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Volumn 47, Issue 3, 2013, Pages 1081-1092

Assessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy

Author keywords

Alpha synuclein; Intracellular dynamics; Parkinson's disease; Photoactivation

Indexed keywords

ALPHA SYNUCLEIN; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 70; G PROTEIN COUPLED RECEPTOR KINASE 5; PHOSPHOSERINE;

EID: 84887273441     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-013-8406-x     Document Type: Article
Times cited : (71)

References (53)
  • 2
    • 34247139885 scopus 로고    scopus 로고
    • Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation
    • Schneider BL, Seehus CR, Capowski E.E., Aebischer P., Zhang SC, Svendsen C.N. (2007) Over-expression of alpha-synuclein in human neural progenitors leads to specific changes in fate and differentiation. Hum Mol Genet 16(6):651-666
    • (2007) Hum Mol Genet , vol.16 , Issue.6 , pp. 651-666
    • Schneider, B.L.1    Seehus, C.R.2    Capowski, E.E.3    Aebischer, P.4    Zhang, S.C.5    Svendsen, C.N.6
  • 3
    • 42949133399 scopus 로고    scopus 로고
    • Alpha-synuclein alters notch-1 expression and neurogenesis in mouse embryonic stem cells and in the hippocampus of transgenic mice
    • doi:10.1523/JNEUROSCI.0066-08.2008
    • Crews L, Mizuno H, Desplats P., Rockenstein E, Adame A, Patrick C., Winner B, Winkler J, Masliah E (2008) Alpha-synuclein alters Notch-1 expression and neurogenesis in mouse embryonic stem cells and in the hippocampus of transgenic mice. J Neurosci 28(16):4250-4260. doi:10.1523/JNEUROSCI.0066-08.2008
    • (2008) J Neurosci , vol.28 , Issue.16 , pp. 4250-4260
    • Crews, L.1    Mizuno, H.2    Desplats, P.3    Rockenstein, E.4    Adame, A.5    Patrick, C.6    Winner, B.7    Winkler, J.8    Masliah, E.9
  • 4
    • 33750117120 scopus 로고    scopus 로고
    • Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging
    • doi:10.1096/fj.05-5422com
    • Klucken J, Outeiro TF, Nguyen P, McLean P.J., Hyman B.T. (2006) Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging. FASEB J 20(12):2050-2057. doi:10.1096/fj.05-5422com
    • (2006) FASEB J , vol.20 , Issue.12 , pp. 2050-2057
    • Klucken, J.1    Outeiro, T.F.2    Nguyen, P.3    McLean, P.J.4    Hyman, B.T.5
  • 5
    • 3342951965 scopus 로고    scopus 로고
    • Lipid rafts mediate the synaptic localization of alpha-synuclein
    • doi:10.1523/JNEUROSCI.1594-04.2004
    • Fortin DL, Troyer MD, Nakamura K, Kubo S., Anthony MD, Edwards R.H. (2004) Lipid rafts mediate the synaptic localization of alpha-synuclein. J Neurosci 24(30):6715-6723. doi:10.1523/JNEUROSCI.1594-04.2004
    • (2004) J Neurosci , vol.24 , Issue.30 , pp. 6715-6723
    • Fortin, D.L.1    Troyer, M.D.2    Nakamura, K.3    Kubo, S.4    Anthony, M.D.5    Edwards, R.H.6
  • 6
    • 79551540871 scopus 로고    scopus 로고
    • Different sub-cellular localization of alpha-synuclein in the C57BL \6J mouse's central nervous system by two novel monoclonal antibodies
    • doi:10.1016/j.jchemneu.2010.12.003
    • Vivacqua G, Casini A, Vaccaro R., Fornai F, Yu S, D'Este L (2011) Different sub-cellular localization of alpha-synuclein in the C57BL \6J mouse's central nervous system by two novel monoclonal antibodies. J Chem Neuroanat 41(2):97-110. doi:10.1016/j.jchemneu.2010.12.003
    • (2011) J Chem Neuroanat , vol.41 , Issue.2 , pp. 97-110
    • Vivacqua, G.1    Casini, A.2    Vaccaro, R.3    Fornai, F.4    Yu, S.5    D'Este, L.6
  • 8
    • 77956289142 scopus 로고    scopus 로고
    • In vivo imaging of alpha-synuclein in mouse cortex demonstrates stable expression and differential subcellular compartment mobility
    • doi:10.1371/journal.pone.0010589
    • Unni VK, Weissman TA, Rockenstein E, Masliah E., McLean PJ, Hyman B.T. (2010) In vivo imaging of alpha-synuclein in mouse cortex demonstrates stable expression and differential subcellular compartment mobility. PLoS One 5(5):e10589. doi:10.1371/journal.pone.0010589
    • (2010) PLoS One , vol.5 , Issue.5
    • Unni, V.K.1    Weissman, T.A.2    Rockenstein, E.3    Masliah, E.4    McLean, P.J.5    Hyman, B.T.6
  • 13
    • 30044450420 scopus 로고    scopus 로고
    • Comparison of structure and dynamics of micelle-bound human alpha-synuclein and parkinson disease variants
    • doi:10.1074/jbc.M507624200
    • Ulmer TS, Bax A. (2005) Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants. J Biol Chem 280(52):43179-43187. doi:10.1074/jbc.M507624200
    • (2005) J Biol Chem , vol.280 , Issue.52 , pp. 43179-43187
    • Ulmer, T.S.1    Bax, A.2
  • 14
    • 75749093356 scopus 로고    scopus 로고
    • Differential phospholipid binding of alpha-synuclein variants implicated in parkinson's disease revealed by solution NMR spectroscopy
    • doi:10.1021/bi901723p
    • Bodner CR, Maltsev AS, Dobson C.M., Bax A. (2010) Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy. Biochemistry 49(5):862-871. doi:10.1021/bi901723p
    • (2010) Biochemistry , vol.49 , Issue.5 , pp. 862-871
    • Bodner, C.R.1    Maltsev, A.S.2    Dobson, C.M.3    Bax, A.4
  • 17
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G protein-coupled receptor kinases
    • Pronin AN, Morris AJ, Surguchov A, Benovic J.L. (2000) Synucleins are a novel class of substrates for G protein-coupled receptor kinases. J Biol Chem 275(34):26515-26522
    • (2000) J Biol Chem , vol.275 , Issue.34 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 20
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a drosophila model for parkinson's disease
    • doi:10.1126/science.1067389
    • Auluck PK, Chan HY, Trojanowski J.Q., Lee VM, Bonini N.M. (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295 (5556):865-868. doi:10.1126/science.1067389
    • (2002) Science , vol.295 , Issue.5556 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 21
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of parkinson's disease
    • doi:10.1016/j.jmb.2005.06.060
    • Flower TR, Chesnokova LS, Froelich C.A., Dixon C., Witt S.N. (2005) Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease. J Mol Biol 351(5):1081-1100. doi:10.1016/j.jmb.2005.06.060
    • (2005) J Mol Biol , vol.351 , Issue.5 , pp. 1081-1100
    • Flower, T.R.1    Chesnokova, L.S.2    Froelich, C.A.3    Dixon, C.4    Witt, S.N.5
  • 22
    • 2942620074 scopus 로고    scopus 로고
    • Hsp70 reduces alpha-synuclein aggregation and toxicity
    • doi:10.1074/jbc.M400255200
    • Klucken J, Shin Y, Masliah E., Hyman BT, McLean P.J. (2004) Hsp70 reduces alpha-synuclein aggregation and toxicity. J Biol Chem 279(24):25497-25502. doi:10.1074/jbc.M400255200
    • (2004) J Biol Chem , vol.279 , Issue.24 , pp. 25497-25502
    • Klucken, J.1    Shin, Y.2    Masliah, E.3    Hyman, B.T.4    McLean, P.J.5
  • 23
    • 17644383748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species
    • doi:10.1074/jbc.M413024200
    • Dedmon MM, Christodoulou J, Wilson M.R., Dobson C.M. (2005) Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species. J Biol Chem 280(15):14733-14740. doi:10.1074/jbc. M413024200
    • (2005) J Biol Chem , vol.280 , Issue.15 , pp. 14733-14740
    • Dedmon, M.M.1    Christodoulou, J.2    Wilson, M.R.3    Dobson, C.M.4
  • 24
    • 84859595997 scopus 로고    scopus 로고
    • A simple photoactivation and image analysis module for visualizing and analyzing axonal transport with high temporal resolution
    • doi:10.1038/nprot.2011.428
    • Roy S, Yang G, Tang Y., Scott D.A. (2012) A simple photoactivation and image analysis module for visualizing and analyzing axonal transport with high temporal resolution. Nat Protoc 7(1):62-68. doi:10.1038/nprot.2011.428
    • (2012) Nat Protoc , vol.7 , Issue.1 , pp. 62-68
    • Roy, S.1    Yang, G.2    Tang, Y.3    Scott, D.A.4
  • 25
    • 0042338695 scopus 로고    scopus 로고
    • Photobleaching and photoactivation: Following protein dynamics in living cells
    • Lippincott-Schwartz J., Altan-Bonnet N, Patterson G.H. (2003) Photobleaching and photoactivation: following protein dynamics in living cells. Nat Cell Biol Suppl: S7-14
    • (2003) Nat Cell Biol , Issue.SUPPL.
    • Lippincott-Schwartz, J.1    Altan-Bonnet, N.2    Patterson, G.H.3
  • 26
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson GH, Lippincott-Schwartz J (2002) A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297 (5588):1873-1877
    • (2002) Science , vol.297 , Issue.5588 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 27
    • 65549107985 scopus 로고    scopus 로고
    • The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast
    • doi:10.1016/j.jmb.2009.03.021
    • Vamvaca K, Volles MJ, Lansbury PT Jr (2009) The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast. J Mol Biol 389(2):413-424. doi:10.1016/j.jmb.2009.03.021
    • (2009) J Mol Biol , vol.389 , Issue.2 , pp. 413-424
    • Vamvaca, K.1    Volles, M.J.2    Lansbury Jr., P.T.3
  • 28
    • 77749239814 scopus 로고    scopus 로고
    • Dynamic transport and localization of alpha-synuclein in primary hippocampal neurons
    • doi:10.1186/1750-1326-5-9
    • Yang ML, Hasadsri L, Woods W.S., George J.M. (2010) Dynamic transport and localization of alpha-synuclein in primary hippocampal neurons. Mol Neurodegener 5(1):9. doi:10.1186/1750-1326-5-9
    • (2010) Mol Neurodegener , vol.5 , Issue.1 , pp. 9
    • Yang, M.L.1    Hasadsri, L.2    Woods, W.S.3    George, J.M.4
  • 29
    • 13444254033 scopus 로고    scopus 로고
    • Subcellular localisation of recombinant alpha-and gamma-synuclein
    • doi:10.1016/j.mcn.2004.09.017
    • Specht CG, Tigaret CM, Rast G.F., Thalhammer A., Rudhard Y, Schoepfer R. (2005) Subcellular localisation of recombinant alpha-and gamma-synuclein. Mol Cell Neurosci 28(2):326-334. doi:10.1016/j.mcn.2004.09.017
    • (2005) Mol Cell Neurosci , vol.28 , Issue.2 , pp. 326-334
    • Specht, C.G.1    Tigaret, C.M.2    Rast, G.F.3    Thalhammer, A.4    Rudhard, Y.5    Schoepfer, R.6
  • 30
    • 33749583553 scopus 로고    scopus 로고
    • Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotox-icity
    • Kontopoulos E, Parvin JD, Feany M.B. (2006) Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotox-icity. Hum Mol Genet 15(20):3012-3023
    • (2006) Hum Mol Genet , vol.15 , Issue.20 , pp. 3012-3023
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 31
    • 84865045728 scopus 로고    scopus 로고
    • Selective binding of nuclear alpha-synuclein to the PGC1alpha promoter under conditions of oxidative stress may contribute to losses in mitochondrial function: Implications for parkinson's disease
    • doi:10.1016/j.freeradbiomed.2012.05.024
    • Siddiqui A, Chinta SJ, Mallajosyula J.K., Rajagopolan S., Hanson I, Rane A, Andersen J.K. (2012) Selective binding of nuclear alpha-synuclein to the PGC1alpha promoter under conditions of oxidative stress may contribute to losses in mitochondrial function: implications for Parkinson's disease. Free Radic Biol Med. doi:10.1016/j.freeradbiomed.2012.05.024
    • (2012) Free Radic Biol Med.
    • Siddiqui, A.1    Chinta, S.J.2    Mallajosyula, J.K.3    Rajagopolan, S.4    Hanson, I.5    Rane, A.6    Andersen, J.K.7
  • 32
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in alzheimer's disease and learning, is natively unfolded
    • doi:10.1021/bi961799n
    • Weinreb PH, Zhen W, Poon A.W., Conway KA, Lansbury PT Jr (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35(43):13709-13715. doi:10.1021/bi961799n
    • (1996) Biochemistry , vol.35 , Issue.43 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5
  • 33
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • doi:10.1038/nature10324
    • Bartels T, Choi JG, Selkoe D.J. (2011) Alpha-synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477(7362):107-110. doi:10.1038/nature10324
    • (2011) Nature , vol.477 , Issue.7362 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 35
    • 0037930855 scopus 로고    scopus 로고
    • Lipid binding inhibits alpha-synuclein fibril formation
    • doi:10.1074/jbc.M210136200
    • Zhu M, Fink A.L. (2003) Lipid binding inhibits alpha-synuclein fibril formation. J Biol Chem 278(19):16873-16877. doi:10.1074/jbc.M210136200
    • (2003) J Biol Chem , vol.278 , Issue.19 , pp. 16873-16877
    • Zhu, M.1    Fink, A.L.2
  • 36
    • 0038341134 scopus 로고    scopus 로고
    • A broken alpha-helix in folded alpha-synuclein
    • doi:10.1074/jbc.M213128200
    • Chandra S, Chen X, Rizo J., Jahn R, Sudhof T.C. (2003) A broken alpha-helix in folded alpha-synuclein. J Biol Chem 278(17):15313-15318. doi:10.1074/jbc.M213128200
    • (2003) J Biol Chem , vol.278 , Issue.17 , pp. 15313-15318
    • Chandra, S.1    Chen, X.2    Rizo, J.3    Jahn, R.4    Sudhof, T.C.5
  • 37
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-synuclein and parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis
    • doi:10.1074/jbc.M004851200
    • Perrin RJ, Woods WS, Clayton D.F., George J.M. (2000) Interaction of human alpha-synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J Biol Chem 275(44):34393-34398. doi:10.1074/jbc.M004851200
    • (2000) J Biol Chem , vol.275 , Issue.44 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 38
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • doi:10.1074/jbc.M411805200
    • Ulmer TS, Bax A, Cole N.B., Nussbaum R.L. (2005) Structure and dynamics of micelle-bound human alpha-synuclein. J Biol Chem 280(10):9595-9603. doi:10.1074/jbc.M411805200
    • (2005) J Biol Chem , vol.280 , Issue.10 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 39
    • 69949092913 scopus 로고    scopus 로고
    • {alpha}-synuclein and its A30P mutant affect actin cytoskeletal structure and dynamics
    • doi:10.1091/mbc.E08-03-0302
    • Sousa VL, Bellani S, Giannandrea M., Yousuf M, Valtorta F, Meldolesi J., Chieregatti E. (2009) {alpha}-synuclein and its A30P mutant affect actin cytoskeletal structure and dynamics. Mol Biol Cell 20(16):3725-3739. doi:10.1091/mbc.E08-03-0302
    • (2009) Mol Biol Cell , vol.20 , Issue.16 , pp. 3725-3739
    • Sousa, V.L.1    Bellani, S.2    Giannandrea, M.3    Yousuf, M.4    Valtorta, F.5    Meldolesi, J.6    Chieregatti, E.7
  • 40
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel HA, Petre BM, Wall J, Simon M., Nowak RJ, Walz T, Lansbury PT Jr (2002) Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 322(5):1089-1102
    • (2002) J Mol Biol , vol.322 , Issue.5 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury Jr., P.T.7
  • 41
    • 84856667162 scopus 로고    scopus 로고
    • Mimicking phosphorylation at serine 87 inhibits the aggregation of human alpha-synuclein and protects against its toxicity in a rat model of parkinson's disease
    • doi:10.1523/JNEUROSCI.3784-11.2012
    • Oueslati A, Paleologou KE, Schneider B.L., Aebischer P., Lashuel H.A. (2012) Mimicking phosphorylation at serine 87 inhibits the aggregation of human alpha-synuclein and protects against its toxicity in a rat model of Parkinson's disease. J Neurosci 32(5):1536-1544. doi:10.1523/JNEUROSCI.3784-11.2012
    • (2012) J Neurosci , vol.32 , Issue.5 , pp. 1536-1544
    • Oueslati, A.1    Paleologou, K.E.2    Schneider, B.L.3    Aebischer, P.4    Lashuel, H.A.5
  • 42
    • 84863349141 scopus 로고    scopus 로고
    • Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: Alpha-synuclein phosphor-ylation at tyrosine 125
    • doi:10.1021/ja210866j
    • Hejjaoui M, Butterfield S, Fauvet B., Vercruysse F, Cui J, Dikiy I., Prudent M, Olschewski D, Zhang Y, Eliezer D, Lashuel HA (2012) Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: alpha-synuclein phosphor-ylation at tyrosine 125. J Am Chem Soc 134(11):5196-5210. doi:10.1021/ja210866j
    • (2012) J Am Chem Soc , vol.134 , Issue.11 , pp. 5196-5210
    • Hejjaoui, M.1    Butterfield, S.2    Fauvet, B.3    Vercruysse, F.4    Cui, J.5    Dikiy, I.6    Prudent, M.7    Olschewski, D.8    Zhang, Y.9    Eliezer, D.10    Lashuel, H.A.11
  • 44
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a drosophila model of parkinson disease
    • Chen L, Feany M.B. (2005) Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat Neurosci 8(5):657-663
    • (2005) Nat Neurosci , vol.8 , Issue.5 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 46
    • 80052722040 scopus 로고    scopus 로고
    • Contribution of alanine-76 and serine phosphorylation in alpha-synuclein membrane association and aggregation in yeasts
    • doi:10.4061/2011/392180
    • Fiske M, Valtierra S, Solvang K., Zorniak M, White M, Herrera S., Konnikova A, Brezinsky R, Debburman S (2011) Contribution of alanine-76 and serine phosphorylation in alpha-synuclein membrane association and aggregation in yeasts. Park Dis 2011: 392180. doi:10.4061/2011/392180
    • (2011) Park Dis , vol.2011 , pp. 392180
    • Fiske, M.1    Valtierra, S.2    Solvang, K.3    Zorniak, M.4    White, M.5    Herrera, S.6    Konnikova, A.7    Brezinsky, R.8    Debburman, S.9
  • 47
    • 75149142186 scopus 로고    scopus 로고
    • Hsp70 molecular chaperones and parkinson's disease
    • doi:10.1002/bip.21302
    • Witt SN (2010) Hsp70 molecular chaperones and Parkinson's disease. Biopolymers 93(3):218-228. doi:10.1002/bip.21302
    • (2010) Biopolymers , vol.93 , Issue.3 , pp. 218-228
    • Witt, S.N.1
  • 50
    • 9344230362 scopus 로고    scopus 로고
    • Alpha-synuclein structures from fluorescence energy-transfer kinetics: Implications for the role of the protein in parkinson's disease
    • Lee JC, Langen R, Hummel P.A., Gray HB, Winkler J.R. (2004) Alpha-synuclein structures from fluorescence energy-transfer kinetics: implications for the role of the protein in Parkinson's disease. Proc Natl Acad Sci U S A 101(47): 16466-16471
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.47 , pp. 16466-16471
    • Lee, J.C.1    Langen, R.2    Hummel, P.A.3    Gray, H.B.4    Winkler, J.R.5
  • 52
    • 0035859226 scopus 로고    scopus 로고
    • Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
    • McLean PJ, Kawamata H, Hyman B.T. (2001) Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons. Neuroscience 104(3):901-912
    • (2001) Neuroscience , vol.104 , Issue.3 , pp. 901-912
    • McLean, P.J.1    Kawamata, H.2    Hyman, B.T.3


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