries and stimulated human vascular smooth muscle cells. Exp Mol Pathol 2004; 76: 99-107.
    • (2004) Exp Mol Pathol , vol.76 , pp. 99-107
    • Autieri, M.V.1
  • 76
    • 0029861449 scopus 로고    scopus 로고
    • Expression of 14-3-3 gamma in injured arteries and growth factor- and cytokine-stimulated human vascular smooth muscle cells
    • Autieri MV, Haines DS, Romanic AM, Ohlstein EH. Expression of 14-3-3 gamma in injured arteries and growth factor- and cytokine-stimulated human vascular smooth muscle cells. Cell Growth Differ 1996; 7: 1453-1460.
    • (1996) Cell Growth Differ , vol.7 , pp. 1453-1460
    • Autieri, M.V.1    Haines, D.S.2    Romanic, A.M.3    Ohlstein, E.H.4
  • 77
    • 36348952677 scopus 로고    scopus 로고
    • Organellar proteomics of human platelet dense granules reveals that 14-3-3zeta is a granule protein related to atherosclerosis
    • Hernandez-Ruiz L, Valverde F, Jimenez-Nunez MD etal. Organellar proteomics of human platelet dense granules reveals that 14-3-3zeta is a granule protein related to atherosclerosis. J Proteome Res 2007; 6: 4449-4457.
    • (2007) J Proteome Res , vol.6 , pp. 4449-4457
    • Hernandez-Ruiz, L.1    Valverde, F.2    Jimenez-Nunez, M.D.3
  • 78
    • 33947715721 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-delta upregulates 14-3-3 epsilon in human endothelial cells via CCAAT/enhancer binding protein-beta
    • Brunelli L, Cieslik KA, Alcorn JL, Vatta M, Baldini A. Peroxisome proliferator-activated receptor-delta upregulates 14-3-3 epsilon in human endothelial cells via CCAAT/enhancer binding protein-beta. Circ Res 2007; 100: e59-e71.
    • (2007) Circ Res , vol.100
    • Brunelli, L.1    Cieslik, K.A.2    Alcorn, J.L.3    Vatta, M.4    Baldini, A.5
  • 79
    • 84860311573 scopus 로고    scopus 로고
    • Isoform-specific immunolocalization of 14-3-3 proteins in atherosclerotic lesions of human carotid and main cerebral arteries
    • in press].
    • Umahara T, Uchihara T, Koyama S etal. Isoform-specific immunolocalization of 14-3-3 proteins in atherosclerotic lesions of human carotid and main cerebral arteries. J Neurol Sci 2012; [in press].
    • (2012) J Neurol Sci
    • Umahara, T.1    Uchihara, T.2    Koyama, S.3
  • 80
    • 33745968479 scopus 로고    scopus 로고
    • Protection of endothelial survival by peroxisome proliferator-activated receptor-delta mediated 14-3-3 upregulation
    • Liou JY, Lee S, Ghelani D, Matijevic-Aleksic N, Wu KK. Protection of endothelial survival by peroxisome proliferator-activated receptor-delta mediated 14-3-3 upregulation. Arterioscler Thromb Vasc Biol 2006; 26: 1481-1487.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 1481-1487
    • Liou, J.Y.1    Lee, S.2    Ghelani, D.3    Matijevic-Aleksic, N.4    Wu, K.K.5
  • 81
    • 0035064951 scopus 로고    scopus 로고
    • Laminar flow inhibits TNF-induced ASK1 activation by preventing dissociation of ASK1 from its inhibitor 14-3-3
    • Liu Y, Yin G, Surapisitchat J, Berk BC, Min W. Laminar flow inhibits TNF-induced ASK1 activation by preventing dissociation of ASK1 from its inhibitor 14-3-3. J Clin Invest 2001; 107: 917-923.
    • (2001) J Clin Invest , vol.107 , pp. 917-923
    • Liu, Y.1    Yin, G.2    Surapisitchat, J.3    Berk, B.C.4    Min, W.5
  • 82
    • 0041743148 scopus 로고    scopus 로고
    • AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3
    • Zhang R, He X, Liu W, Lu M, Hsieh JT, Min W. AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3. J Clin Invest 2003; 111: 1933-1943.
    • (2003) J Clin Invest , vol.111 , pp. 1933-1943
    • Zhang, R.1    He, X.2    Liu, W.3    Lu, M.4    Hsieh, J.T.5    Min, W.6
  • 83
    • 0013784893 scopus 로고
    • Autoradiographic and histological evidence of postnatal hippocampal neurogenesis in rats
    • Altman J, Das GD. Autoradiographic and histological evidence of postnatal hippocampal neurogenesis in rats. J Comp Neurol 1965; 124: 319-335.
    • (1965) J Comp Neurol , vol.124 , pp. 319-335
    • Altman, J.1    Das, G.D.2
  • 84
    • 0026340585 scopus 로고
    • The persistent expression of a highly polysialylated NCAM in the dentate gyrus of the adult rat
    • Seki T, Arai Y. The persistent expression of a highly polysialylated NCAM in the dentate gyrus of the adult rat. Neurosci Res 1991; 12: 503-513.
    • (1991) Neurosci Res , vol.12 , pp. 503-513
    • Seki, T.1    Arai, Y.2
  • 86
    • 77951498581 scopus 로고    scopus 로고
    • New neurons and new memories: how does adult hippocampal neurogenesis affect learning and memory?
    • Deng W, Aimone JB, Gage FH. New neurons and new memories: how does adult hippocampal neurogenesis affect learning and memory? Nat Rev Neurosci 2010; 11: 339-350.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 339-350
    • Deng, W.1    Aimone, J.B.2    Gage, F.H.3
  • 87
    • 0023724031 scopus 로고
    • Spatial and temporal patterns of oligodendrocyte differentiation in rat cerebrum and cerebellum
    • LeVine SM, Goldman JE. Spatial and temporal patterns of oligodendrocyte differentiation in rat cerebrum and cerebellum. J Comp Neurol 1988; 277: 441-455.
    • (1988) J Comp Neurol , vol.277 , pp. 441-455
    • LeVine, S.M.1    Goldman, J.E.2
  • 88
    • 0028335641 scopus 로고
    • Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14-3-3 protein and differential distributions of their mRNAs in the brain
    • Watanabe M, Isobe T, Ichimura T etal. Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14-3-3 protein and differential distributions of their mRNAs in the brain. Brain Res Mol Brain Res 1994; 25: 113-121.
    • (1994) Brain Res Mol Brain Res , vol.25 , pp. 113-121
    • Watanabe, M.1    Isobe, T.2    Ichimura, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.