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Volumn 62, Issue 6, 2014, Pages 333-336

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease

Author keywords

Alzheimer's disease; GAPDH; Neurofibrillary tangles; amyloid aggregation

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; AMYLOID PROTEIN; BIOLOGICAL MARKER; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; TAU PROTEIN; AMYLOID PRECURSOR PROTEIN; MAPT PROTEIN, HUMAN; PROTEIN AGGREGATE;

EID: 84908327030     PISSN: 03698114     EISSN: 17683114     Source Type: Journal    
DOI: 10.1016/j.patbio.2014.08.002     Document Type: Review
Times cited : (41)

References (55)
  • 2
    • 0000858424 scopus 로고
    • Über einen eigenartigen schweren Erkrankungsprozeβ der Hirnrincle
    • Alzheimer A. Über einen eigenartigen schweren Erkrankungsprozeβ der Hirnrincle. Neurol Central 1906, 25:1134.
    • (1906) Neurol Central , vol.25 , pp. 1134
    • Alzheimer, A.1
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 4
    • 80052266213 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics
    • Karran E., Mercken M., De Strooper B. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat Rev Drug Discov 2011, 10:698-712.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 698-712
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 5
    • 0141596079 scopus 로고    scopus 로고
    • Transgenic mouse models of Alzheimer's disease: phenotype and application
    • Higgins G.A., Jacobsen H. Transgenic mouse models of Alzheimer's disease: phenotype and application. Behav Pharmacol 2003, 14:419-438.
    • (2003) Behav Pharmacol , vol.14 , pp. 419-438
    • Higgins, G.A.1    Jacobsen, H.2
  • 6
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield D.A. Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic Res 2002, 36:1307-1313.
    • (2002) Free Radic Res , vol.36 , pp. 1307-1313
    • Butterfield, D.A.1
  • 8
    • 84866508857 scopus 로고    scopus 로고
    • Model Hirano bodies protect against tau-independent and tau-dependent cell death initiated by the amyloid precursor protein intracellular domain
    • Furgerson M., Fechheimer M., Furukawa R. Model Hirano bodies protect against tau-independent and tau-dependent cell death initiated by the amyloid precursor protein intracellular domain. PloS One 2012, 7:e44996.
    • (2012) PloS One , vol.7 , pp. e44996
    • Furgerson, M.1    Fechheimer, M.2    Furukawa, R.3
  • 10
    • 67449118593 scopus 로고    scopus 로고
    • Proteomic identification of proteins in the human brain: Towards a more comprehensive understanding of neurodegenerative disease
    • Caudle W.M., Pan S., Shi M., Quinn T., Hoekstra J., Beyer R.P., et al. Proteomic identification of proteins in the human brain: Towards a more comprehensive understanding of neurodegenerative disease. Proteomics Clin Appl 2008, 2:1484-1497.
    • (2008) Proteomics Clin Appl , vol.2 , pp. 1484-1497
    • Caudle, W.M.1    Pan, S.2    Shi, M.3    Quinn, T.4    Hoekstra, J.5    Beyer, R.P.6
  • 11
    • 33845892752 scopus 로고    scopus 로고
    • Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database
    • Bertram L., McQueen M.B., Mullin K., Blacker D., Tanzi R.E. Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database. Nat Gen 2007, 39:17-23.
    • (2007) Nat Gen , vol.39 , pp. 17-23
    • Bertram, L.1    McQueen, M.B.2    Mullin, K.3    Blacker, D.4    Tanzi, R.E.5
  • 12
    • 0028865070 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain
    • Sunaga K., Takahashi H., Chuang D.M., Ishitani R. Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain. Neurosci Lett 1995, 200:133-136.
    • (1995) Neurosci Lett , vol.200 , pp. 133-136
    • Sunaga, K.1    Takahashi, H.2    Chuang, D.M.3    Ishitani, R.4
  • 13
    • 77954497959 scopus 로고    scopus 로고
    • Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration
    • Butterfield D.A., Hardas S.S., Lange M.L. Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegeneration. J Alzheimer's Dis 2010, 20:369-393.
    • (2010) J Alzheimer's Dis , vol.20 , pp. 369-393
    • Butterfield, D.A.1    Hardas, S.S.2    Lange, M.L.3
  • 14
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress
    • Butterfield D.A., Lauderback C.M. Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress. Free Radic Biol Med 2002, 32:1050-1060.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 15
    • 65949121134 scopus 로고    scopus 로고
    • Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options
    • Uttara B., Singh A.V., Zamboni P., Mahajan R.T. Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options. Curr Neuropharmacol 2009, 7:65-74.
    • (2009) Curr Neuropharmacol , vol.7 , pp. 65-74
    • Uttara, B.1    Singh, A.V.2    Zamboni, P.3    Mahajan, R.T.4
  • 16
    • 34248223082 scopus 로고    scopus 로고
    • An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach
    • Newman S.F., Sultana R., Perluigi M., Coccia R., Cai J., Pierce W.M., et al. An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach. J Neurosci Res 2007, 85:1506-1514.
    • (2007) J Neurosci Res , vol.85 , pp. 1506-1514
    • Newman, S.F.1    Sultana, R.2    Perluigi, M.3    Coccia, R.4    Cai, J.5    Pierce, W.M.6
  • 17
    • 33645089917 scopus 로고    scopus 로고
    • Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach
    • Sultana R., Poon H.F., Cai J., Pierce W.M., Merchant M., Klein J.B., et al. Identification of nitrated proteins in Alzheimer's disease brain using a redox proteomics approach. Neurobiol Dis 2006, 22:76-87.
    • (2006) Neurobiol Dis , vol.22 , pp. 76-87
    • Sultana, R.1    Poon, H.F.2    Cai, J.3    Pierce, W.M.4    Merchant, M.5    Klein, J.B.6
  • 18
    • 84867514319 scopus 로고    scopus 로고
    • Basic biology of GAPDH
    • Seidler N.W. Basic biology of GAPDH. Adv Exp Med Biol 2013, 985:1-36.
    • (2013) Adv Exp Med Biol , vol.985 , pp. 1-36
    • Seidler, N.W.1
  • 19
    • 33646541982 scopus 로고    scopus 로고
    • High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase
    • Jenkins J.L., Tanner J.J. High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr D Biol Crystallogr 2006, 62:290-301.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 290-301
    • Jenkins, J.L.1    Tanner, J.J.2
  • 20
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M.A. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1999, 1432:159-184.
    • (1999) Biochim Biophys Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 21
    • 70449525136 scopus 로고    scopus 로고
    • Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation
    • Demarse N.A., Ponnusamy S., Spicer E.K., Apohan E., Baatz J.E., Ogretmen B., et al. Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation. J Mol Biol 2009, 394:789-803.
    • (2009) J Mol Biol , vol.394 , pp. 789-803
    • Demarse, N.A.1    Ponnusamy, S.2    Spicer, E.K.3    Apohan, E.4    Baatz, J.E.5    Ogretmen, B.6
  • 22
    • 79951580936 scopus 로고    scopus 로고
    • Binding of glyceraldehyde-3-phosphate dehydrogenase to the cis-acting element of structure-anchored repression in ccn2 mRNA
    • Kondo S., Kubota S., Mukudai Y., Nishida T., Yoshihama Y., Shirota T., et al. Binding of glyceraldehyde-3-phosphate dehydrogenase to the cis-acting element of structure-anchored repression in ccn2 mRNA. Biochem Biophys Res Commun 2011, 405:382-387.
    • (2011) Biochem Biophys Res Commun , vol.405 , pp. 382-387
    • Kondo, S.1    Kubota, S.2    Mukudai, Y.3    Nishida, T.4    Yoshihama, Y.5    Shirota, T.6
  • 23
    • 0041352962 scopus 로고    scopus 로고
    • S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component
    • Zheng L., Roeder R.G., Luo Y. S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 2003, 114:255-266.
    • (2003) Cell , vol.114 , pp. 255-266
    • Zheng, L.1    Roeder, R.G.2    Luo, Y.3
  • 24
    • 0036479109 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota/lambda and plays a role in microtubule dynamics in the early secretory pathway
    • Tisdale E.J. Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota/lambda and plays a role in microtubule dynamics in the early secretory pathway. J Biol Chem 2002, 277:3334-3341.
    • (2002) J Biol Chem , vol.277 , pp. 3334-3341
    • Tisdale, E.J.1
  • 25
    • 46449101370 scopus 로고    scopus 로고
    • Role of glyceraldehyde-3-phosphate dehydrogenase in vesicular transport from golgi apparatus to endoplasmic reticulum
    • Bryksin A.V., Laktionov P.P. Role of glyceraldehyde-3-phosphate dehydrogenase in vesicular transport from golgi apparatus to endoplasmic reticulum. Biochem Biokhim 2008, 73:619-625.
    • (2008) Biochem Biokhim , vol.73 , pp. 619-625
    • Bryksin, A.V.1    Laktionov, P.P.2
  • 26
    • 13444255991 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor/GAPDH complex augments Ca2+ release via locally derived NADH
    • Patterson R.L., van Rossum D.B., Kaplin A.I., Barrow R.K., Snyder S.H. Inositol 1,4,5-trisphosphate receptor/GAPDH complex augments Ca2+ release via locally derived NADH. Proc Natl Acad Sci USA 2005, 102:1357-1359.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1357-1359
    • Patterson, R.L.1    van Rossum, D.B.2    Kaplin, A.I.3    Barrow, R.K.4    Snyder, S.H.5
  • 27
    • 0029870382 scopus 로고    scopus 로고
    • Enhancement of hammerhead ribozyme catalysis by glyceraldehyde-3-phosphate dehydrogenase
    • Sioud M., Jespersen L. Enhancement of hammerhead ribozyme catalysis by glyceraldehyde-3-phosphate dehydrogenase. J Mol Biol 1996, 257:775-789.
    • (1996) J Mol Biol , vol.257 , pp. 775-789
    • Sioud, M.1    Jespersen, L.2
  • 28
    • 0030887909 scopus 로고    scopus 로고
    • Glutathione conjugates recognize the Rossmann fold of glyceraldehyde-3-phosphate dehydrogenase
    • Puder M., Soberman R.J. Glutathione conjugates recognize the Rossmann fold of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 1997, 272:10936-10940.
    • (1997) J Biol Chem , vol.272 , pp. 10936-10940
    • Puder, M.1    Soberman, R.J.2
  • 29
    • 0033232529 scopus 로고    scopus 로고
    • Involvement of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and p53 in neuronal apoptosis: evidence that GAPDH is upregulated by p53
    • Chen R.W., Saunders P.A., Wei H., Li Z., Seth P., Chuang D.M. Involvement of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and p53 in neuronal apoptosis: evidence that GAPDH is upregulated by p53. J Neurosci 1999, 19:9654-9662.
    • (1999) J Neurosci , vol.19 , pp. 9654-9662
    • Chen, R.W.1    Saunders, P.A.2    Wei, H.3    Li, Z.4    Seth, P.5    Chuang, D.M.6
  • 30
    • 33746445177 scopus 로고    scopus 로고
    • Nitric oxide-GAPDH-Siah: a novel cell death cascade
    • Hara M.R., Snyder S.H. Nitric oxide-GAPDH-Siah: a novel cell death cascade. Cell Mol Neurobiol 2006, 26:527-538.
    • (2006) Cell Mol Neurobiol , vol.26 , pp. 527-538
    • Hara, M.R.1    Snyder, S.H.2
  • 34
    • 0029664992 scopus 로고    scopus 로고
    • Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH
    • Burke J.R., Enghild J.J., Martin M.E., Jou Y.S., Myers R.M., Roses A.D., et al. Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nat Med 1996, 2:347-350.
    • (1996) Nat Med , vol.2 , pp. 347-350
    • Burke, J.R.1    Enghild, J.J.2    Martin, M.E.3    Jou, Y.S.4    Myers, R.M.5    Roses, A.D.6
  • 35
    • 47249104380 scopus 로고    scopus 로고
    • Characterization of the interaction between Abeta 1-42 and glyceraldehyde phosphodehydrogenase
    • Verdier Y., Foldi I., Sergeant N., Fulop L., Penke Z., Janaky T., et al. Characterization of the interaction between Abeta 1-42 and glyceraldehyde phosphodehydrogenase. J Pept Sci 2008, 14:755-762.
    • (2008) J Pept Sci , vol.14 , pp. 755-762
    • Verdier, Y.1    Foldi, I.2    Sergeant, N.3    Fulop, L.4    Penke, Z.5    Janaky, T.6
  • 36
    • 28744448949 scopus 로고    scopus 로고
    • Amyloid beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease
    • Cumming R.C., Schubert D. Amyloid beta induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease. FASEB J 2005, 19:2060-2062.
    • (2005) FASEB J , vol.19 , pp. 2060-2062
    • Cumming, R.C.1    Schubert, D.2
  • 37
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein
    • Schulze H., Schuler A., Stuber D., Dobeli H., Langen H., Huber G. Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein. J Neurochem 1993, 60:1915-1922.
    • (1993) J Neurochem , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuler, A.2    Stuber, D.3    Dobeli, H.4    Langen, H.5    Huber, G.6
  • 38
    • 84856072360 scopus 로고    scopus 로고
    • Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in alpha-synuclein aggregation
    • Torres-Bugeau C.M., Avila C.L., Raisman-Vozari R., Papy-Garcia D., Itri R., Barbosa L.R., et al. Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in alpha-synuclein aggregation. J Biol Chem 2012, 287:2398-2409.
    • (2012) J Biol Chem , vol.287 , pp. 2398-2409
    • Torres-Bugeau, C.M.1    Avila, C.L.2    Raisman-Vozari, R.3    Papy-Garcia, D.4    Itri, R.5    Barbosa, L.R.6
  • 39
    • 0029898223 scopus 로고    scopus 로고
    • Antibodies to amyloid beta protein (A beta) crossreact with glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
    • Tamaoka A., Endoh R., Shoji S., Takahashi H., Hirokawa K., Teplow D.B., et al. Antibodies to amyloid beta protein (A beta) crossreact with glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Neurobiol Aging 1996, 17:405-414.
    • (1996) Neurobiol Aging , vol.17 , pp. 405-414
    • Tamaoka, A.1    Endoh, R.2    Shoji, S.3    Takahashi, H.4    Hirokawa, K.5    Teplow, D.B.6
  • 40
    • 0028818826 scopus 로고
    • Carboxyl end-specific monoclonal antibodies to amyloid beta protein (A beta) subtypes (A beta 40 and A beta 42(43)) differentiate A beta in senile plaques and amyloid angiopathy in brains of aged cynomolgus monkeys
    • Nakamura S., Tamaoka A., Sawamura N., Shoji S., Nakayama H., Ono F., et al. Carboxyl end-specific monoclonal antibodies to amyloid beta protein (A beta) subtypes (A beta 40 and A beta 42(43)) differentiate A beta in senile plaques and amyloid angiopathy in brains of aged cynomolgus monkeys. Neurosci Lett 1995, 201:151-154.
    • (1995) Neurosci Lett , vol.201 , pp. 151-154
    • Nakamura, S.1    Tamaoka, A.2    Sawamura, N.3    Shoji, S.4    Nakayama, H.5    Ono, F.6
  • 41
    • 0034660602 scopus 로고    scopus 로고
    • Glutamine synthetase, hemoglobin alpha-chain, and macrophage migration inhibitory factor binding to amyloid beta protein: their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation
    • Oyama R., Yamamoto H., Titani K. Glutamine synthetase, hemoglobin alpha-chain, and macrophage migration inhibitory factor binding to amyloid beta protein: their identification in rat brain by a novel affinity chromatography and in Alzheimer's disease brain by immunoprecipitation. Biochim Biophys Acta 2000, 1479:91-102.
    • (2000) Biochim Biophys Acta , vol.1479 , pp. 91-102
    • Oyama, R.1    Yamamoto, H.2    Titani, K.3
  • 42
    • 23244467989 scopus 로고    scopus 로고
    • Identification of synaptic plasma membrane proteins co-precipitated with fibrillar beta-amyloid peptide
    • Verdier Y., Huszar E., Penke B., Penke Z., Woffendin G., Scigelova M., et al. Identification of synaptic plasma membrane proteins co-precipitated with fibrillar beta-amyloid peptide. J Neurochem 2005, 94:617-628.
    • (2005) J Neurochem , vol.94 , pp. 617-628
    • Verdier, Y.1    Huszar, E.2    Penke, B.3    Penke, Z.4    Woffendin, G.5    Scigelova, M.6
  • 43
    • 54549093577 scopus 로고    scopus 로고
    • Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures
    • Naletova I., Schmalhausen E., Kharitonov A., Katrukha A., Saso L., Caprioli A., et al. Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures. Biochim Biophys Acta 2008, 1784:2052-2058.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 2052-2058
    • Naletova, I.1    Schmalhausen, E.2    Kharitonov, A.3    Katrukha, A.4    Saso, L.5    Caprioli, A.6
  • 44
    • 0035145627 scopus 로고    scopus 로고
    • Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts
    • Mazzola J.L., Sirover M.A. Reduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts. J Neurochem 2001, 76:442-449.
    • (2001) J Neurochem , vol.76 , pp. 442-449
    • Mazzola, J.L.1    Sirover, M.A.2
  • 46
    • 70449712602 scopus 로고    scopus 로고
    • Novel roles for GAPDH in cell death and carcinogenesis
    • Colell A., Green D.R., Ricci J.E. Novel roles for GAPDH in cell death and carcinogenesis. Cell Death Differ 2009, 16:1573-1581.
    • (2009) Cell Death Differ , vol.16 , pp. 1573-1581
    • Colell, A.1    Green, D.R.2    Ricci, J.E.3
  • 47
    • 34548845570 scopus 로고    scopus 로고
    • The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress induced aggregation and cell death
    • Nakajima H., Amano W., Fujita A., Fukuhara A., Azuma Y.T., Hata F., et al. The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress induced aggregation and cell death. J Biol Chem 2007, 282:26562-26574.
    • (2007) J Biol Chem , vol.282 , pp. 26562-26574
    • Nakajima, H.1    Amano, W.2    Fujita, A.3    Fukuhara, A.4    Azuma, Y.T.5    Hata, F.6
  • 49
    • 26844433190 scopus 로고    scopus 로고
    • Axonal degeneration induced by targeted expression of mutant human tau in oligodendrocytes of transgenic mice that model glial tauopathies
    • Higuchi M., Zhang B., Forman M.S., Yoshiyama Y., Trojanowski J.Q., Lee V.M. Axonal degeneration induced by targeted expression of mutant human tau in oligodendrocytes of transgenic mice that model glial tauopathies. J Neurosci 2005, 25:9434-9443.
    • (2005) J Neurosci , vol.25 , pp. 9434-9443
    • Higuchi, M.1    Zhang, B.2    Forman, M.S.3    Yoshiyama, Y.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 51
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang Q., Woltjer R.L., Cimino P.J., Pan C., Montine K.S., Zhang J., et al. Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J 2005, 19:869-871.
    • (2005) FASEB J , vol.19 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6
  • 52
    • 47749133771 scopus 로고    scopus 로고
    • Identification of non-Alzheimer's disease tauopathies-related proteins by proteomic analysis
    • Yang G., Wang L., Zhu M., Xu D. Identification of non-Alzheimer's disease tauopathies-related proteins by proteomic analysis. Neurol Res 2008, 30:613-622.
    • (2008) Neurol Res , vol.30 , pp. 613-622
    • Yang, G.1    Wang, L.2    Zhu, M.3    Xu, D.4
  • 54
    • 0035261534 scopus 로고    scopus 로고
    • CSF phosphorylated tau is a possible marker for discriminating Alzheimer's disease from dementia with Lewy bodies. Phospho-Tau International Study Group
    • Parnetti L., Lanari A., Amici S., Gallai V., Vanmechelen E., Hulstaert F., et al. CSF phosphorylated tau is a possible marker for discriminating Alzheimer's disease from dementia with Lewy bodies. Phospho-Tau International Study Group. Neurol Sci 2001, 22:77-78.
    • (2001) Neurol Sci , vol.22 , pp. 77-78
    • Parnetti, L.1    Lanari, A.2    Amici, S.3    Gallai, V.4    Vanmechelen, E.5    Hulstaert, F.6
  • 55
    • 0035997222 scopus 로고    scopus 로고
    • Beta-amyloid (Abeta) protein in cerebrospinal fluid as a biomarker for Alzheimer's disease
    • Andreasen N., Blennow K. Beta-amyloid (Abeta) protein in cerebrospinal fluid as a biomarker for Alzheimer's disease. Peptides 2002, 23:1205-1214.
    • (2002) Peptides , vol.23 , pp. 1205-1214
    • Andreasen, N.1    Blennow, K.2


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