메뉴 건너뛰기




Volumn 38, Issue , 2016, Pages 90-96

Mitochondria-associated ER membranes and Alzheimer disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; TAU PROTEIN; SECRETASE;

EID: 84969801217     PISSN: 0959437X     EISSN: 18790380     Source Type: Journal    
DOI: 10.1016/j.gde.2016.04.006     Document Type: Review
Times cited : (92)

References (72)
  • 2
    • 44849083256 scopus 로고    scopus 로고
    • What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease?
    • Armstrong R.A., Lantos P.L., Cairns N.J. What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease?. Neuropathology 2008, 28:351-365.
    • (2008) Neuropathology , vol.28 , pp. 351-365
    • Armstrong, R.A.1    Lantos, P.L.2    Cairns, N.J.3
  • 3
    • 0035997249 scopus 로고    scopus 로고
    • Senile plaque composition and posttranslational modification of amyloid-β peptide and associated proteins
    • Atwood C.S., Martins R.N., Smith M.A., Perry G. Senile plaque composition and posttranslational modification of amyloid-β peptide and associated proteins. Peptides 2002, 23:1343-1350.
    • (2002) Peptides , vol.23 , pp. 1343-1350
    • Atwood, C.S.1    Martins, R.N.2    Smith, M.A.3    Perry, G.4
  • 5
    • 84863504256 scopus 로고    scopus 로고
    • Apolipoprotein E and apolipoprotein E receptors: normal biology and roles in Alzheimer disease
    • Holtzman D.M., Herz J., Bu G. Apolipoprotein E and apolipoprotein E receptors: normal biology and roles in Alzheimer disease. Cold Spring Harb Perspect Biol 2012, 2:a006312.
    • (2012) Cold Spring Harb Perspect Biol , vol.2 , pp. a006312
    • Holtzman, D.M.1    Herz, J.2    Bu, G.3
  • 6
    • 77953286012 scopus 로고    scopus 로고
    • Aβ-independent roles of apolipoprotein E4 in the pathogenesis of Alzheimer's disease
    • Huang Y. Aβ-independent roles of apolipoprotein E4 in the pathogenesis of Alzheimer's disease. Trends Mol Med 2010, 16:287-294.
    • (2010) Trends Mol Med , vol.16 , pp. 287-294
    • Huang, Y.1
  • 7
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992, 256:184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 8
    • 77956203927 scopus 로고    scopus 로고
    • Is Alzheimer's disease a disorder of mitochondria-associated membranes?
    • Schon E.A., Area-Gomez E. Is Alzheimer's disease a disorder of mitochondria-associated membranes?. J Alzheimers Dis 2010, 20:S281-S292.
    • (2010) J Alzheimers Dis , vol.20 , pp. S281-S292
    • Schon, E.A.1    Area-Gomez, E.2
  • 9
    • 84875599536 scopus 로고    scopus 로고
    • Mitochondria-associated E.R. membranes in Alzheimer disease
    • Schon E.A., Area-Gomez E. Mitochondria-associated E.R. membranes in Alzheimer disease. Mol Cell Neurosci 2013, 55:26-36.
    • (2013) Mol Cell Neurosci , vol.55 , pp. 26-36
    • Schon, E.A.1    Area-Gomez, E.2
  • 10
    • 58149220667 scopus 로고    scopus 로고
    • Cholesterol in Alzheimer's disease: unresolved questions
    • Stefani M., Liguri G. Cholesterol in Alzheimer's disease: unresolved questions. Curr Alzheimer Res 2009, 6:15-29.
    • (2009) Curr Alzheimer Res , vol.6 , pp. 15-29
    • Stefani, M.1    Liguri, G.2
  • 11
    • 76849108962 scopus 로고    scopus 로고
    • Fatty acid composition of frontal, temporal and parietal neocortex in the normal human brain and in Alzheimer's disease
    • Fraser T., Tayler H., Love S. Fatty acid composition of frontal, temporal and parietal neocortex in the normal human brain and in Alzheimer's disease. Neurochem Res 2010, 35:503-513.
    • (2010) Neurochem Res , vol.35 , pp. 503-513
    • Fraser, T.1    Tayler, H.2    Love, S.3
  • 12
    • 0023737618 scopus 로고
    • Glucose metabolism as the site of the primary abnormality in early-onset dementia of Alzheimer type?
    • Hoyer S., Oesterreich K., Wagner O. Glucose metabolism as the site of the primary abnormality in early-onset dementia of Alzheimer type?. J Neurol 1988, 235:143-148.
    • (1988) J Neurol , vol.235 , pp. 143-148
    • Hoyer, S.1    Oesterreich, K.2    Wagner, O.3
  • 13
    • 67650072530 scopus 로고    scopus 로고
    • Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease
    • Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K., Gong C.X. Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease. Brain 2009, 132:1820-1832.
    • (2009) Brain , vol.132 , pp. 1820-1832
    • Liu, F.1    Shi, J.2    Tanimukai, H.3    Gu, J.4    Gu, J.5    Grundke-Iqbal, I.6    Iqbal, K.7    Gong, C.X.8
  • 15
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny I., Mattson M.P. Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci 2008, 31:454-463.
    • (2008) Trends Neurosci , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 16
    • 64349099993 scopus 로고    scopus 로고
    • The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease
    • Wang X., Su B., Zheng L., Perry G., Smith M.A., Zhu X. The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease. J Neurochem 2009, 109:153-159.
    • (2009) J Neurochem , vol.109 , pp. 153-159
    • Wang, X.1    Su, B.2    Zheng, L.3    Perry, G.4    Smith, M.A.5    Zhu, X.6
  • 17
    • 84927758518 scopus 로고    scopus 로고
    • Mitochondrial genetics and disease
    • Area-Gomez E., Schon E.A. Mitochondrial genetics and disease. J Child Neurol 2014, 29:1208-1215.
    • (2014) J Child Neurol , vol.29 , pp. 1208-1215
    • Area-Gomez, E.1    Schon, E.A.2
  • 20
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM)
    • Raturi A., Simmen T. Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM). Biochim Biophys Acta 2013, 1833:213-224.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 21
    • 0027973135 scopus 로고
    • A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins
    • Rusinol A.E., Cui Z., Chen M.H., Vance J.E. A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J Biol Chem 1994, 269:27494-27502.
    • (1994) J Biol Chem , vol.269 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 22
    • 0031552936 scopus 로고    scopus 로고
    • Phosphatidylethanolamine N-methyltransferase from liver
    • Vance D.E., Walkey C.J., Cui Z. Phosphatidylethanolamine N-methyltransferase from liver. Biochim Biophys Acta 1997, 1348:142-150.
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 142-150
    • Vance, D.E.1    Walkey, C.J.2    Cui, Z.3
  • 23
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes
    • Stone S.J., Vance J.E. Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes. J Biol Chem 2000, 275:34534-34540.
    • (2000) J Biol Chem , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 24
    • 84921929741 scopus 로고    scopus 로고
    • Mitochondria-associated endoplasmic reticulum membrane (MAM) regulates steroidogenic activity via steroidogenic acute regulatory protein (StAR)-voltage-dependent anion channel 2 (VDAC2) interaction
    • Prasad M., Kaur J., Pawlak K.J., Bose M., Whittal R.M., Bose H.S. Mitochondria-associated endoplasmic reticulum membrane (MAM) regulates steroidogenic activity via steroidogenic acute regulatory protein (StAR)-voltage-dependent anion channel 2 (VDAC2) interaction. J Biol Chem 2015, 290:2604-2616.
    • (2015) J Biol Chem , vol.290 , pp. 2604-2616
    • Prasad, M.1    Kaur, J.2    Pawlak, K.J.3    Bose, M.4    Whittal, R.M.5    Bose, H.S.6
  • 27
    • 34547117903 scopus 로고    scopus 로고
    • Fatty acid transport protein 4 is the principal very long chain fatty acyl-CoA synthetase in skin fibroblasts
    • Jia W., Moulson C.L., Pei Z., Miner J.H., Watkins P.A. Fatty acid transport protein 4 is the principal very long chain fatty acyl-CoA synthetase in skin fibroblasts. J Biol Chem 2007, 282:20573-20583.
    • (2007) J Biol Chem , vol.282 , pp. 20573-20583
    • Jia, W.1    Moulson, C.L.2    Pei, Z.3    Miner, J.H.4    Watkins, P.A.5
  • 29
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito O.M., Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008, 456:605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 33
    • 84911899819 scopus 로고    scopus 로고
    • Amyloid-β peptides are generated in mitochondria-associated endoplasmic reticulum membranes
    • Schreiner B., Hedskog L., Wiehager B., Ankarcrona M. Amyloid-β peptides are generated in mitochondria-associated endoplasmic reticulum membranes. J Alzheimers Dis 2015, 43:369-374.
    • (2015) J Alzheimers Dis , vol.43 , pp. 369-374
    • Schreiner, B.1    Hedskog, L.2    Wiehager, B.3    Ankarcrona, M.4
  • 34
    • 53549129483 scopus 로고    scopus 로고
    • Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
    • Du H., Guo L., Fang F., Chen D., Sosunov A.A., McKhann G.M., Yan Y., Wang C., Zhang H., Molkentin J.D., et al. Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat Med 2008, 14:1097-1105.
    • (2008) Nat Med , vol.14 , pp. 1097-1105
    • Du, H.1    Guo, L.2    Fang, F.3    Chen, D.4    Sosunov, A.A.5    McKhann, G.M.6    Yan, Y.7    Wang, C.8    Zhang, H.9    Molkentin, J.D.10
  • 37
    • 77950284301 scopus 로고    scopus 로고
    • Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction
    • Hayashi T., Fujimoto M. Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction. Mol Pharmacol 2010, 77:517-528.
    • (2010) Mol Pharmacol , vol.77 , pp. 517-528
    • Hayashi, T.1    Fujimoto, M.2
  • 39
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P., Shioi J., Serban G., Georgakopoulos A., Sarner S., Nagy V., Baki L., Wen P., Efthimiopoulos S., Shao Z., et al. A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J 2002, 21:1948-1956.
    • (2002) EMBO J , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3    Georgakopoulos, A.4    Sarner, S.5    Nagy, V.6    Baki, L.7    Wen, P.8    Efthimiopoulos, S.9    Shao, Z.10
  • 42
    • 84930198272 scopus 로고    scopus 로고
    • 2+ dysregulation in the endoplasmic reticulum related to Alzheimer's disease: a review on experimental progress and computational modeling
    • 2+ dysregulation in the endoplasmic reticulum related to Alzheimer's disease: a review on experimental progress and computational modeling. Biosystems 2015, 134:1-15.
    • (2015) Biosystems , vol.134 , pp. 1-15
    • Liang, J.1    Kulasiri, D.2    Samarasinghe, S.3
  • 43
    • 77953634580 scopus 로고    scopus 로고
    • ER calcium and Alzheimer's disease: in a state of flux
    • Mattson M.P. ER calcium and Alzheimer's disease: in a state of flux. Sci Signal 2010, 3:pe10.
    • (2010) Sci Signal , vol.3 , pp. pe10
    • Mattson, M.P.1
  • 44
    • 77956220629 scopus 로고    scopus 로고
    • Neuronal calcium signaling, mitochondrial dysfunction, and Alzheimer's disease
    • Supnet C., Bezprozvanny I. Neuronal calcium signaling, mitochondrial dysfunction, and Alzheimer's disease. J Alzheimers Dis 2010, 20(Suppl 2):S487-S498.
    • (2010) J Alzheimers Dis , vol.20 , pp. S487-S498
    • Supnet, C.1    Bezprozvanny, I.2
  • 46
    • 0343050763 scopus 로고
    • Alterations in calcium content and biochemical processes in cultured skin fibroblasts from aged and Alzheimer donors
    • Peterson C., Goldman J.E. Alterations in calcium content and biochemical processes in cultured skin fibroblasts from aged and Alzheimer donors. Proc Natl Acad Sci U S A 1986, 83:2758-2762.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 2758-2762
    • Peterson, C.1    Goldman, J.E.2
  • 47
    • 0023191781 scopus 로고
    • Altered metabolic properties of cultured skin fibroblasts in Alzheimer's disease
    • Sims N.R., Finegan J.M., Blass J.P. Altered metabolic properties of cultured skin fibroblasts in Alzheimer's disease. Ann Neurol 1987, 21:451-457.
    • (1987) Ann Neurol , vol.21 , pp. 451-457
    • Sims, N.R.1    Finegan, J.M.2    Blass, J.P.3
  • 48
    • 84897463426 scopus 로고    scopus 로고
    • Reduced synaptic STIM2 expression and impaired store-operated calcium entry cause destabilization of mature spines in mutant presenilin mice
    • Sun S., Zhang H., Liu J., Popugaeva E., Xu N.-J., Feske S., White C.L., Bezprozvanny I. Reduced synaptic STIM2 expression and impaired store-operated calcium entry cause destabilization of mature spines in mutant presenilin mice. Neuron 2014, 82:79-93.
    • (2014) Neuron , vol.82 , pp. 79-93
    • Sun, S.1    Zhang, H.2    Liu, J.3    Popugaeva, E.4    Xu, N.-J.5    Feske, S.6    White, C.L.7    Bezprozvanny, I.8
  • 49
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates β-amyloid-related mitochondrial fission and neuronal injury
    • Cho D.-H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z., Lipton S.A. S-nitrosylation of Drp1 mediates β-amyloid-related mitochondrial fission and neuronal injury. Science 2009, 324:102-105.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.-H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 50
    • 70449435581 scopus 로고    scopus 로고
    • Altered mitochondria, energy metabolism, voltage-dependent anion channel, and lipid rafts converge to exhaust neurons in Alzheimer's disease
    • Ferrer I. Altered mitochondria, energy metabolism, voltage-dependent anion channel, and lipid rafts converge to exhaust neurons in Alzheimer's disease. J Bioenerg Biomembr 2009, 41:425-431.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 425-431
    • Ferrer, I.1
  • 51
    • 10244255083 scopus 로고    scopus 로고
    • Mitochondrial enzymes and endoplasmic reticulum calcium stores as targets of oxidative stress in neurodegenerative diseases
    • Gibson G.E., Huang H.-M. Mitochondrial enzymes and endoplasmic reticulum calcium stores as targets of oxidative stress in neurodegenerative diseases. J Bioenerg Biomembr 2004, 36:335-340.
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 335-340
    • Gibson, G.E.1    Huang, H.-M.2
  • 52
    • 84884289093 scopus 로고    scopus 로고
    • Axonal transport and mitochondrial dysfunction in Alzheimer's disease
    • Riemer J., Kins S. Axonal transport and mitochondrial dysfunction in Alzheimer's disease. Neurodegener Dis 2013, 12:111-124.
    • (2013) Neurodegener Dis , vol.12 , pp. 111-124
    • Riemer, J.1    Kins, S.2
  • 54
    • 58049218922 scopus 로고    scopus 로고
    • Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins
    • Wang X., Su B., Siedlak S.L., Moreira P.I., Fujioka H., Wang Y., Casadesus G., Zhu X. Amyloid-β overproduction causes abnormal mitochondrial dynamics via differential modulation of mitochondrial fission/fusion proteins. Proc Natl Acad Sci U S A 2008, 105:19318-19323.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19318-19323
    • Wang, X.1    Su, B.2    Siedlak, S.L.3    Moreira, P.I.4    Fujioka, H.5    Wang, Y.6    Casadesus, G.7    Zhu, X.8
  • 55
    • 84858018995 scopus 로고    scopus 로고
    • The dying of the light: mitochondrial failure in Alzheimer's disease
    • Young-Collier K.J., McArdle M., Bennett J.P. The dying of the light: mitochondrial failure in Alzheimer's disease. J Alzheimers Dis 2012, 28:771-781.
    • (2012) J Alzheimers Dis , vol.28 , pp. 771-781
    • Young-Collier, K.J.1    McArdle, M.2    Bennett, J.P.3
  • 56
    • 84878938660 scopus 로고    scopus 로고
    • Lipid transport between the endoplasmic reticulum and mitochondria
    • Flis V.V., Daum G. Lipid transport between the endoplasmic reticulum and mitochondria. Cold Spring Harb Perspect Biol 2013, 5:a013235.
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , pp. a013235
    • Flis, V.V.1    Daum, G.2
  • 57
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • Voelker D.R. Bridging gaps in phospholipid transport. Trends Biochem Sci 2005, 30:396-404.
    • (2005) Trends Biochem Sci , vol.30 , pp. 396-404
    • Voelker, D.R.1
  • 60
    • 33847732649 scopus 로고    scopus 로고
    • Ultrastructural localization of intraneuronal Aβ-peptide in Alzheimer disease brains
    • Gómez-Ramos P., Asunción Morán M. Ultrastructural localization of intraneuronal Aβ-peptide in Alzheimer disease brains. J Alzheimers Dis 2007, 11:53-59.
    • (2007) J Alzheimers Dis , vol.11 , pp. 53-59
    • Gómez-Ramos, P.1    Asunción Morán, M.2
  • 62
    • 16544376730 scopus 로고    scopus 로고
    • Role of acyl-coenzyme A:cholesterol acyltransferase activity in the processing of the amyloid precursor protein
    • Puglielli L., Ellis B.C., Ingano L.A., Kovacs D.M. Role of acyl-coenzyme A:cholesterol acyltransferase activity in the processing of the amyloid precursor protein. J Mol Neurosci 2004, 24:93-96.
    • (2004) J Mol Neurosci , vol.24 , pp. 93-96
    • Puglielli, L.1    Ellis, B.C.2    Ingano, L.A.3    Kovacs, D.M.4
  • 64
    • 0037853140 scopus 로고    scopus 로고
    • Recycling of apoprotein E is associated with cholesterol efflux and high density lipoprotein internalization
    • Heeren J., Grewal T., Laatsch A., Rottke D., Rinninger F., Enrich C., Beisiegel U. Recycling of apoprotein E is associated with cholesterol efflux and high density lipoprotein internalization. J Biol Chem 2003, 278:14370-14378.
    • (2003) J Biol Chem , vol.278 , pp. 14370-14378
    • Heeren, J.1    Grewal, T.2    Laatsch, A.3    Rottke, D.4    Rinninger, F.5    Enrich, C.6    Beisiegel, U.7
  • 65
    • 11244275436 scopus 로고    scopus 로고
    • Impaired recycling of apolipoprotein E4 is associated with intracellular cholesterol accumulation
    • Heeren J., Grewal T., Laatsch A., Becker N., Rinninger F., Rye K.-A., Beisiegel U. Impaired recycling of apolipoprotein E4 is associated with intracellular cholesterol accumulation. J Biol Chem 2004, 279:55483-55492.
    • (2004) J Biol Chem , vol.279 , pp. 55483-55492
    • Heeren, J.1    Grewal, T.2    Laatsch, A.3    Becker, N.4    Rinninger, F.5    Rye, K.-A.6    Beisiegel, U.7
  • 66
    • 38549141572 scopus 로고    scopus 로고
    • Cellular cholesterol trafficking and compartmentalization
    • Ikonen E. Cellular cholesterol trafficking and compartmentalization. Nat Rev Mol Cell Biol 2008, 9:125-138.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 125-138
    • Ikonen, E.1
  • 67
    • 77953271492 scopus 로고    scopus 로고
    • Cholesterol-related genes in Alzheimer's disease
    • Wollmer M.A. Cholesterol-related genes in Alzheimer's disease. Biochim Biophys Acta 2010, 1801:762-773.
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 762-773
    • Wollmer, M.A.1
  • 69
    • 0345791510 scopus 로고    scopus 로고
    • Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein
    • Abe-Dohmae S., Ikeda Y., Matsuo M., Hayashi M., Okuhira K.-i., Ueda K., Yokoyama S. Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein. J Biol Chem 2004, 279:604-611.
    • (2004) J Biol Chem , vol.279 , pp. 604-611
    • Abe-Dohmae, S.1    Ikeda, Y.2    Matsuo, M.3    Hayashi, M.4    Okuhira, K.-I.5    Ueda, K.6    Yokoyama, S.7
  • 71
    • 75649135280 scopus 로고    scopus 로고
    • Neuropathology of Alzheimer's disease
    • Perl D.P. Neuropathology of Alzheimer's disease. Mt Sinai J Med 2010, 77:32-42.
    • (2010) Mt Sinai J Med , vol.77 , pp. 32-42
    • Perl, D.P.1
  • 72
    • 0022801449 scopus 로고
    • Three-dimensional observation of intracellular membranous structures in dog heart muscle cells by scanning electron microscopy
    • Yoshikane H., Nihei T., Moriyama K. Three-dimensional observation of intracellular membranous structures in dog heart muscle cells by scanning electron microscopy. J Submicrosc Cytol 1986, 18:629-636.
    • (1986) J Submicrosc Cytol , vol.18 , pp. 629-636
    • Yoshikane, H.1    Nihei, T.2    Moriyama, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.