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Volumn 6, Issue 2, 2014, Pages 95-109

Accumulation of amyloid-like Aβ1-42 in AEL (autophagy-endosomal-lysosomal) vesicles: Potential implications for plaque biogenesis

Author keywords

AEL (autophagy endosomal lysosomal) vesicle; Alzheimer's disease; Amyloid

Indexed keywords

AMYLOID BETA PROTEIN ANTIBODY; AMYLOID BETA PROTEIN [1-40]; AMYLOID BETA PROTEIN [1-42]; AUTOPHAGY PROTEIN 5; CATHEPSIN D; CONGO RED; GREEN FLUORESCENT PROTEIN; MESSENGER RNA; MIFEPRISTONE; TRANSCRIPTION FACTOR GAL4; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

EID: 84896301845     PISSN: 17590914     EISSN: None     Source Type: Journal    
DOI: 10.1042/AN20130044     Document Type: Article
Times cited : (40)

References (68)
  • 1
    • 0031811820 scopus 로고    scopus 로고
    • Beta-amyloid plaques: Stages in life history or independent origin?
    • Armstrong R. A (1998) Beta-amyloid plaques: stages in life history or independent origin? Dement Geriatr Cogn Disord 9:227-238.
    • (1998) Dement Geriatr Cogn Disord , vol.9 , pp. 227-238
    • Armstrong, R.A.1
  • 2
    • 78549273390 scopus 로고    scopus 로고
    • Macroautophagy is not directly involved in the metabolism of amyloid precursor protein
    • Boland B., Smith D, Mooney D, Jung SS, Walsh DM, Platt FM (2010) Macroautophagy is not directly involved in the metabolism of amyloid precursor protein. J Biol Chem 285:37415-37426.
    • (2010) J Biol Chem , vol.285 , pp. 37415-37426
    • Boland, B.1    Smith, D.2    Mooney, D.3    Jung, S.S.4    Walsh, D.M.5    Platt, F.M.6
  • 3
    • 0031030053 scopus 로고    scopus 로고
    • Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ 1-42, in differentiated PC12 cells
    • Burdick D., Kosmoski J, Knauer MF, Glabe CG (1997) Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ 1-42, in differentiated PC12 cells. Brain Res 746:275-284.
    • (1997) Brain Res , vol.746 , pp. 275-284
    • Burdick, D.1    Kosmoski, J.2    Knauer, M.F.3    Glabe, C.G.4
  • 4
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
    • Cataldo A. M, Nixon RA (1990) Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc Natl Acad Sci USA 87:3861-3865.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 6
    • 65249155441 scopus 로고    scopus 로고
    • An Atg1/Atg13 complex with multiple roles in TOR-mediated autophagy regulation
    • Chang Y.-Y, Neufeld TP (2009) An Atg1/Atg13 complex with multiple roles in TOR-mediated autophagy regulation. Mol Biol Cell 20:2004-2014.
    • (2009) Mol Biol Cell , vol.20 , pp. 2004-2014
    • Chang, Y.-Y.1    Neufeld, T.P.2
  • 7
    • 33745026738 scopus 로고    scopus 로고
    • Autophagy and aging: The importance of maintaining "clean" cells
    • Cuervo A. M, Bergamini E, Brunk UT, Droge W, Ffrench M, Terman A (2005) Autophagy and aging: the importance of maintaining "clean" cells. Autophagy 1:131-140. D'Andrea MR, Reiser PA, Polkovitch DA, Gumula NA, Branchide B, Hertzog BM
    • (2005) Autophagy , vol.1 , pp. 131-140
    • Cuervo, A.M.1    Bergamini, E.2    Brunk, U.T.3    Droge, W.4    Ffrench, M.5    Terman, A.6
  • 9
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in mammalian cells
    • Eskelinen E. L (2005) Maturation of autophagic vacuoles in mammalian cells. Autophagy 1:1-10.
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.L.1
  • 10
    • 36248971777 scopus 로고    scopus 로고
    • Mechanisms of amyloid plaque pathogenesis
    • Fiala J. C (2007) Mechanisms of amyloid plaque pathogenesis. Acta Neuropathol 114:551-571.
    • (2007) Acta Neuropathol , vol.114 , pp. 551-571
    • Fiala, J.C.1
  • 11
    • 3242809725 scopus 로고    scopus 로고
    • A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster
    • Finelli A., Kelkar A, Song HJ, Yang H, Konsolaki M (2004) A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster. Mol Cell Neurosci 26:365-375.
    • (2004) Mol Cell Neurosci , vol.26 , pp. 365-375
    • Finelli, A.1    Kelkar, A.2    Song, H.J.3    Yang, H.4    Konsolaki, M.5
  • 13
    • 84867028097 scopus 로고    scopus 로고
    • Lysosomal fusion dysfunction as a unifying hypothesis for Alzheimer's disease pathology
    • Funk K. E, Kuret J (2012) Lysosomal fusion dysfunction as a unifying hypothesis for Alzheimer's disease pathology. Int J Alzheimers Dis 2012:752894.
    • (2012) Int J Alzheimers Dis , vol.2012 , pp. 752894
    • Funk, K.E.1    Kuret, J.2
  • 14
    • 79951790558 scopus 로고    scopus 로고
    • Granulovacuolar degeneration (GVD) bodies of Alzheimer's disease (AD) resemble late-stage autophagic organelles
    • Funk K. E, Mrak RE, Kuret J (2011) Granulovacuolar degeneration (GVD) bodies of Alzheimer's disease (AD) resemble late-stage autophagic organelles. Neuropathol Appl Neurobiol 37:295-306.
    • (2011) Neuropathol Appl Neurobiol , vol.37 , pp. 295-306
    • Funk, K.E.1    Mrak, R.E.2    Kuret, J.3
  • 15
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • Glabe C. (2001) Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease. J Mol Neurosci 17:137-145.
    • (2001) J Mol Neurosci , vol.17 , pp. 137-145
    • Glabe, C.1
  • 16
    • 25144501662 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease
    • Gouras G. K, Almeida CG, Takahashi RH (2005) Intraneuronal Abeta accumulation and origin of plaques in Alzheimer's disease. Neurobiol Aging 26:1235-1244.
    • (2005) Neurobiol Aging , vol.26 , pp. 1235-1244
    • Gouras, G.K.1    Almeida, C.G.2    Takahashi, R.H.3
  • 21
    • 79952089521 scopus 로고    scopus 로고
    • Meta-analysis for genome-wide association study identifies multiple variants at the BIN1 locus associated with late-onset Alzheimer's disease
    • Hu X., Pickering E, Liu YC, Hall S, Fournier H, Katz E, Dechairo B, John S, Van Eerdewegh P., Soares H (2011a) Meta-analysis for genome-wide association study identifies multiple variants at the BIN1 locus associated with late-onset Alzheimer's disease. PLoS One 6:e16616.
    • (2011) PLoS One , vol.6
    • Hu, X.1    Pickering, E.2    Liu, Y.C.3    Hall, S.4    Fournier, H.5    Katz, E.6    Dechairo, B.7    John, S.8    Van Eerdewegh, P.9    Soares, H.10
  • 23
    • 2342473791 scopus 로고    scopus 로고
    • Dissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: A potential model for Alzheimer's disease
    • Iijima K., Liu H-PP, Chiang A-SS, Hearn SA, Konsolaki M, Zhong Y (2004) Dissecting the pathological effects of human Abeta40 and Abeta42 in Drosophila: a potential model for Alzheimer's disease. Proc Natl Acad Sci USA 101:6623-6628.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6623-6628
    • Iijima, K.1    Liu, H.-P.P.2    Chiang, A.-S.S.3    Hearn, S.A.4    Konsolaki, M.5    Zhong, Y.6
  • 24
    • 77950458277 scopus 로고    scopus 로고
    • Transgenic Drosophila models of Alzheimer's disease and tauopathies
    • Iijima-Ando K., Iijima K (2010) Transgenic Drosophila models of Alzheimer's disease and tauopathies. Brain Struct Funct 214:245-262.
    • (2010) Brain Struct Funct , vol.214 , pp. 245-262
    • Iijima-Ando, K.1    Iijima, K.2
  • 26
    • 0026778656 scopus 로고
    • Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein
    • Knauer M. F, Soreghan B, Burdick D, Kosmoski J, Glabe CG (1992) Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein. Proc Natl Acad Sci USA 89:7437-7441.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7437-7441
    • Knauer, M.F.1    Soreghan, B.2    Burdick, D.3    Kosmoski, J.4    Glabe, C.G.5
  • 27
    • 34447564164 scopus 로고    scopus 로고
    • Intracellular Abeta and cognitive deficits precede beta-amyloid deposition in transgenic arcAbeta mice
    • Knobloch M., Konietzko U, Krebs DC, Nitsch RM (2007) Intracellular Abeta and cognitive deficits precede beta-amyloid deposition in transgenic arcAbeta mice. Neurobiol Aging 28:1297-1306.
    • (2007) Neurobiol Aging , vol.28 , pp. 1297-1306
    • Knobloch, M.1    Konietzko, U.2    Krebs, D.C.3    Nitsch, R.M.4
  • 28
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • Laferla F. M, Green KN, Oddo S (2007) Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 8:499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 29
    • 0028981717 scopus 로고
    • The Alzheimer's A beta peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • LaFerla F. M, Tinkle BT, Bieberich CJ, Haudenschild CC, Jay G (1995) The Alzheimer's A beta peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nat Genet 9:21-30.
    • (1995) Nat Genet , vol.9 , pp. 21-30
    • LaFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 30
    • 2142765951 scopus 로고    scopus 로고
    • A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: Analysis by quantitative immunocolocalization
    • Li Q., Lau A, Morris TJ, Guo L, Fordyce CB, Stanley EF (2004) A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization. J Neurosci 24:4070-4081.
    • (2004) J Neurosci , vol.24 , pp. 4070-4081
    • Li, Q.1    Lau, A.2    Morris, T.J.3    Guo, L.4    Fordyce, C.B.5    Stanley, E.F.6
  • 31
    • 84855441938 scopus 로고    scopus 로고
    • SASqPCR: Robust and rapid analysis of RT-qPCR data in SAS
    • Ling D. (2012) SASqPCR: robust and rapid analysis of RT-qPCR data in SAS. PLoS One 7:e29788.
    • (2012) PLoS One , vol.7
    • Ling, D.1
  • 32
    • 84861404120 scopus 로고    scopus 로고
    • Deconvolution of the confounding variations for reverse transcription quantitative real-time polymerase chain reaction by separate analysis of biological replicate data
    • Ling D., Pike CJ, Salvaterra PM (2012) Deconvolution of the confounding variations for reverse transcription quantitative real-time polymerase chain reaction by separate analysis of biological replicate data. Anal Biochem 427:21-25.
    • (2012) Anal Biochem , vol.427 , pp. 21-25
    • Ling, D.1    Pike, C.J.2    Salvaterra, P.M.3
  • 33
    • 84896272647 scopus 로고    scopus 로고
    • In: Alzheimer's Disease Pathogenesis-Core Concepts, Shifting Paradigms and Therapeutic Targets (De La Monte S, ed.), InTech
    • Ling D., Salvaterra PM (2011a) Autophagy-derived Alzheimer's pathogenesis. In: Alzheimer's Disease Pathogenesis-Core Concepts, Shifting Paradigms and Therapeutic Targets (De La Monte S, ed.), pp. 539-560, InTech.
    • (2011) Autophagy-derived Alzheimer's pathogenesis. , pp. 539-560
    • Ling, D.1    Salvaterra, P.M.2
  • 34
    • 79451471809 scopus 로고    scopus 로고
    • Brain aging and Aβ1-42 neurotoxicity converge via deterioration in autophagy-lysosomal system: A conditional Drosophila model linking Alzheimer's neurodegeneration with aging
    • Ling D., Salvaterra PM (2011b) Brain aging and Aβ1-42 neurotoxicity converge via deterioration in autophagy-lysosomal system: a conditional Drosophila model linking Alzheimer's neurodegeneration with aging. Acta Neuropathol 121:183-191.
    • (2011) Acta Neuropathol , vol.121 , pp. 183-191
    • Ling, D.1    Salvaterra, P.M.2
  • 35
    • 79952646811 scopus 로고    scopus 로고
    • Robust RT-qPCR data normalization: Validation and selection of internal reference genes during post-experimental data analysis
    • Ling D., Salvaterra PM (2011c) Robust RT-qPCR data normalization: validation and selection of internal reference genes during post-experimental data analysis. PLoS One 6:e17762.
    • (2011) PLoS One , vol.6
    • Ling, D.1    Salvaterra, P.M.2
  • 36
    • 84896276789 scopus 로고    scopus 로고
    • Autophagy-derived Alzheimer's Pathogenesis
    • In: Shifting Paradigms and Therapeutic Targets (Monte SD La, ed). InTech
    • Ling D., Salvaterra PM (2011d) Autophagy-derived Alzheimer's Pathogenesis. In: Alzheimer's Disease Pathogenesis-Core Concepts, Shifting Paradigms and Therapeutic Targets (Monte SD La, ed). InTech.
    • (2011) Alzheimer's Disease Pathogenesis-Core Concepts
    • Ling, D.1    Salvaterra, P.M.2
  • 37
    • 58449101589 scopus 로고    scopus 로고
    • Abeta42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila
    • Ling D., Song H-J, Garza D, Neufeld TP, Salvaterra PM (2009) Abeta42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila. PLoS One 4:e4201.
    • (2009) PLoS One , vol.4
    • Ling, D.1    Song, H.-J.2    Garza, D.3    Neufeld, T.P.4    Salvaterra, P.M.5
  • 38
    • 0031031041 scopus 로고    scopus 로고
    • The autophagic and endocytic pathways converge at the nascent autophagic vacuoles
    • Liou W., Geuze HJ, Geelen MJ, Slot JW (1997) The autophagic and endocytic pathways converge at the nascent autophagic vacuoles. J Cell Biol 136:61-70.
    • (1997) J Cell Biol , vol.136 , pp. 61-70
    • Liou, W.1    Geuze, H.J.2    Geelen, M.J.3    Slot, J.W.4
  • 39
    • 79151470481 scopus 로고    scopus 로고
    • Autophagy: A broad role in unconventional protein secretion?
    • Manjithaya R., Subramani S (2011) Autophagy: a broad role in unconventional protein secretion? Trends Cell Biol 21:67-73.
    • (2011) Trends Cell Biol , vol.21 , pp. 67-73
    • Manjithaya, R.1    Subramani, S.2
  • 40
    • 21544465581 scopus 로고    scopus 로고
    • An alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's disease
    • Marchesi V. T (2005) An alternative interpretation of the amyloid Abeta hypothesis with regard to the pathogenesis of Alzheimer's disease. Proc Natl Acad Sci USA 102:9093-9098.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9093-9098
    • Marchesi, V.T.1
  • 46
    • 11444267601 scopus 로고    scopus 로고
    • Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases
    • Nixon R. A (2005) Endosome function and dysfunction in Alzheimer's disease and other neurodegenerative diseases. Neurobiol Aging 26:373-382.
    • (2005) Neurobiol Aging , vol.26 , pp. 373-382
    • Nixon, R.A.1
  • 49
    • 75649135280 scopus 로고    scopus 로고
    • Neuropathology of Alzheimer's disease
    • Perl D. PD (2010) Neuropathology of Alzheimer's disease. Mt Sinai J Med 77:32-42.
    • (2010) Mt Sinai J Med , vol.77 , pp. 32-42
    • Perl, D.P.D.1
  • 51
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • Saftig P., Klumperman J (2009) Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat Rev Mol Cell Biol 10: 623-635.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 52
    • 0043239580 scopus 로고    scopus 로고
    • Primary culture of Drosophila embryo cells
    • In: Celis JE (Ed.), Academic Press, New York
    • Salvaterra P., Hayashi I, Ikeda K (1998) Primary culture of Drosophila embryo cells. In: Celis JE (Ed.), Cell Biology: A Laboratory Handbook, Vol. 1 Academic Press, New York, pp 393-397.
    • (1998) Cell Biology: A Laboratory Handbook , vol.1 , pp. 393-397
    • Salvaterra, P.1    Hayashi, I.2    Ikeda, K.3
  • 53
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in the Drosophila fat body
    • Scott R. C, Schuldiner O, Neufeld TP (2004) Role and regulation of starvation-induced autophagy in the Drosophila fat body. Dev Cell 7:167-178.
    • (2004) Dev Cell , vol.7 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3
  • 54
    • 37249067994 scopus 로고    scopus 로고
    • The cell-selective neurotoxicity of the Alzheimer's Abeta peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Abeta toxicity
    • Simakova O., Arispe NJ (2007) The cell-selective neurotoxicity of the Alzheimer's Abeta peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Abeta toxicity. J Neurosci 27:13719-13729.
    • (2007) J Neurosci , vol.27 , pp. 13719-13729
    • Simakova, O.1    Arispe, N.J.2
  • 55
    • 78649315112 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis
    • Sipe J. D, Benson MD, Buxbaum JN, Ikeda S-I, Merlini G, Saraiva MJM, Westermark P (2010) Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis. Amyloid 17:101-104.
    • (2010) Amyloid , vol.17 , pp. 101-104
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.-I.4    Merlini, G.5    Saraiva, M.J.M.6    Westermark, P.7
  • 56
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sönnichsen B, De Renzis S, Nielsen E, Rietdorf J, Zerial M (2000) Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 149:901-914.
    • (2000) J Cell Biol , vol.149 , pp. 901-914
    • Sönnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 58
    • 0035793953 scopus 로고    scopus 로고
    • Acidic pH promotes the formation of toxic fibrils from beta-amyloid peptide
    • Su Y., Chang PT (2001) Acidic pH promotes the formation of toxic fibrils from beta-amyloid peptide. Brain Res 893:287-291.
    • (2001) Brain Res , vol.893 , pp. 287-291
    • Su, Y.1    Chang, P.T.2
  • 59
    • 0014193263 scopus 로고
    • Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia
    • Suzuki K., Terry RD (1967) Fine structural localization of acid phosphatase in senile plaques in Alzheimer's presenile dementia. Acta Neuropathol 8:276-284.
    • (1967) Acta Neuropathol , vol.8 , pp. 276-284
    • Suzuki, K.1    Terry, R.D.2
  • 60
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain
    • Takahashi R. H, Almeida CG, Kearney PF, Yu F, Lin MT, Milner TA, Gouras GK (2004) Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain. J Neurosci 24:3592-3599.
    • (2004) J Neurosci , vol.24 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6    Gouras, G.K.7
  • 62
    • 0036165129 scopus 로고    scopus 로고
    • Alzheimer beta-amyloid peptides: Normal and abnormal localization
    • Takahashi R. H, Nam EE, Edgar M, Gouras GK (2002b) Alzheimer beta-amyloid peptides: normal and abnormal localization. Histol Histopathol 17:239-246.
    • (2002) Histol Histopathol , vol.17 , pp. 239-246
    • Takahashi, R.H.1    Nam, E.E.2    Edgar, M.3    Gouras, G.K.4
  • 64
    • 0041467577 scopus 로고    scopus 로고
    • Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display
    • Wiesehan K., Buder K, Linke RP, Patt S, Stoldt M, Unger E, Schmitt B, Bucci E, Willbold D (2003) Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display. Chembiochem 4:748-753.
    • (2003) Chembiochem , vol.4 , pp. 748-753
    • Wiesehan, K.1    Buder, K.2    Linke, R.P.3    Patt, S.4    Stoldt, M.5    Unger, E.6    Schmitt, B.7    Bucci, E.8    Willbold, D.9
  • 65
    • 34347240979 scopus 로고    scopus 로고
    • Quantification of cerebral amyloid angiopathy and parenchymal amyloid plaques with Congo red histochemical stain
    • Wilcock D. M, Gordon MN, Morgan D (2006) Quantification of cerebral amyloid angiopathy and parenchymal amyloid plaques with Congo red histochemical stain. Nat Protoc 1:1591-1595.
    • (2006) Nat Protoc , vol.1 , pp. 1591-1595
    • Wilcock, D.M.1    Gordon, M.N.2    Morgan, D.3
  • 66
    • 0032790483 scopus 로고    scopus 로고
    • Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D
    • Yasuda Y., Kageyama T, Akamine A, Shibata M, Kominami E, Uchiyama Y, Yamamoto K (1999) Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D. J Biochem 125:1137-1143.
    • (1999) J Biochem , vol.125 , pp. 1137-1143
    • Yasuda, Y.1    Kageyama, T.2    Akamine, A.3    Shibata, M.4    Kominami, E.5    Uchiyama, Y.6    Yamamoto, K.7


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