메뉴 건너뛰기




Volumn 2016, Issue , 2016, Pages

The microtubule-associated protein Tau and its relevance for pancreatic beta cells

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; GLYCOGEN SYNTHASE KINASE 3BETA; INSULIN; MICROTUBULE ASSOCIATED PROTEIN 2; MICROTUBULE ASSOCIATED PROTEIN 4; MOLECULAR MOTOR; PHOSPHATIDYLINOSITOL 3 KINASE; TAU PROTEIN; WORTMANNIN; ISOPROTEIN; MAPT PROTEIN, HUMAN;

EID: 84957061064     PISSN: 23146745     EISSN: 23146753     Source Type: Journal    
DOI: 10.1155/2016/1964634     Document Type: Article
Times cited : (28)

References (62)
  • 2
    • 79952279828 scopus 로고    scopus 로고
    • DAXX/ATRX, MEN1, and mTOR pathway genes are frequently altered in pancreatic neuroendocrine tumors
    • Y. Jiao, C. Shi, B. H. Edil et al. , "DAXX/ATRX, MEN1, and mTOR pathway genes are frequently altered in pancreatic neuroendocrine tumors," Science, vol. 331, no. 6021, pp. 1199-1203, 2011.
    • (2011) Science , vol.331 , Issue.6021 , pp. 1199-1203
    • Jiao, Y.1    Shi, C.2    Edil, B.H.3
  • 4
    • 0025219162 scopus 로고
    • Microtubule MAPping
    • D. W. Cleveland, "Microtubule MAPping," Cell, vol. 60, no. 5, pp. 701-702, 1990.
    • (1990) Cell , vol.60 , Issue.5 , pp. 701-702
    • Cleveland, D.W.1
  • 5
    • 0033568402 scopus 로고    scopus 로고
    • Microtubule-binding property of microtubule-associated protein differs from that of microtubule-associated protein 4 and tau
    • K. Tokuraku, M. Katsuki, T. Matui, T. Kuroya, and S. Kotani, "Microtubule-binding property of microtubule-associated protein differs from that of microtubule-associated protein 4 and tau," European Journal of Biochemistry, vol. 264, no. 3, pp. 996-1001, 1999.
    • (1999) European Journal of Biochemistry , vol.264 , Issue.3 , pp. 996-1001
    • Tokuraku, K.1    Katsuki, M.2    Matui, T.3    Kuroya, T.4    Kotani, S.5
  • 6
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • D. W. Cleveland, S.-Y. Hwo, and M. W. Kirschner, "Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin," Journal of Molecular Biology, vol. 116, no. 2, pp. 207-225, 1977.
    • (1977) Journal of Molecular Biology , vol.116 , Issue.2 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.-Y.2    Kirschner, M.W.3
  • 7
    • 0022896901 scopus 로고
    • Tau protein function in living cells
    • D. G. Drubin and M. W. Kirschner, "Tau protein function in living cells, The Journal of Cell Biology, vol. 103, no. 6, part 2, pp. 2739-2746, 1986.
    • (1986) The Journal of Cell Biology , vol.103 , Issue.6 , pp. 2739-2746
    • Drubin, D.G.1    Kirschner, M.W.2
  • 8
    • 0025098891 scopus 로고
    • Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons
    • A. Caceres and K. S. Kosik, "Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons," Nature, vol. 343, no. 6257, pp. 461-463, 1990.
    • (1990) Nature , vol.343 , Issue.6257 , pp. 461-463
    • Caceres, A.1    Kosik, K.S.2
  • 9
    • 69449091821 scopus 로고    scopus 로고
    • Basic mechanisms for recognition and transport of synaptic cargos
    • article 25
    • M. A. Schlager and C. C. Hoogenraad, "Basic mechanisms for recognition and transport of synaptic cargos," Molecular Brain, vol. 2, no. 1, article 25, 2009.
    • (2009) Molecular Brain , vol.2 , Issue.1
    • Schlager, M.A.1    Hoogenraad, C.C.2
  • 10
    • 0015294789 scopus 로고
    • The stimulus-secretion coupling of glucose-induced insulin release. VII. A proposed site of action for adenosine-3, 5'-cyclic monophosphate
    • G. R. Brisson, F. Malaisse-Lagae, and W. J. Malaisse, "The stimulus-secretion coupling of glucose-induced insulin release. VII. A proposed site of action for adenosine-3, 5-cyclic monophosphate," The Journal of Clinical Investigation, vol. 51, no. 2, pp. 232-241, 1972.
    • (1972) The Journal of Clinical Investigation , vol.51 , Issue.2 , pp. 232-241
    • Brisson, G.R.1    Malaisse-Lagae, F.2    Malaisse, W.J.3
  • 12
    • 0016760397 scopus 로고
    • Dynamics of insulin release and microtubular-microfilamentous system. VII. Do microfilaments provide the motive force for the translocation and extrusion of beta granules?
    • E. Van Obberghen, G. Somers, G. Devis et al. , "Dynamics of insulin release and microtubular-microfilamentous system. VII. Do microfilaments provide the motive force for the translocation and extrusion of beta granules?" Diabetes, vol. 24, no. 10, pp. 892-901, 1975.
    • (1975) Diabetes , vol.24 , Issue.10 , pp. 892-901
    • Van Obberghen, E.1    Somers, G.2    Devis, G.3
  • 13
    • 0018743708 scopus 로고
    • Role of microtubules in the synthesis, conversion, and release of (pro)insulin. A biochemical and radioautographic study in rat islets
    • F. Malaisse-Lagae, M. Amherdt, M. Ravazzola et al. , "Role of microtubules in the synthesis, conversion, and release of (pro)insulin. A biochemical and radioautographic study in rat islets," The Journal of Clinical Investigation, vol. 63, no. 6, pp. 1284-1296, 1979.
    • (1979) The Journal of Clinical Investigation , vol.63 , Issue.6 , pp. 1284-1296
    • Malaisse-Lagae, F.1    Amherdt, M.2    Ravazzola, M.3
  • 14
    • 0022494874 scopus 로고
    • The cytoskeleton and insulin secretion
    • S. L. Howell and M. Tyhurst, "The cytoskeleton and insulin secretion," Diabetes/Metabolism Reviews, vol. 2, no. 1-2, pp. 107-123, 1986.
    • (1986) Diabetes/Metabolism Reviews , vol.2 , Issue.1-2 , pp. 107-123
    • Howell, S.L.1    Tyhurst, M.2
  • 15
    • 0029161127 scopus 로고
    • In situ localization with digoxigenin-labelled probes of tau-related mRNAs in the rat pancreas
    • P. Neuville, M. T. Vanier, L. Michalik, and J. F. Launay, "In situ localization with digoxigenin-labelled probes of tau-related mRNAs in the rat pancreas," The Histochemical Journal, vol. 27, no. 8, pp. 565-574, 1995.
    • (1995) The Histochemical Journal , vol.27 , Issue.8 , pp. 565-574
    • Neuville, P.1    Vanier, M.T.2    Michalik, L.3    Launay, J.F.4
  • 18
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • C. Duyckaerts, B. Delatour, and M.-C. Potier, "Classification and basic pathology of Alzheimer disease," Acta Neuropathologica, vol. 118, no. 1, pp. 5-36, 2009.
    • (2009) Acta Neuropathologica , vol.118 , Issue.1 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.-C.3
  • 19
    • 77954955774 scopus 로고    scopus 로고
    • Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes
    • J. Miklossy, H. Qing, A. Radenovic et al. , "Beta amyloid and hyperphosphorylated tau deposits in the pancreas in type 2 diabetes," Neurobiology of Aging, vol. 31, no. 9, pp. 1503-1515, 2010.
    • (2010) Neurobiology of Aging , vol.31 , Issue.9 , pp. 1503-1515
    • Miklossy, J.1    Qing, H.2    Radenovic, A.3
  • 20
    • 77949500684 scopus 로고    scopus 로고
    • Expression of TAU in insulin-secreting cells and its interaction with the calcium-binding protein secretagogin
    • M. Maj, W. Gartner, A. Ilhan, D. Neziri, J. Attems, and L. Wagner, "Expression of TAU in insulin-secreting cells and its interaction with the calcium-binding protein secretagogin," Journal of Endocrinology, vol. 205, no. 1, pp. 25-36, 2010.
    • (2010) Journal of Endocrinology , vol.205 , Issue.1 , pp. 25-36
    • Maj, M.1    Gartner, W.2    Ilhan, A.3    Neziri, D.4    Attems, J.5    Wagner, L.6
  • 21
    • 0014599508 scopus 로고
    • Islet-cell metabolism during insulin release. Effects of glucose, citrate, octanoate, tolbutamide, glucagon and theophylline
    • W. Montague and K. W. Taylor, "Islet-cell metabolism during insulin release. Effects of glucose, citrate, octanoate, tolbutamide, glucagon and theophylline," Biochemical Journal, vol. 115, no. 2, pp. 257-262, 1969.
    • (1969) Biochemical Journal , vol.115 , Issue.2 , pp. 257-262
    • Montague, W.1    Taylor, K.W.2
  • 22
    • 0015351852 scopus 로고
    • Studies on the secretion of newly synthesized proinsulin and insulin fromisolated rat islets of Langerhans, the
    • H. Sando, J. Borg, and D. F. Steiner, "Studies on the secretion of newly synthesized proinsulin and insulin fromisolated rat islets of Langerhans, The Journal of Clinical Investigation, vol. 51, no. 6, pp. 1476-1485, 1972.
    • (1972) Journal of Clinical Investigation , vol.51 , Issue.6 , pp. 1476-1485
    • Sando, H.1    Borg, J.2    Steiner, D.F.3
  • 23
    • 0016803496 scopus 로고
    • Investigations on isolated islets of Langerhans in vitro. Influence of temperature changes during preparation on some parameters of insulin metabolism
    • H. J. Hahn, H. Jahr, K. D. Kohnert, and H. Zuehlke, "Investigations on isolated islets of Langerhans in vitro. Influence of temperature changes during preparation on some parameters of insulin metabolism," Hormone Research, vol. 6, no. 3, pp. 169-176, 1975.
    • (1975) Hormone Research , vol.6 , Issue.3 , pp. 169-176
    • Hahn, H.J.1    Jahr, H.2    Kohnert, K.D.3    Zuehlke, H.4
  • 25
    • 0027233478 scopus 로고
    • Murine insulinoma cell line with normal glucoseregulated insulin secretion
    • S. Efrat, M. Leiser, M. Surana, M. Tal, D. Fusco-Demane, and N. Fleischer, "Murine insulinoma cell line with normal glucoseregulated insulin secretion," Diabetes, vol. 42, no. 6, pp. 901-907, 1993.
    • (1993) Diabetes , vol.42 , Issue.6 , pp. 901-907
    • Efrat, S.1    Leiser, M.2    Surana, M.3    Tal, M.4    Fusco-Demane, D.5    Fleischer, N.6
  • 26
    • 78349238941 scopus 로고    scopus 로고
    • Pancreatic beta cell lines and their applications in diabetes mellitus research
    • M. Skelin, M. Rupnik, and A. Cencic, "Pancreatic beta cell lines and their applications in diabetes mellitus research," ALTEX, vol. 27, no. 2, pp. 105-113, 2010.
    • (2010) ALTEX , vol.27 , Issue.2 , pp. 105-113
    • Skelin, M.1    Rupnik, M.2    Cencic, A.3
  • 27
    • 0027424235 scopus 로고
    • Insulin secretion, insulin content and glucose phosphorylation in RINm5F insulinoma cells after transfection with human GLUT2 glucose-transporter cDNA
    • M. Tiedge, M. Hohne, and S. Lenzen, "Insulin secretion, insulin content and glucose phosphorylation in RINm5F insulinoma cells after transfection with human GLUT2 glucose-transporter cDNA," Biochemical Journal, vol. 296, no. 1, pp. 113-118, 1993.
    • (1993) Biochemical Journal , vol.296 , Issue.1 , pp. 113-118
    • Tiedge, M.1    Hohne, M.2    Lenzen, S.3
  • 28
    • 0022129515 scopus 로고
    • Direct identification of prohormone conversion site in insulin-secreting cells
    • L. Orci, M. Ravazzola, M. Amherdt, O. Madsen, J.-D. Vassalli, and A. Perrelet, "Direct identification of prohormone conversion site in insulin-secreting cells," Cell, vol. 42, no. 2, pp. 671-681, 1985.
    • (1985) Cell , vol.42 , Issue.2 , pp. 671-681
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Vassalli, J.-D.5    Perrelet, A.6
  • 29
    • 0036678101 scopus 로고    scopus 로고
    • Severe block in processing of proinsulin to insulin accompanied by elevation of des-64, 65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3
    • X. Zhu, L. Orci, R. Carroll, C. Norrbom, M. Ravazzola, and D. F. Steiner, "Severe block in processing of proinsulin to insulin accompanied by elevation of des-64, 65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3," Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 16, pp. 10299-10304, 2002.
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.16 , pp. 10299-10304
    • Zhu, X.1    Orci, L.2    Carroll, R.3    Norrbom, C.4    Ravazzola, M.5    Steiner, D.F.6
  • 30
    • 0037024694 scopus 로고    scopus 로고
    • Ca2+-dependent dephosphorylation of kinesin heavy chain onβ-granules in pancreaticβ-cells: Implications for regulatedβ-granule transport and insulin exocytosis
    • M. J. Donelan, G. Morfini, R. Julyan et al. , "Ca2+-dependent dephosphorylation of kinesin heavy chain oβ-granules in pancreatic β-cells: implications for regulated β-granule transport and insulin exocytosis, The Journal of Biological Chemistry, vol. 277, no. 27, pp. 24232-24242, 2002.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24232-24242
    • Donelan, M.J.1    Morfini, G.2    Julyan, R.3
  • 31
    • 0345580607 scopus 로고    scopus 로고
    • Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimers disease
    • J.-P. Brion, G. Trempdagger, and J.-N. Octavedagger, "Transgenic expression of the shortest human tau affects its compartmentalization and its phosphorylation as in the pretangle stage of Alzheimers disease," American Journal of Pathology, vol. 154, no. 1, pp. 255-270, 1999.
    • (1999) American Journal of Pathology , vol.154 , Issue.1 , pp. 255-270
    • Brion, J.-P.1    Trempdagger, G.2    Octavedagger, J.-N.3
  • 32
    • 0032786370 scopus 로고    scopus 로고
    • Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein
    • K. Spittaels, C. Van Den Haute, J. Van Dorpe et al. , "Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein," American Journal of Pathology, vol. 155, no. 6, pp. 2153-2165, 1999.
    • (1999) American Journal of Pathology , vol.155 , Issue.6 , pp. 2153-2165
    • Spittaels, K.1    Haute Den C.Van2    Van Dorpe, J.3
  • 33
    • 0342803685 scopus 로고    scopus 로고
    • Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein
    • A. Probst, J. Gotz, K. H. Wiederhold et al. , "Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein," Acta Neuropathologica, vol. 99, no. 5, pp. 469-481, 2000.
    • (2000) Acta Neuropathologica , vol.99 , Issue.5 , pp. 469-481
    • Probst, A.1    Gotz, J.2    Wiederhold, K.H.3
  • 34
    • 58749088408 scopus 로고    scopus 로고
    • Tau isoform regulation is region-and cell-specific in mouse brain
    • P. McMillan, E. Korvatska, P. Poorkaj et al. , "Tau isoform regulation is region-and cell-specific in mouse brain," Journal of Comparative Neurology, vol. 511, no. 6, pp. 788-803, 2008.
    • (2008) Journal of Comparative Neurology , vol.511 , Issue.6 , pp. 788-803
    • McMillan, P.1    Korvatska, E.2    Poorkaj, P.3
  • 35
    • 79959256140 scopus 로고    scopus 로고
    • Identification of oncostatin M as a STAT5-dependent mediator of bone marrow remodeling in KIT D816V-positive systemic mastocytosis
    • G. Hoermann, S. Cerny-Reiterer, A. Perne et al. , "Identification of oncostatin M as a STAT5-dependent mediator of bone marrow remodeling in KIT D816V-positive systemic mastocytosis," The American Journal of Pathology, vol. 178, no. 5, pp. 2344-2356, 2011.
    • (2011) The American Journal of Pathology , vol.178 , Issue.5 , pp. 2344-2356
    • Hoermann, G.1    Cerny-Reiterer, S.2    Perne, A.3
  • 36
    • 0024433060 scopus 로고
    • Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: Evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau
    • A. Ferreira, J. Busciglio, and A. Caceres, "Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau," Developmental Brain Research, vol. 49, no. 2, pp. 215-228, 1989.
    • (1989) Developmental Brain Research , vol.49 , Issue.2 , pp. 215-228
    • Ferreira, A.1    Busciglio, J.2    Caceres, A.3
  • 37
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • D. N. Drechsel, A. A. Hyman, M. H. Cobb, and M. W. Kirschner, "Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau," Molecular Biology of the Cell, vol. 3, no. 10, pp. 1141-1154, 1992.
    • (1992) Molecular Biology of the Cell , vol.3 , Issue.10 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 38
    • 0031801129 scopus 로고    scopus 로고
    • Expression of specific tau exons in normal and tumoral pancreatic acinar cells
    • M.-T. Vanier, P. Neuville, L. Michalik, and J.-F. Launay, "Expression of specific tau exons in normal and tumoral pancreatic acinar cells," Journal of Cell Science, vol. 111, part 10, pp. 1419-1432, 1998.
    • (1998) Journal of Cell Science , vol.111 , pp. 1419-1432
    • Vanier, M.-T.1    Neuville, P.2    Michalik, L.3    Launay, J.-F.4
  • 39
    • 0025600995 scopus 로고
    • Expression of separate isoforms of human tau protein: Correlation with the tau pattern in brain and effects on tubulin polymerization
    • M. Goedert and R. Jakes, "Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization," The EMBO Journal, vol. 9, no. 13, pp. 4225-4230, 1990.
    • (1990) The EMBO Journal , vol.9 , Issue.13 , pp. 4225-4230
    • Goedert, M.1    Jakes, R.2
  • 40
    • 0030048118 scopus 로고    scopus 로고
    • Distribution of isoforms of the microtubule-associated protein tau in grey and white matter areas of human brain: A two-dimensional gelelectrophoretic analysis
    • C. Janke, M. Holzer, J. Klose, and T. Arendt, "Distribution of isoforms of the microtubule-associated protein tau in grey and white matter areas of human brain: a two-dimensional gelelectrophoretic analysis," FEBS Letters, vol. 379, no. 3, pp. 222-226, 1996.
    • (1996) FEBS Letters , vol.379 , Issue.3 , pp. 222-226
    • Janke, C.1    Holzer, M.2    Klose, J.3    Arendt, T.4
  • 42
    • 0037299017 scopus 로고    scopus 로고
    • Microtubule associated protein tau binds to double-stranded but not single-stranded DNA
    • Q. Hua, R.-Q. He, N. Haque et al. , "Microtubule associated protein tau binds to double-stranded but not single-stranded DNA," Cellular and Molecular Life Sciences, vol. 60, no. 2, pp. 413-421, 2003.
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.2 , pp. 413-421
    • Hua, Q.1    He, R.-Q.2    Haque, N.3
  • 43
    • 0033214612 scopus 로고    scopus 로고
    • Regulation of glycogen synthase in rat hepatocytes. Evidence for multiple signaling pathways
    • L. Lavoie, C. J. Band, M. Kong, J. J. M. Bergeron, and B. I. Posner, "Regulation of glycogen synthase in rat hepatocytes. Evidence for multiple signaling pathways," The Journal of Biological Chemistry, vol. 274, no. 40, pp. 28279-28285, 1999.
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.40 , pp. 28279-28285
    • Lavoie, L.1    Band, C.J.2    Kong, M.3    Bergeron, J.J.M.4    Posner, B.I.5
  • 44
    • 0028316882 scopus 로고
    • Sense and antisense transfection analysis of tau function: Tau influences net microtubule assembly, neurite outgrowth and neuritic stability
    • B. Esmaeli-Azad, J. H. McCarty, and S. C. Feinstein, "Sense and antisense transfection analysis of tau function: tau influences net microtubule assembly, neurite outgrowth and neuritic stability," Journal of Cell Science, vol. 107, part 4, pp. 869-879, 1994.
    • (1994) Journal of Cell Science , vol.107 , pp. 869-879
    • Esmaeli-Azad, B.1    McCarty, J.H.2    Feinstein, S.C.3
  • 46
    • 0031446859 scopus 로고    scopus 로고
    • Transneuronal degeneration in the spread of Alzheimers disease pathology: Immunohistochemical evidence for the transmission of tau hyperphosphorylation
    • J. H. Su, G. Deng, and C. W. Cotman, "Transneuronal degeneration in the spread of Alzheimers disease pathology: immunohistochemical evidence for the transmission of tau hyperphosphorylation," Neurobiology of Disease, vol. 4, no. 5, pp. 365-375, 1997.
    • (1997) Neurobiology of Disease , vol.4 , Issue.5 , pp. 365-375
    • Su, J.H.1    Deng, G.2    Cotman, C.W.3
  • 47
    • 0033792070 scopus 로고    scopus 로고
    • Structural and functional implications of tau hyperphosphorylation: Information fromphosphorylationmimicking mutated tau proteins
    • J. Eidenmuller, T. Fath, A. Hellwig, J. Reed, E. Sontag, and R. Brandt, "Structural and functional implications of tau hyperphosphorylation: information fromphosphorylationmimicking mutated tau proteins," Biochemistry, vol. 39, no. 43, pp. 13166-13175, 2000.
    • (2000) Biochemistry , vol.39 , Issue.43 , pp. 13166-13175
    • Eidenmuller, J.1    Fath, T.2    Hellwig, A.3    Reed, J.4    Sontag, E.5    Brandt, R.6
  • 49
    • 0028210962 scopus 로고
    • Abnormally phosphorylated tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat
    • H. Braak, E. Braak, and M. Strothjohann, "Abnormally phosphorylated tau protein related to the formation of neurofibrillary tangles and neuropil threads in the cerebral cortex of sheep and goat," Neuroscience Letters, vol. 171, no. 1-2, pp. 1-4, 1994.
    • (1994) Neuroscience Letters , vol.171 , Issue.1-2 , pp. 1-4
    • Braak, H.1    Braak, E.2    Strothjohann, M.3
  • 50
    • 0031633953 scopus 로고    scopus 로고
    • Mechanisms of neurofibrillary degeneration and the formation of neurofibrillary tangles
    • K. Iqbal, A. D. C. Alonso, C.-X. Gong et al. , "Mechanisms of neurofibrillary degeneration and the formation of neurofibrillary tangles," Journal of Neural TransmissionSupplement, vol. 53, pp. 169-180, 1998.
    • (1998) Journal of Neural TransmissionSupplement , vol.53 , pp. 169-180
    • Iqbal, K.1    Alonso, A.D.C.2    Gong, C.-X.3
  • 51
    • 36448936053 scopus 로고    scopus 로고
    • Common pathological processes in Alzheimer disease and type 2 diabetes: A review
    • L. Li and C. Holscher, "Common pathological processes in Alzheimer disease and type 2 diabetes: a review," Brain Research Reviews, vol. 56, no. 2, pp. 384-402, 2007.
    • (2007) Brain Research Reviews , vol.56 , Issue.2 , pp. 384-402
    • Li, L.1    Holscher, C.2
  • 52
    • 64249129005 scopus 로고    scopus 로고
    • Insulin resistance and amyloidogenesis as common molecular foundation for type 2 diabetes and Alzheimers disease
    • W.-Q. Zhao and M. Townsend, "Insulin resistance and amyloidogenesis as common molecular foundation for type 2 diabetes and Alzheimers disease," Biochimica et Biophysica Acta, vol. 1792, no. 5, pp. 482-496, 2009.
    • (2009) Biochimica et Biophysica Acta , vol.1792 , Issue.5 , pp. 482-496
    • Zhao, W.-Q.1    Townsend, M.2
  • 53
    • 67349112388 scopus 로고    scopus 로고
    • Common features between diabetes mellitus and Alzheimers disease
    • J. Gotz, L. M. Ittner, and Y.-A. Lim, "Common features between diabetes mellitus and Alzheimers disease," Cellular and Molecular Life Sciences, vol. 66, no. 8, pp. 1321-1325, 2009.
    • (2009) Cellular and Molecular Life Sciences , vol.66 , Issue.8 , pp. 1321-1325
    • Gotz, J.1    Ittner, L.M.2    Lim, Y.-A.3
  • 54
    • 79952703206 scopus 로고    scopus 로고
    • Increased expression of three-repeat isoforms of tau contributes to tau pathology in a rat model of chronic type 2 diabetes
    • H. J. Jung, S. S. Park, J. O. Mok, T. K. Lee, C. S. Park, and S. A. Park, "Increased expression of three-repeat isoforms of tau contributes to tau pathology in a rat model of chronic type 2 diabetes," Experimental Neurology, vol. 228, no. 2, pp. 232-241, 2011.
    • (2011) Experimental Neurology , vol.228 , Issue.2 , pp. 232-241
    • Jung, H.J.1    Park, S.S.2    Mok, J.O.3    Lee, T.K.4    Park, C.S.5    Park, S.A.6
  • 55
    • 79751481634 scopus 로고    scopus 로고
    • MAPT isoforms: Differential transcriptional profiles related to 3R and 4R splice variants
    • S. Chen, K. Townsend, T. E. Goldberg, P. Davies, and C. Conejero-Goldberg, "MAPT isoforms: differential transcriptional profiles related to 3R and 4R splice variants," Journal of Alzheimers Disease, vol. 22, no. 4, pp. 1313-1329, 2010.
    • (2010) Journal of Alzheimers Disease , vol.22 , Issue.4 , pp. 1313-1329
    • Chen, S.1    Townsend, K.2    Goldberg, T.E.3    Davies, P.4    Conejero-Goldberg, C.5
  • 56
    • 77956542660 scopus 로고    scopus 로고
    • Three repeat isoforms of tau inhibit assembly of four repeat tau filaments
    • Article ID e10810
    • S. J. Adams, M. A. DeTure, M. McBride, D. W. Dickson, and L. Petrucelli, "Three repeat isoforms of tau inhibit assembly of four repeat tau filaments," PLoS ONE, vol. 5, no. 5, Article ID e10810, 2010.
    • (2010) PLoS ONE , vol.5 , Issue.5
    • Adams, S.J.1    DeTure, M.A.2    McBride, M.3    Dickson, D.W.4    Petrucelli, L.5
  • 57
    • 48249148310 scopus 로고    scopus 로고
    • Tau exon 10 alternative splicing and tauopathies
    • article 8
    • F. Liu and C.-X. Gong, "Tau exon 10 alternative splicing and tauopathies," Molecular Neurodegeneration, vol. 3, no. 1, article 8, 2008.
    • (2008) Molecular Neurodegeneration , vol.3 , Issue.1
    • Liu, F.1    Gong, C.-X.2
  • 58
    • 33746074397 scopus 로고    scopus 로고
    • Peri-nuclear clustering of mitochondria is triggered during aluminum maltolate induced apoptosis
    • D. A. Dewitt, J. A. Hurd, N. Fox et al. , "Peri-nuclear clustering of mitochondria is triggered during aluminum maltolate induced apoptosis," Journal of Alzheimers Disease, vol. 9, no. 2, pp. 195-205, 2006.
    • (2006) Journal of Alzheimers Disease , vol.9 , Issue.2 , pp. 195-205
    • Dewitt, D.A.1    Hurd, J.A.2    Fox, N.3
  • 60
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimers disease, the
    • A. Ebneth, R. Godemann, K. Stamer et al. , "Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimers disease, The Journal of Cell Biology, vol. 143, no. 3, pp. 777-794, 1998.
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3
  • 61
    • 1342347848 scopus 로고    scopus 로고
    • Stable-tau overexpression in human neuroblastoma cells: An open door for explaining neuronal death in tauopathies
    • P. Delobel, C. Mailliot, M. Hamdane et al. , "Stable-tau overexpression in human neuroblastoma cells: an open door for explaining neuronal death in tauopathies," Annals of the New York Academy of Sciences, vol. 1010, pp. 623-634, 2003.
    • (2003) Annals of the New York Academy of Sciences , vol.1010 , pp. 623-634
    • Delobel, P.1    Mailliot, C.2    Hamdane, M.3
  • 62
    • 2342425038 scopus 로고    scopus 로고
    • Role of tau phosphorylation by glycogen synthase kinase-3β in the regulation of organelle transport
    • Y. Tatebayashi, N. Haque, Y.-C. Tung, K. Iqbal, and I. Grundke-Iqbal, "Role of tau phosphorylation by glycogen synthase kinase-3β in the regulation of organelle transport," Journal of Cell Science, vol. 117, no. 9, pp. 1653-1663, 2004.
    • (2004) Journal of Cell Science , vol.117 , Issue.9 , pp. 1653-1663
    • Tatebayashi, Y.1    Haque, N.2    Tung, Y.-C.3    Iqbal, K.4    Grundke-Iqbal, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.