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Volumn 92, Issue 1, 2014, Pages 104-115

Zebrafish brain proteomics reveals central proteins involved in neurodegeneration

Author keywords

Brain; Neurodegeneration; Proteomics; Zebrafish

Indexed keywords

BRAIN PROTEIN; PROTEOME;

EID: 84888073546     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.23297     Document Type: Article
Times cited : (17)

References (59)
  • 1
    • 0034604710 scopus 로고    scopus 로고
    • Phosphorylation of collapsin response mediator protein-2 by rho-kinase. Evidence for two separate signaling pathways for growth cone collapse
    • Arimura N, Inagaki N, Chihara K, Ménager C, Nakamura N, Amano M, Iwamatsu A, Goshima Y, Kaibuchi K. 2000. Phosphorylation of collapsin response mediator protein-2 by rho-kinase. Evidence for two separate signaling pathways for growth cone collapse. J Biol Chem 275:23973-23980.
    • (2000) J Biol Chem , vol.275 , pp. 23973-23980
    • Arimura, N.1    Inagaki, N.2    Chihara, K.3    Ménager, C.4    Nakamura, N.5    Amano, M.6    Iwamatsu, A.7    Goshima, Y.8    Kaibuchi, K.9
  • 3
    • 69249089272 scopus 로고    scopus 로고
    • Neuroproteomics: understanding the molecular organization and complexity of the brain
    • Bayes A, Grant SG. 2009. Neuroproteomics: understanding the molecular organization and complexity of the brain. Nat Rev Neurosci 10:635-646.
    • (2009) Nat Rev Neurosci , vol.10 , pp. 635-646
    • Bayes, A.1    Grant, S.G.2
  • 5
  • 6
    • 73249116888 scopus 로고    scopus 로고
    • Software tool for researching annotations of proteins: open-source protein annotation software with data visualization
    • Bhatia VN, Perlman DH, Costello CE, McComb ME. 2009. Software tool for researching annotations of proteins: open-source protein annotation software with data visualization. Anal Chem 81:9819-9823.
    • (2009) Anal Chem , vol.81 , pp. 9819-9823
    • Bhatia, V.N.1    Perlman, D.H.2    Costello, C.E.3    McComb, M.E.4
  • 7
    • 84859732716 scopus 로고    scopus 로고
    • Classic and new animal models of Parkinson's disease
    • doi: 10.1155/2012/845618.
    • Blesa J, Phani S, Jackson-Lewis V, Przedborski S. 2012. Classic and new animal models of Parkinson's disease. J Biomed Biotechnol 2012:845618. doi: 10.1155/2012/845618.
    • (2012) J Biomed Biotechnol , vol.2012 , pp. 845618
    • Blesa, J.1    Phani, S.2    Jackson-Lewis, V.3    Przedborski, S.4
  • 10
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of BB, oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A, Aksenov M, Aksenova M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR, Butterfield DA. 2002. Proteomic identification of BB, oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic Biol Med 33:562-571.
    • (2002) Free Radic Biol Med , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 11
    • 79952757411 scopus 로고    scopus 로고
    • Amyloid P component as a plasma marker for Parkinson's disease identified by a proteomic approach
    • Chen HM, Lin CY, Wang V. 2011. Amyloid P component as a plasma marker for Parkinson's disease identified by a proteomic approach. Clin Biochem 44:377-385.
    • (2011) Clin Biochem , vol.44 , pp. 377-385
    • Chen, H.M.1    Lin, C.Y.2    Wang, V.3
  • 12
    • 14744302540 scopus 로고    scopus 로고
    • Accumulation of human SOD1 and ubiquitinated deposits in the spinal cord of SOD1G93A mice during motor neuron disease progression correlates with a decrease of proteasome
    • Cheroni C, Peviani M, Cascio P, Debiasi S, Monti C, Bendotti C. 2005. Accumulation of human SOD1 and ubiquitinated deposits in the spinal cord of SOD1G93A mice during motor neuron disease progression correlates with a decrease of proteasome. Neurobiol Dis 18:509-522.
    • (2005) Neurobiol Dis , vol.18 , pp. 509-522
    • Cheroni, C.1    Peviani, M.2    Cascio, P.3    Debiasi, S.4    Monti, C.5    Bendotti, C.6
  • 13
    • 84875635613 scopus 로고    scopus 로고
    • Mitophagy and Parkinson's disease: be eaten to stay healthy
    • in press).
    • de Vries RL, Przedborski S. 2012. Mitophagy and Parkinson's disease: be eaten to stay healthy. Mol Cell Neurosci (in press).
    • (2012) Mol Cell Neurosci
    • de Vries, R.L.1    Przedborski, S.2
  • 14
    • 84857061103 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in familial amyotrophic lateral sclerosis
    • Faes L, Callewaert G. 2011. Mitochondrial dysfunction in familial amyotrophic lateral sclerosis. J Bioenerg Biomembr 43:587-592.
    • (2011) J Bioenerg Biomembr , vol.43 , pp. 587-592
    • Faes, L.1    Callewaert, G.2
  • 16
    • 84862501132 scopus 로고    scopus 로고
    • 14-3-3 Proteins in neurological disorders
    • Foote M, Zhou Y. 2012. 14-3-3 Proteins in neurological disorders. Int J Biochem Mol Biol. 3:152-164.
    • (2012) Int J Biochem Mol Biol. , vol.3 , pp. 152-164
    • Foote, M.1    Zhou, Y.2
  • 17
    • 79961193678 scopus 로고    scopus 로고
    • Superoxide dismutases: role in redox signaling, vascular function, and diseases
    • Fukai T, Ushio-Fukai M. 2011. Superoxide dismutases: role in redox signaling, vascular function, and diseases. Antioxid Redox Signal 15:1583-1606.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 1583-1606
    • Fukai, T.1    Ushio-Fukai, M.2
  • 20
    • 0034433275 scopus 로고    scopus 로고
    • Neurofilament protein synthesis and phosphorylation
    • Grant P, Pant HC. 2000. Neurofilament protein synthesis and phosphorylation. J Neurocytol 29:843-872.
    • (2000) J Neurocytol , vol.29 , pp. 843-872
    • Grant, P.1    Pant, H.C.2
  • 21
    • 78650142376 scopus 로고    scopus 로고
    • Protein oxidative modifications in the ageing brain: consequence for the onset of neurodegenerative disease
    • Grimm S, Hoehn A, Davies KJ, Grune T. 2011. Protein oxidative modifications in the ageing brain: consequence for the onset of neurodegenerative disease. Free Radic Res 45:73-88.
    • (2011) Free Radic Res , vol.45 , pp. 73-88
    • Grimm, S.1    Hoehn, A.2    Davies, K.J.3    Grune, T.4
  • 22
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex
    • Hernández MP, Sullivan WP, Toft DO. 2002. The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J Biol Chem 277:38294-38304.
    • (2002) J Biol Chem , vol.277 , pp. 38294-38304
    • Hernández, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 23
    • 0041851031 scopus 로고    scopus 로고
    • Glycosylation of the alpha and beta tubulin by sialyloligosaccharides
    • Hino M, Kijima-Suda I, Nagai Y, Hosoya H. 2003. Glycosylation of the alpha and beta tubulin by sialyloligosaccharides. Zool Sci 20:709-715.
    • (2003) Zool Sci , vol.20 , pp. 709-715
    • Hino, M.1    Kijima-Suda, I.2    Nagai, Y.3    Hosoya, H.4
  • 24
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using David bioinformatics resources
    • Huang daW, Sherman BT, Lempicki RA. 2009. Systematic and integrative analysis of large gene lists using David bioinformatics resources. Nat Protoc 4:44-57.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • Huang, daW.1    Sherman, B.T.2    Lempicki, R.A.3
  • 27
    • 79955049275 scopus 로고    scopus 로고
    • The role of ubiquitylation in nerve cell development
    • Kawabe H, Brose N. 2011. The role of ubiquitylation in nerve cell development. Nat Rev Neurosci 12:251-268.
    • (2011) Nat Rev Neurosci , vol.12 , pp. 251-268
    • Kawabe, H.1    Brose, N.2
  • 29
    • 27744553322 scopus 로고    scopus 로고
    • Proteomic analysis of glial fibrillary acidic protein in Alzheimer's disease and aging brain
    • Korolainen MA, Auriola S, Nyman TA, Alafuzoff I, Pirttilä T. 2005. Proteomic analysis of glial fibrillary acidic protein in Alzheimer's disease and aging brain. Neurobiol Dis 20:858-870.
    • (2005) Neurobiol Dis , vol.20 , pp. 858-870
    • Korolainen, M.A.1    Auriola, S.2    Nyman, T.A.3    Alafuzoff, I.4    Pirttilä, T.5
  • 30
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman NL. 2009. The ubiquitin proteasome system in neuropathology. Acta Neuropathol 118:329-347.
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 32
    • 70449417623 scopus 로고    scopus 로고
    • Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities
    • Magrané J, Hervias I, Henning MS, Damiano M, Kawamata H, Manfredi G. 2009. Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities. Hum Mol Genet 18:4552-4564.
    • (2009) Hum Mol Genet , vol.18 , pp. 4552-4564
    • Magrané, J.1    Hervias, I.2    Henning, M.S.3    Damiano, M.4    Kawamata, H.5    Manfredi, G.6
  • 33
    • 34447506680 scopus 로고    scopus 로고
    • Transgenic mice with human mutant genes causing Parkinson's disease and amyotrophic lateral sclerosis provide common insight into mechanisms of motor neuron selective vulnerability to degeneration
    • Martin LJ. 2007. Transgenic mice with human mutant genes causing Parkinson's disease and amyotrophic lateral sclerosis provide common insight into mechanisms of motor neuron selective vulnerability to degeneration. Rev Neurosci 18:115-136.
    • (2007) Rev Neurosci , vol.18 , pp. 115-136
    • Martin, L.J.1
  • 34
    • 0033929093 scopus 로고    scopus 로고
    • Adducin: structure, function and regulation
    • Matsuoka Y, Li X, Bennett V. 2000. Adducin: structure, function and regulation. Cell Mol Life Sci 57:884-895.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 884-895
    • Matsuoka, Y.1    Li, X.2    Bennett, V.3
  • 35
    • 0032564134 scopus 로고    scopus 로고
    • Parkinson's disease, pesticides, and glutathione transferase polymorphisms
    • Menegon A, Board PG, Blackburn AC, Mellick GD, Le Couteur DG. 1998. Parkinson's disease, pesticides, and glutathione transferase polymorphisms. Lancet 352:1344-1346.
    • (1998) Lancet , vol.352 , pp. 1344-1346
    • Menegon, A.1    Board, P.G.2    Blackburn, A.C.3    Mellick, G.D.4    Le Couteur, D.G.5
  • 36
    • 2342417953 scopus 로고    scopus 로고
    • Oxidative stress and neuroinflammation in Alzheimer's disease and amyotrophic lateral sclerosis: common links and potential therapeutic targets
    • Mhatre M, Floyd RA, Hensley K. 2004. Oxidative stress and neuroinflammation in Alzheimer's disease and amyotrophic lateral sclerosis: common links and potential therapeutic targets. J Alzheimers Dis 6:147-157.
    • (2004) J Alzheimers Dis , vol.6 , pp. 147-157
    • Mhatre, M.1    Floyd, R.A.2    Hensley, K.3
  • 42
    • 67349126209 scopus 로고    scopus 로고
    • CSF neurofilament protein analysis in the differential diagnosis of ALS
    • Reijn TS, Abdo WF, Schelhaas HJ, Verbeek MM. 2009. CSF neurofilament protein analysis in the differential diagnosis of ALS. J Neurol 256:615-619.
    • (2009) J Neurol , vol.256 , pp. 615-619
    • Reijn, T.S.1    Abdo, W.F.2    Schelhaas, H.J.3    Verbeek, M.M.4
  • 43
    • 77954999004 scopus 로고    scopus 로고
    • Understanding the molecular basis of Parkinson's disease, identification of biomarkers and routes to therapy
    • Robinson PA. 2010. Understanding the molecular basis of Parkinson's disease, identification of biomarkers and routes to therapy. Expert Rev Proteomics 7:565-578.
    • (2010) Expert Rev Proteomics , vol.7 , pp. 565-578
    • Robinson, P.A.1
  • 44
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein JD. 2009. Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann Neurol 65(Suppl 1):S3-S9.
    • (2009) Ann Neurol , vol.65 , Issue.SUPPL 1
    • Rothstein, J.D.1
  • 47
    • 77953623249 scopus 로고    scopus 로고
    • Proteomic profile of zebrafish brain based on two-dimensional gel electrophoresis matrix-assisted laser desorption/ionization MS/MS analysis
    • Singh SK, Sundaram CS, Shanbhag S, Idris MM. 2010. Proteomic profile of zebrafish brain based on two-dimensional gel electrophoresis matrix-assisted laser desorption/ionization MS/MS analysis. Zebrafish 7:169-177.
    • (2010) Zebrafish , vol.7 , pp. 169-177
    • Singh, S.K.1    Sundaram, C.S.2    Shanbhag, S.3    Idris, M.M.4
  • 51
    • 53049090386 scopus 로고    scopus 로고
    • Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation
    • Ström AL, Shi P, Zhang F, Gal J, Kilty R, Hayward LJ, Zhu H. 2008. Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation. J Biol Chem 283:22795-22805.
    • (2008) J Biol Chem , vol.283 , pp. 22795-22805
    • Ström, A.L.1    Shi, P.2    Zhang, F.3    Gal, J.4    Kilty, R.5    Hayward, L.J.6    Zhu, H.7
  • 52
    • 84878108098 scopus 로고    scopus 로고
    • α-Synuclein coaggregation in familial amyotrophic lateral sclerosis with SOD1 gene mutation
    • S0046-8177(12)00422-4 (in press).
    • Takei YI, Oguchi K, Koshihara H, Hineno A, Nakamura A, Ohara S. 2013. α-Synuclein coaggregation in familial amyotrophic lateral sclerosis with SOD1 gene mutation. Hum Pathol S0046-8177(12)00422-4 (in press).
    • (2013) Hum Pathol
    • Takei, Y.I.1    Oguchi, K.2    Koshihara, H.3    Hineno, A.4    Nakamura, A.5    Ohara, S.6
  • 53
    • 60549104791 scopus 로고    scopus 로고
    • Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3
    • Tateno M, Kato S, Sakurai T, Nukina N, Takahashi R, Araki T. 2009. Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3. Hum Mol Genet 18:942-955.
    • (2009) Hum Mol Genet , vol.18 , pp. 942-955
    • Tateno, M.1    Kato, S.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Araki, T.6
  • 54
    • 0036199623 scopus 로고    scopus 로고
    • High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation
    • Wang J, Xu G, Borchelt DR. 2002. High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation. Neurobiol Dis 9:139-148.
    • (2002) Neurobiol Dis , vol.9 , pp. 139-148
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 56
    • 77952353245 scopus 로고    scopus 로고
    • The arabidopsis DJ-1a protein confers stress protection through cytosolic SOD activation
    • Xu XM, Lin H, Maple J, Björkblom B, Alves G, Larsen JP, Møller SG. 2010. The arabidopsis DJ-1a protein confers stress protection through cytosolic SOD activation. J Cell Sci 123:1644-1651.
    • (2010) J Cell Sci , vol.123 , pp. 1644-1651
    • Xu, X.M.1    Lin, H.2    Maple, J.3    Björkblom, B.4    Alves, G.5    Larsen, J.P.6    Møller, S.G.7
  • 57
    • 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. 2004. 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 279:26105-26114.
    • (2004) J Biol Chem , vol.279 , pp. 26105-26114
    • Yuan, Z.1    Agarwal-Mawal, A.2    Paudel, H.K.3
  • 59
    • 77957372670 scopus 로고    scopus 로고
    • Galectin-3 is a candidate biomarker for amyotrophic lateral sclerosis: discovery by a proteomics approach
    • Zhou JY, Afjehi-Sadat L, Asress S, Duong DM, Cudkowicz M, Glass JD, Peng J. 2010. Galectin-3 is a candidate biomarker for amyotrophic lateral sclerosis: discovery by a proteomics approach. J Proteome Res 9:5133-5141.
    • (2010) J Proteome Res , vol.9 , pp. 5133-5141
    • Zhou, J.Y.1    Afjehi-Sadat, L.2    Asress, S.3    Duong, D.M.4    Cudkowicz, M.5    Glass, J.D.6    Peng, J.7


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