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Volumn 31, Issue 6, 2009, Pages 676-686

An unstructured protein with destructive potential: TPPP/p25 in neurodegeneration

Author keywords

Inclusion; Microtubule; Neurodegeneration; Unstructured protein

Indexed keywords

BRAIN PROTEIN; PROTEIN P25; TUBULIN POLYMERIZATION PROMOTING PROTEIN; UNCLASSIFIED DRUG; NERVE PROTEIN; P25 PROTEIN, HUMAN;

EID: 67650175319     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.200900008     Document Type: Article
Times cited : (40)

References (70)
  • 1
    • 0029847843 scopus 로고    scopus 로고
    • Metabolic consequences of enzyme interactions
    • Ovádi, J. and Srere, P. A., Metabolic consequences of enzyme interactions. Cell Biochem Funct 1996. 14: 249-258.
    • (1996) Cell Biochem Funct , vol.14 , pp. 249-258
    • Ovádi, J.1    Srere, P.A.2
  • 2
    • 0842345408 scopus 로고    scopus 로고
    • On the origin of intracellular compartmentation and organized metabolic systems
    • Ovádi, J. and Saks, V., On the origin of intracellular compartmentation and organized metabolic systems. Mol Cell Biochem 2004. 256-257: 5-12.
    • (2004) Mol Cell Biochem , vol.256-257 , pp. 5-12
    • Ovádi, J.1    Saks, V.2
  • 3
    • 0037047003 scopus 로고    scopus 로고
    • Brain-specific p25 protein binds to tubulin and microtubule and induces aberrant microtuble assemblies at substoichiometreic concentration
    • Hlavanda, E., Kovács, J., Oláh, J., Orosz, F., Medzihradszky, K. F., et al. Brain-specific p25 protein binds to tubulin and microtubule and induces aberrant microtuble assemblies at substoichiometreic concentration. Biochemistry 2002. 41: 8657-8664.
    • (2002) Biochemistry , vol.41 , pp. 8657-8664
    • Hlavanda, E.1    Kovács, J.2    Oláh, J.3    Orosz, F.4    Medzihradszky, K.F.5
  • 4
    • 0025769484 scopus 로고
    • A novel brain-specific 25 kDa protein (p25) is phosphorylated by a Ser/Thr-Pro kinase (TPK II) from tau protein kinase fractions
    • Takahashi, M., Tomizawa, K., Ishiguro, K., Sato, K., Omori, A., et al. A novel brain-specific 25 kDa protein (p25) is phosphorylated by a Ser/Thr-Pro kinase (TPK II) from tau protein kinase fractions. FEBS Lett 1991. 289: 37-43.
    • (1991) FEBS Lett , vol.289 , pp. 37-43
    • Takahashi, M.1    Tomizawa, K.2    Ishiguro, K.3    Sato, K.4    Omori, A.5
  • 5
    • 0344702694 scopus 로고    scopus 로고
    • TPPP/p25 promotes tubulin assemblies and blocks mitotic spindle formation
    • Tirián, L., Hlavanda, E., Oláh, J., Horváth, I., Orosz, F., et al. TPPP/p25 promotes tubulin assemblies and blocks mitotic spindle formation. Proc Natl Acad Sci USA 2003. 100: 13976-13981.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13976-13981
    • Tirián, L.1    Hlavanda, E.2    Oláh, J.3    Horváth, I.4    Orosz, F.5
  • 6
    • 56149124896 scopus 로고    scopus 로고
    • The tubulin polymerization promoting protein, TPPP/p25
    • Ovádi, J., The tubulin polymerization promoting protein, TPPP/p25. IUBMB Life 2008. 60: 637-642.
    • (2008) IUBMB Life , vol.60 , pp. 637-642
    • Ovádi, J.1
  • 8
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N., Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002. 11: 739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 9
    • 10244264868 scopus 로고    scopus 로고
    • TPPP/p25: From unfolded protein to misfolding disease. Prediction and experiments
    • Orosz, F., Kovács, G. G., Lehotzky, A., Oláh, J., Vincze, O., et al. TPPP/p25: from unfolded protein to misfolding disease. Prediction and experiments. Biol Cell 2004. 96: 701-711.
    • (2004) Biol Cell , vol.96 , pp. 701-711
    • Orosz, F.1    Kovács, G.G.2    Lehotzky, A.3    Oláh, J.4    Vincze, O.5
  • 10
    • 33751243970 scopus 로고    scopus 로고
    • TPPP proteins: Members of a new family with distinct structures and functions
    • Vincze, O., Tokési, N., Oláh, J., Hlavanda, E., Zotter, Á., et al. TPPP proteins: members of a new family with distinct structures and functions. Biochemistry 2006. 45: 13818-13826.
    • (2006) Biochemistry , vol.45 , pp. 13818-13826
    • Vincze, O.1    Tokési, N.2    Oláh, J.3    Hlavanda, E.4    Zotter, A.5
  • 11
    • 5144231819 scopus 로고    scopus 로고
    • Natively unfolded tubulin polymerization promoting protein TPPP/p25 is a common marker of alpha-synucleinopathies
    • Kovács, G. G., László, L., Kovács, J., Jensen, P. H., Lindersson, E., et al. Natively unfolded tubulin polymerization promoting protein TPPP/p25 is a common marker of alpha-synucleinopathies. Neurobiol Dis 2004. 17: 155-162.
    • (2004) Neurobiol Dis , vol.17 , pp. 155-162
    • Kovács, G.G.1    László, L.2    Kovács, J.3    Jensen, P.H.4    Lindersson, E.5
  • 12
    • 22444431956 scopus 로고    scopus 로고
    • p25 alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry
    • Otzen, D. E., Lundvig, D. M. S., Wimmer, R., Nielsen, L. H., Pedersen, J. R., et al. p25 alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry. Protein Sci 2005. 14: 1396-1409.
    • (2005) Protein Sci , vol.14 , pp. 1396-1409
    • Otzen, D.E.1    Lundvig, D.M.S.2    Wimmer, R.3    Nielsen, L.H.4    Pedersen, J.R.5
  • 13
    • 47849089500 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder
    • Collins, M. O., Yu, L., Campuzano, I., Grant, S. G. and Choudhary, J. S., Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder. Mol Cell Proteomics 2008. 7: 1331-1348.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1331-1348
    • Collins, M.O.1    Yu, L.2    Campuzano, I.3    Grant, S.G.4    Choudhary, J.S.5
  • 14
    • 67650408870 scopus 로고    scopus 로고
    • Intrinsic disorder in proteins associated with neurodegenerative diseases
    • Ovádi, J. and Orosz, F. editors, Springer
    • Uversky, V. N., Intrinsic disorder in proteins associated with neurodegenerative diseases, In: Ovádi, J. and Orosz, F. editors. Protein folding and misfolding: neurodegenerative diseases, Springer, 2009. pp 21-75.
    • (2009) Protein folding and misfolding: Neurodegenerative diseases , pp. 21-75
    • Uversky, V.N.1
  • 19
    • 14044254894 scopus 로고    scopus 로고
    • Proteomic analysis of in vivo phosphorylated synaptic proteins
    • Collins, M. O., Yu, L., Coba, M. P., Husi, H., Campuzano, I., et al. Proteomic analysis of in vivo phosphorylated synaptic proteins. J Biol Chem 2005. 280: 5972-5982.
    • (2005) J Biol Chem , vol.280 , pp. 5972-5982
    • Collins, M.O.1    Yu, L.2    Coba, M.P.3    Husi, H.4    Campuzano, I.5
  • 20
  • 22
    • 51649129138 scopus 로고    scopus 로고
    • Identification of multiple post-translational modifications in the porcine brain specific p25alpha
    • Kleinnijenhuis, A. J., Hedegaard, C., Lundvig, D., Sundbye, S., Issinger, O. G., et al. Identification of multiple post-translational modifications in the porcine brain specific p25alpha. J Neurochem 2008. 106: 925-933.
    • (2008) J Neurochem , vol.106 , pp. 925-933
    • Kleinnijenhuis, A.J.1    Hedegaard, C.2    Lundvig, D.3    Sundbye, S.4    Issinger, O.G.5
  • 23
    • 33646900710 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller, K., Trinidad, J. C., Chalkley, R. J., Specht, C. G., Thalhammer, A., et al. O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Mol Cell Proteomics 2006. 5: 923-934.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1    Trinidad, J.C.2    Chalkley, R.J.3    Specht, C.G.4    Thalhammer, A.5
  • 24
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • Lee, G., Neve, R. L. and Kosik, K. S., The microtubule binding domain of tau protein. Neuron 1989. 2: 1615-1624.
    • (1989) Neuron , vol.2 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 25
    • 0024507707 scopus 로고
    • Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains
    • Himmler, A., Drechsel, D., Kirschner, M.W. and Martin, D.W., Jr., Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains. Mol Cell Biol 1989. 9: 1381-1388.
    • (1989) Mol Cell Biol , vol.9 , pp. 1381-1388
    • Himmler, A.1    Drechsel, D.2    Kirschner, M.W.3    Martin Jr., D.W.4
  • 26
    • 36049044152 scopus 로고    scopus 로고
    • The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its ability to assemble microtubules
    • Acevedo, K., Li, R., Soo, P., Suryadinata, R., Sarcevic, B., et al. The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its ability to assemble microtubules. Exp Cell Res 2007. 313: 4091-4106.
    • (2007) Exp Cell Res , vol.313 , pp. 4091-4106
    • Acevedo, K.1    Li, R.2    Soo, P.3    Suryadinata, R.4    Sarcevic, B.5
  • 28
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F. and Jones, D. T., Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 2004. 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 29
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztányi, Z., Csizmók, V., Tompa, P. and Simon, I., IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005. 21: 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztányi, Z.1    Csizmók, V.2    Tompa, P.3    Simon, I.4
  • 30
    • 12344322940 scopus 로고    scopus 로고
    • Dynamic targeting of microtubules by TPPP/p25 affects cell survival
    • Lehotzky, A., Tirián, L., Tokési, N., Lénárt, P., Szabó, B., et al. Dynamic targeting of microtubules by TPPP/p25 affects cell survival. J Cell Sci 2004. 117: 6249-6259.
    • (2004) J Cell Sci , vol.117 , pp. 6249-6259
    • Lehotzky, A.1    Tirián, L.2    Tokési, N.3    Lénárt, P.4    Szabó, B.5
  • 31
    • 51049090182 scopus 로고    scopus 로고
    • Progress in the development of early diagnosis and a drug with unique pharmacology to improve cancer therapy
    • Lehotzky, A., Tokési, N., Gonzalez-Alvarez, I., Merino, V., Bermejo, M., et al. Progress in the development of early diagnosis and a drug with unique pharmacology to improve cancer therapy. Philos Transact A Math Phys Eng Sci 2008. 366: 3599-3617.
    • (2008) Philos Transact A Math Phys Eng Sci , vol.366 , pp. 3599-3617
    • Lehotzky, A.1    Tokési, N.2    Gonzalez-Alvarez, I.3    Merino, V.4    Bermejo, M.5
  • 32
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J. A., Ward, C. L. and Kopito, R. R., Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998. 143: 1883-1898.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 33
    • 62149092613 scopus 로고    scopus 로고
    • The expression of tubulin polymerization promoting protein TPPP/p25alpha is developmentally regulated in cultured rat brain oligodendrocytes and affected by proteolytic stress
    • Goldbaum, O., Jensen, P. H. and Richter-Landsberg, C., The expression of tubulin polymerization promoting protein TPPP/p25alpha is developmentally regulated in cultured rat brain oligodendrocytes and affected by proteolytic stress. Glia 2008. 56: 1736-1746.
    • (2008) Glia , vol.56 , pp. 1736-1746
    • Goldbaum, O.1    Jensen, P.H.2    Richter-Landsberg, C.3
  • 34
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal, M. F., Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci 2000. 23: 298-304.
    • (2000) Trends Neurosci , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 35
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: New targets for drug discovery
    • Lee, V. M. and Trojanowski, J. Q., Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: new targets for drug discovery. Neuron 2006. 52: 33-38.
    • (2006) Neuron , vol.52 , pp. 33-38
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 36
    • 51749107237 scopus 로고    scopus 로고
    • Increased glucose metabolism and ATP level in brain tissue of Huntington's disease transgenic mice
    • Oláh, J., Klivényi, P., Gardián, G., Vécsei, L., Orosz, F., et al. Increased glucose metabolism and ATP level in brain tissue of Huntington's disease transgenic mice. FEBS J 2008. 275: 4740-4755.
    • (2008) FEBS J , vol.275 , pp. 4740-4755
    • Oláh, J.1    Klivényi, P.2    Gardián, G.3    Vécsei, L.4    Orosz, F.5
  • 37
    • 0027393390 scopus 로고
    • A brain-specific protein p25 is localized and associated with oligodendrocytes, neuropil, and fiber-like structures of the CA3 hippocampal region in the rat brain
    • Takahashi, M., Tomizawa, K., Fujita, S. C., Sato, K., Uchida, T., et al. A brain-specific protein p25 is localized and associated with oligodendrocytes, neuropil, and fiber-like structures of the CA3 hippocampal region in the rat brain. J Neurochem 1993. 60: 228-235.
    • (1993) J Neurochem , vol.60 , pp. 228-235
    • Takahashi, M.1    Tomizawa, K.2    Fujita, S.C.3    Sato, K.4    Uchida, T.5
  • 38
    • 33846558382 scopus 로고    scopus 로고
    • The brain-specific protein TPPP/p25 in pathological protein deposits of neurodegenerative diseases
    • Kovács, G. G., Gelpi, E., Lehotzky, A., Hoftberger, R., Erdei, A., et al. The brain-specific protein TPPP/p25 in pathological protein deposits of neurodegenerative diseases. Acta Neuropathol (Berl) 2007. 113: 213-215.
    • (2007) Acta Neuropathol (Berl) , vol.113 , pp. 213-215
    • Kovács, G.G.1    Gelpi, E.2    Lehotzky, A.3    Hoftberger, R.4    Erdei, A.5
  • 39
    • 38149129457 scopus 로고    scopus 로고
    • A transcriptome database for astrocytes, neurons, and oligodendrocytes: A new resource for understanding brain development and function
    • Cahoy, J. D., Emery, B., Kaushal, A., Foo, L. C., Zamanian, J. L., et al. A transcriptome database for astrocytes, neurons, and oligodendrocytes: a new resource for understanding brain development and function. J Neurosci 2008. 28: 264-278.
    • (2008) J Neurosci , vol.28 , pp. 264-278
    • Cahoy, J.D.1    Emery, B.2    Kaushal, A.3    Foo, L.C.4    Zamanian, J.L.5
  • 40
    • 0036146078 scopus 로고    scopus 로고
    • A proteomic approach to rapidly elucidate oligodendrocyte-associated proteins expressed in the myelinating rat optic nerve
    • Colello, R. J., Fuss, B., Fox, M. A. and Alberti, J., A proteomic approach to rapidly elucidate oligodendrocyte-associated proteins expressed in the myelinating rat optic nerve. Electrophoresis 2002. 23: 144-151.
    • (2002) Electrophoresis , vol.23 , pp. 144-151
    • Colello, R.J.1    Fuss, B.2    Fox, M.A.3    Alberti, J.4
  • 41
    • 33748689004 scopus 로고    scopus 로고
    • P25 alpha/tubulin polymerization promoting protein expression by myelinating oligodendrocytes of the developing rat brain
    • Skjoerringe, T., Lundvig, D. M. S., Jensen, P. H. and Moos, T., P25 alpha/tubulin polymerization promoting protein expression by myelinating oligodendrocytes of the developing rat brain. J Neurochem 2006. 99: 333-342.
    • (2006) J Neurochem , vol.99 , pp. 333-342
    • Skjoerringe, T.1    Lundvig, D.M.S.2    Jensen, P.H.3    Moos, T.4
  • 42
    • 54849427024 scopus 로고    scopus 로고
    • TPPP orthologs are ciliary proteins
    • Orosz, F. and Ovádi, J., TPPP orthologs are ciliary proteins. FEBS Lett 2008. 582: 3757-3764.
    • (2008) FEBS Lett , vol.582 , pp. 3757-3764
    • Orosz, F.1    Ovádi, J.2
  • 43
    • 0003515251 scopus 로고
    • Berlin/Heidelberg/New York, Springer Verlag
    • Ohno, S., Evolution by gene duplication, Berlin/Heidelberg/New York, Springer Verlag, 1970.
    • (1970) Evolution by gene duplication
    • Ohno, S.1
  • 44
    • 0038817812 scopus 로고    scopus 로고
    • New evidence for genome-wide duplications at the origin of vertebrates using an amphioxus gene set and completed animal genomes
    • Panopoulou, G., Hennig, S., Groth, D., Krause, A., Poustka, A. J., et al. New evidence for genome-wide duplications at the origin of vertebrates using an amphioxus gene set and completed animal genomes. Genome Res 2003. 13: 1056-1066.
    • (2003) Genome Res , vol.13 , pp. 1056-1066
    • Panopoulou, G.1    Hennig, S.2    Groth, D.3    Krause, A.4    Poustka, A.J.5
  • 45
    • 0036208071 scopus 로고    scopus 로고
    • The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa
    • Cavalier-Smith, T., The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa. Int J Syst Evol Microbiol 2002. 52: 297-354.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 297-354
    • Cavalier-Smith, T.1
  • 46
    • 33644533515 scopus 로고    scopus 로고
    • Evolution of intraflagellar transport from coated vesicles and autogenous origin of the eukaryotic cilium
    • Jékely, G. and Arendt, D., Evolution of intraflagellar transport from coated vesicles and autogenous origin of the eukaryotic cilium. BioEssays 2006. 28: 191-198.
    • (2006) BioEssays , vol.28 , pp. 191-198
    • Jékely, G.1    Arendt, D.2
  • 47
    • 2342657884 scopus 로고    scopus 로고
    • Decoding cilia function: Defining specialized genes required for compartmentalized cilia biogenesis
    • Avidor-Reiss, T., Maer, A. M., Koundakjian, E., Polyanovsky, A., Keil, T., et al. Decoding cilia function: defining specialized genes required for compartmentalized cilia biogenesis. Cell 2004. 117: 527- 539.
    • (2004) Cell , vol.117 , pp. 527-539
    • Avidor-Reiss, T.1    Maer, A.M.2    Koundakjian, E.3    Polyanovsky, A.4    Keil, T.5
  • 49
    • 34548429735 scopus 로고    scopus 로고
    • The proteome of the mouse photoreceptor sensory cilium complex
    • Liu, Q., Tan, G., Levenkova, N., Li, T., Pugh, E. N., Jr., et al. The proteome of the mouse photoreceptor sensory cilium complex. Mol Cell Proteomics 2007. 6: 1299-1317.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1299-1317
    • Liu, Q.1    Tan, G.2    Levenkova, N.3    Li, T.4    Pugh Jr., E.N.5
  • 50
    • 34250183465 scopus 로고    scopus 로고
    • TPPP/p25 in brain tumours: Expression in non-neoplastic oligodendrocytes but not in oligodendroglioma cells
    • Preusser, M., Lehotzky, A., Budka, H., Ovádi, J. and Kovács, G. G., TPPP/p25 in brain tumours: expression in non-neoplastic oligodendrocytes but not in oligodendroglioma cells. Acta Neuropathol 2007. 113: 213-215.
    • (2007) Acta Neuropathol , vol.113 , pp. 213-215
    • Preusser, M.1    Lehotzky, A.2    Budka, H.3    Ovádi, J.4    Kovács, G.G.5
  • 51
    • 35348909482 scopus 로고    scopus 로고
    • P25 alpha relocalizes in oligodendroglia from myelin to cytoplasmic inclusions in multiple system atrophy
    • Song, Y. J. C., Lundvig, D. M. S., Huang, Y., Gai, W. P., Blumbergs, P. C., et al. P25 alpha relocalizes in oligodendroglia from myelin to cytoplasmic inclusions in multiple system atrophy. Am J Pathol 2007. 171: 1291-1303.
    • (2007) Am J Pathol , vol.171 , pp. 1291-1303
    • Song, Y.J.C.1    Lundvig, D.M.S.2    Huang, Y.3    Gai, W.P.4    Blumbergs, P.C.5
  • 52
    • 34249656320 scopus 로고    scopus 로고
    • Process elongation of oligodendrocytes is promoted by the Kelch-related protein MRP2/KLHL1
    • Jiang, S., Seng, S., Avraham, H. K., Fu, Y. and Avraham, S., Process elongation of oligodendrocytes is promoted by the Kelch-related protein MRP2/KLHL1. J Biol Chem 2007. 282: 12319-12329.
    • (2007) J Biol Chem , vol.282 , pp. 12319-12329
    • Jiang, S.1    Seng, S.2    Avraham, H.K.3    Fu, Y.4    Avraham, S.5
  • 53
    • 17844361897 scopus 로고    scopus 로고
    • ATP regulates oligodendrocyte progenitor migration, proliferation, and differentiation: Involvement of metabotropic P2 receptors
    • Agresti, C., Meomartini, M. E., Amadio, S., Ambrosini, E., Volonté, C., et al. ATP regulates oligodendrocyte progenitor migration, proliferation, and differentiation: involvement of metabotropic P2 receptors. Brain Res Brain Res Rev 2005. 48: 157-165.
    • (2005) Brain Res Brain Res Rev , vol.48 , pp. 157-165
    • Agresti, C.1    Meomartini, M.E.2    Amadio, S.3    Ambrosini, E.4    Volonté, C.5
  • 54
    • 0033520474 scopus 로고    scopus 로고
    • Alpha-synuclein binds to tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356
    • Jensen, P. H., Hager, H., Nielsen, M. S., Hojrup, P., Gliemann, J., et al. Alpha-synuclein binds to tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. J Biol Chem 1999. 274: 25481-25489.
    • (1999) J Biol Chem , vol.274 , pp. 25481-25489
    • Jensen, P.H.1    Hager, H.2    Nielsen, M.S.3    Hojrup, P.4    Gliemann, J.5
  • 55
    • 0035500991 scopus 로고    scopus 로고
    • Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells
    • Payton, J. E., Perrin, R. J., Clayton, D. F. and George, J. M., Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells. Brain Res Mol Brain Res 2001. 95: 138-145.
    • (2001) Brain Res Mol Brain Res , vol.95 , pp. 138-145
    • Payton, J.E.1    Perrin, R.J.2    Clayton, D.F.3    George, J.M.4
  • 57
    • 20044383388 scopus 로고    scopus 로고
    • p25alpha Stimulates alpha-synuclein aggregation and is colocalized with aggregated alpha-synuclein in alpha-synucleinopathies
    • Lindersson, E., Lundvig, D., Petersen, C., Madsen, P., Nyengaard, J. R., et al. p25alpha Stimulates alpha-synuclein aggregation and is colocalized with aggregated alpha-synuclein in alpha-synucleinopathies. J Biol Chem 2005. 280: 5703-5715.
    • (2005) J Biol Chem , vol.280 , pp. 5703-5715
    • Lindersson, E.1    Lundvig, D.2    Petersen, C.3    Madsen, P.4    Nyengaard, J.R.5
  • 58
    • 33750063178 scopus 로고    scopus 로고
    • Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies
    • Oláh, J., Tokési, N., Vincze, O., Horváth, I., Lehotzky, A., et al. Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies. FEBS Lett 2006. 580: 5807-5814.
    • (2006) FEBS Lett , vol.580 , pp. 5807-5814
    • Oláh, J.1    Tokési, N.2    Vincze, O.3    Horváth, I.4    Lehotzky, A.5
  • 59
    • 33744937070 scopus 로고    scopus 로고
    • Subcellular proteomics reveals neuromelanin granules to be a lysosomerelated organelle
    • Tribl, F., Marcus, K., Meyer, H. E., Bringmann, G., Gerlach, M., et al. Subcellular proteomics reveals neuromelanin granules to be a lysosomerelated organelle. J Neural Transm 2006. 113: 741-749.
    • (2006) J Neural Transm , vol.113 , pp. 741-749
    • Tribl, F.1    Marcus, K.2    Meyer, H.E.3    Bringmann, G.4    Gerlach, M.5
  • 60
    • 5644266504 scopus 로고    scopus 로고
    • Identification and verification of novel rodent postsynaptic density proteins
    • Jordan, B. A., Fernholz, B. D., Boussac, M., Xu, C., Grigorean, G., et al. Identification and verification of novel rodent postsynaptic density proteins. Mol Cell Proteomics 2004. 3: 857-871.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 857-871
    • Jordan, B.A.1    Fernholz, B.D.2    Boussac, M.3    Xu, C.4    Grigorean, G.5
  • 61
    • 9144265671 scopus 로고    scopus 로고
    • Proteomics analysis of rat brain postsynaptic density. Implications of the diverse protein functional groups for the integration of synaptic physiology
    • Li, K.W., Hornshaw, M. P., Van der Schors, R. C., Watson, R., Tate, S., et al. Proteomics analysis of rat brain postsynaptic density. Implications of the diverse protein functional groups for the integration of synaptic physiology. J Biol Chem 2004. 279: 987-1002.
    • (2004) J Biol Chem , vol.279 , pp. 987-1002
    • Li, K.W.1    Hornshaw, M.P.2    Van der Schors, R.C.3    Watson, R.4    Tate, S.5
  • 62
    • 0942287657 scopus 로고    scopus 로고
    • Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry
    • Yoshimura, Y., Yamauchi, Y., Shinkawa, T., Taoka, M., Donai, H., et al. Molecular constituents of the postsynaptic density fraction revealed by proteomic analysis using multidimensional liquid chromatography-tandem mass spectrometry. J Neurochem 2004. 88: 759-768.
    • (2004) J Neurochem , vol.88 , pp. 759-768
    • Yoshimura, Y.1    Yamauchi, Y.2    Shinkawa, T.3    Taoka, M.4    Donai, H.5
  • 63
  • 64
    • 12144291497 scopus 로고    scopus 로고
    • Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling
    • Blondeau, F., Ritter, B., Allaire, P. D., Wasiak, S., Girard, M., et al. Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling. Proc Natl Acad Sci USA 2004. 101: 3833-3838.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3833-3838
    • Blondeau, F.1    Ritter, B.2    Allaire, P.D.3    Wasiak, S.4    Girard, M.5
  • 65
    • 1542395746 scopus 로고    scopus 로고
    • Hippocampal protein-protein interactions in spatial memory
    • Nelson, T. J., Backlund, P. S. and Alkon, D. L., Hippocampal protein-protein interactions in spatial memory. Hippocampus 2004. 14: 46-57.
    • (2004) Hippocampus , vol.14 , pp. 46-57
    • Nelson, T.J.1    Backlund, P.S.2    Alkon, D.L.3
  • 67
    • 36448991500 scopus 로고    scopus 로고
    • Larkin, M. A, Blackshields, G, Brown, N. P, Chenna, R, McGettigan, P. A, et al. Clustal W and Clustal X version 2.0. Bioinformatics 2007. 23: 2947-2948
    • Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., et al. Clustal W and Clustal X version 2.0. Bioinformatics 2007. 23: 2947-2948.
  • 68
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R., Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000. 10: 524-530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 70
    • 0031841616 scopus 로고    scopus 로고
    • Phosphatidic acid-dependent phosphorylation of a 29-kDa protein by protein kinase C alpha in bovine brain cytosol
    • Yokozeki, T., Homma, K., Kuroda, S., Kikkawa, U., Ohno, S., et al. Phosphatidic acid-dependent phosphorylation of a 29-kDa protein by protein kinase C alpha in bovine brain cytosol. J Neurochem 1998. 71: 410-417.
    • (1998) J Neurochem , vol.71 , pp. 410-417
    • Yokozeki, T.1    Homma, K.2    Kuroda, S.3    Kikkawa, U.4    Ohno, S.5


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