메뉴 건너뛰기




Volumn 73, Issue , 2015, Pages 24-35

Astrocytes and microglia but not neurons preferentially generate N-terminally truncated Aβ peptides

Author keywords

Alzheimer's disease; Astrocytes; A ; BACE; Extracellular; Intracellular; Microglia; N terminally truncated; Neurons; Secretase

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN 2 X; AMYLOID BETA PROTEIN 3 X; AMYLOID BETA PROTEIN 4 X; AMYLOID BETA PROTEIN 5 X; BETA SECRETASE 1; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; N [N (3,5 DIFLUOROPHENACETYL)ALANYL]PHENYLGLYCINE TERT BUTYL ESTER; UNCLASSIFIED DRUG; ASPARTIC PROTEINASE; PEPTIDE FRAGMENT; TAU PROTEIN;

EID: 84908439707     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2014.08.031     Document Type: Article
Times cited : (51)

References (75)
  • 1
    • 84901613223 scopus 로고    scopus 로고
    • Focusing the amyloid cascade hypothesis on N-truncated Abeta peptides as drug targets against Alzheimer's disease
    • Bayer T.A., Wirths O. Focusing the amyloid cascade hypothesis on N-truncated Abeta peptides as drug targets against Alzheimer's disease. Acta Neuropathol. 2014, 127:787-801.
    • (2014) Acta Neuropathol. , vol.127 , pp. 787-801
    • Bayer, T.A.1    Wirths, O.2
  • 2
    • 84866893131 scopus 로고    scopus 로고
    • The metalloprotease meprin beta generates amino terminal-truncated amyloid beta peptide species
    • Bien J., et al. The metalloprotease meprin beta generates amino terminal-truncated amyloid beta peptide species. J. Biol. Chem. 2012, 287:33304-33313.
    • (2012) J. Biol. Chem. , vol.287 , pp. 33304-33313
    • Bien, J.1
  • 3
    • 50849139570 scopus 로고    scopus 로고
    • Isoaspartate-containing amyloid precursor protein-derived peptides alter efficacy and specificity of potential beta-secretases
    • Bohme L., et al. Isoaspartate-containing amyloid precursor protein-derived peptides alter efficacy and specificity of potential beta-secretases. Biol. Chem. 2008, 389:1055-1066.
    • (2008) Biol. Chem. , vol.389 , pp. 1055-1066
    • Bohme, L.1
  • 4
    • 84881099652 scopus 로고    scopus 로고
    • N-truncated amyloid beta (Abeta) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits
    • Bouter Y., et al. N-truncated amyloid beta (Abeta) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits. Acta Neuropathol. 2013, 126:189-205.
    • (2013) Acta Neuropathol. , vol.126 , pp. 189-205
    • Bouter, Y.1
  • 5
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H., Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 1991, 82:239-259.
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 6
    • 33749150163 scopus 로고    scopus 로고
    • Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry
    • Braak H., et al. Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry. Acta Neuropathol. 2006, 112:389-404.
    • (2006) Acta Neuropathol. , vol.112 , pp. 389-404
    • Braak, H.1
  • 7
    • 23944510149 scopus 로고    scopus 로고
    • The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing
    • Carrodeguas J.A., et al. The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing. Neuroscience 2005, 134:1285-1300.
    • (2005) Neuroscience , vol.134 , pp. 1285-1300
    • Carrodeguas, J.A.1
  • 8
    • 4644276796 scopus 로고    scopus 로고
    • Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model
    • Casas C., et al. Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model. Am. J. Pathol. 2004, 165:1289-1300.
    • (2004) Am. J. Pathol. , vol.165 , pp. 1289-1300
    • Casas, C.1
  • 9
    • 33749615367 scopus 로고    scopus 로고
    • Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells
    • Cynis H., et al. Inhibition of glutaminyl cyclase alters pyroglutamate formation in mammalian cells. Biochim. Biophys. Acta 2006, 1764:1618-1625.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1618-1625
    • Cynis, H.1
  • 10
    • 47249117092 scopus 로고    scopus 로고
    • Amyloidogenic processing of amyloid precursor protein: evidence of a pivotal role of glutaminyl cyclase in generation of pyroglutamate-modified amyloid-beta
    • Cynis H., et al. Amyloidogenic processing of amyloid precursor protein: evidence of a pivotal role of glutaminyl cyclase in generation of pyroglutamate-modified amyloid-beta. Biochemistry 2008, 47:7405-7413.
    • (2008) Biochemistry , vol.47 , pp. 7405-7413
    • Cynis, H.1
  • 11
    • 84880570156 scopus 로고    scopus 로고
    • Intracellular accumulation of aggregated pyroglutamate amyloid beta: convergence of aging and Abeta pathology at the lysosome
    • De Kimpe L., et al. Intracellular accumulation of aggregated pyroglutamate amyloid beta: convergence of aging and Abeta pathology at the lysosome. Age (Dordr) 2013, 35:673-687.
    • (2013) Age (Dordr) , vol.35 , pp. 673-687
    • De Kimpe, L.1
  • 12
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and nicastrin with presenilin generate an active gamma-secretase complex
    • De Strooper B. Aph-1, Pen-2, and nicastrin with presenilin generate an active gamma-secretase complex. Neuron 2003, 38:9-12.
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 13
    • 0022980104 scopus 로고
    • Alzheimer's disease: tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments
    • Delacourte A., Defossez A. Alzheimer's disease: tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments. J. Neurol. Sci. 1986, 76:173-186.
    • (1986) J. Neurol. Sci. , vol.76 , pp. 173-186
    • Delacourte, A.1    Defossez, A.2
  • 14
    • 9244246339 scopus 로고    scopus 로고
    • Lithium decreases secretion of Abeta1-42 and C-truncated species Abeta1-37/38/39/40 in chicken telencephalic cultures but specifically increases intracellular Abeta1-38
    • Esselmann H., et al. Lithium decreases secretion of Abeta1-42 and C-truncated species Abeta1-37/38/39/40 in chicken telencephalic cultures but specifically increases intracellular Abeta1-38. Neurodegener. Dis. 2004, 1:236-241.
    • (2004) Neurodegener. Dis. , vol.1 , pp. 236-241
    • Esselmann, H.1
  • 15
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G.G., Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 1984, 120:885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 16
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I., et al. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. U. S. A. 1986, 83:4913-4917.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1
  • 17
    • 33750825049 scopus 로고    scopus 로고
    • High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain
    • Guntert A., et al. High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain. Neuroscience 2006, 143:461-475.
    • (2006) Neuroscience , vol.143 , pp. 461-475
    • Guntert, A.1
  • 18
    • 0027333557 scopus 로고
    • Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide
    • Haass C., Selkoe D.J. Cellular processing of beta-amyloid precursor protein and the genesis of amyloid beta-peptide. Cell 1993, 75:1039-1042.
    • (1993) Cell , vol.75 , pp. 1039-1042
    • Haass, C.1    Selkoe, D.J.2
  • 19
    • 0026325645 scopus 로고
    • Processing of beta-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretion
    • Haass C., et al. Processing of beta-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretion. J. Neurosci. 1991, 11:3783-3793.
    • (1991) J. Neurosci. , vol.11 , pp. 3783-3793
    • Haass, C.1
  • 20
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
    • Harper J.D., et al. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chem. Biol. 1997, 4:951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1
  • 21
    • 84883475331 scopus 로고    scopus 로고
    • Analysis of amino-terminal variants of amyloid-beta peptides by capillary isoelectric focusing immunoassay
    • Haussmann U., et al. Analysis of amino-terminal variants of amyloid-beta peptides by capillary isoelectric focusing immunoassay. Anal. Chem. 2013, 85:8142-8149.
    • (2013) Anal. Chem. , vol.85 , pp. 8142-8149
    • Haussmann, U.1
  • 22
    • 84904353612 scopus 로고    scopus 로고
    • The glia/neuron ratio: how it varies uniformly across brain structures and species and what that means for brain physiology and evolution
    • Herculano-Houzel S. The glia/neuron ratio: how it varies uniformly across brain structures and species and what that means for brain physiology and evolution. Glia 2014, 62(9):1377-1391.
    • (2014) Glia , vol.62 , Issue.9 , pp. 1377-1391
    • Herculano-Houzel, S.1
  • 23
    • 26844559355 scopus 로고    scopus 로고
    • Inhibition of cathepsin B reduces beta-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate beta-secretase of Alzheimer's disease
    • Hook V., et al. Inhibition of cathepsin B reduces beta-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate beta-secretase of Alzheimer's disease. Biol. Chem. 2005, 386:931-940.
    • (2005) Biol. Chem. , vol.386 , pp. 931-940
    • Hook, V.1
  • 24
    • 0029061685 scopus 로고
    • Neutral endopeptidase can hydrolyze beta-amyloid(1-40) but shows no effect on beta-amyloid precursor protein metabolism
    • Howell S., et al. Neutral endopeptidase can hydrolyze beta-amyloid(1-40) but shows no effect on beta-amyloid precursor protein metabolism. Peptides 1995, 16:647-652.
    • (1995) Peptides , vol.16 , pp. 647-652
    • Howell, S.1
  • 25
    • 0035930538 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme degrades Alzheimer amyloid beta-peptide (A beta); retards A beta aggregation, deposition, fibril formation; and inhibits cytotoxicity
    • Hu J., et al. Angiotensin-converting enzyme degrades Alzheimer amyloid beta-peptide (A beta); retards A beta aggregation, deposition, fibril formation; and inhibits cytotoxicity. J. Biol. Chem. 2001, 276:47863-47868.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47863-47868
    • Hu, J.1
  • 26
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp 2) as beta-secretase
    • Hussain I., et al. Identification of a novel aspartic protease (Asp 2) as beta-secretase. Mol. Cell. Neurosci. 1999, 14:419-427.
    • (1999) Mol. Cell. Neurosci. , vol.14 , pp. 419-427
    • Hussain, I.1
  • 27
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., et al. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1
  • 28
    • 0029665851 scopus 로고    scopus 로고
    • Electrophoretic separation of betaA4 peptides (1-40) and (1-42)
    • Klafki H.W., et al. Electrophoretic separation of betaA4 peptides (1-40) and (1-42). Anal. Biochem. 1996, 237:24-29.
    • (1996) Anal. Biochem. , vol.237 , pp. 24-29
    • Klafki, H.W.1
  • 29
    • 0035918312 scopus 로고    scopus 로고
    • Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains
    • Kuo Y.M., et al. Comparative analysis of amyloid-beta chemical structure and amyloid plaque morphology of transgenic mouse and Alzheimer's disease brains. J. Biol. Chem. 2001, 276:12991-12998.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12991-12998
    • Kuo, Y.M.1
  • 30
    • 0029980902 scopus 로고    scopus 로고
    • Amyloid precursor protein metabolism in primary cell cultures of neurons, astrocytes, and microglia
    • LeBlanc A.C., et al. Amyloid precursor protein metabolism in primary cell cultures of neurons, astrocytes, and microglia. J. Neurochem. 1996, 66:2300-2310.
    • (1996) J. Neurochem. , vol.66 , pp. 2300-2310
    • LeBlanc, A.C.1
  • 31
    • 0031017752 scopus 로고    scopus 로고
    • Processing of amyloid precursor protein in human primary neuron and astrocyte cultures
    • LeBlanc A.C., et al. Processing of amyloid precursor protein in human primary neuron and astrocyte cultures. J. Neurochem. 1997, 68:1183-1190.
    • (1997) J. Neurochem. , vol.68 , pp. 1183-1190
    • LeBlanc, A.C.1
  • 32
    • 0038751845 scopus 로고    scopus 로고
    • Secretion and intracellular generation of truncated Abeta in beta-site amyloid-beta precursor protein-cleaving enzyme expressing human neurons
    • Lee E.B., et al. Secretion and intracellular generation of truncated Abeta in beta-site amyloid-beta precursor protein-cleaving enzyme expressing human neurons. J. Biol. Chem. 2003, 278:4458-4466.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4458-4466
    • Lee, E.B.1
  • 33
    • 10744229989 scopus 로고    scopus 로고
    • Neurochemical diagnosis of Alzheimer's dementia by CSF Abeta42, Abeta42/Abeta40 ratio and total tau
    • Lewczuk P., et al. Neurochemical diagnosis of Alzheimer's dementia by CSF Abeta42, Abeta42/Abeta40 ratio and total tau. Neurobiol. Aging 2004, 25:273-281.
    • (2004) Neurobiol. Aging , vol.25 , pp. 273-281
    • Lewczuk, P.1
  • 34
    • 77952548703 scopus 로고    scopus 로고
    • Amyloid beta peptides in plasma in early diagnosis of Alzheimer's disease: a multicenter study with multiplexing
    • Lewczuk P., et al. Amyloid beta peptides in plasma in early diagnosis of Alzheimer's disease: a multicenter study with multiplexing. Exp. Neurol. 2010, 223:366-370.
    • (2010) Exp. Neurol. , vol.223 , pp. 366-370
    • Lewczuk, P.1
  • 35
    • 70350366775 scopus 로고    scopus 로고
    • Degradation of amyloid beta protein by purified myelin basic protein
    • Liao M.C., et al. Degradation of amyloid beta protein by purified myelin basic protein. J. Biol. Chem. 2009, 284:28917-28925.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28917-28925
    • Liao, M.C.1
  • 36
    • 84867266792 scopus 로고    scopus 로고
    • Optimisation of BACE1 inhibition of tripartite structures by modification of membrane anchors, spacers and pharmacophores - development of potential agents for the treatment of Alzheimer's disease
    • Linning P., et al. Optimisation of BACE1 inhibition of tripartite structures by modification of membrane anchors, spacers and pharmacophores - development of potential agents for the treatment of Alzheimer's disease. Org. Biomol. Chem. 2012, 10:8216-8235.
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 8216-8235
    • Linning, P.1
  • 37
    • 35648929821 scopus 로고    scopus 로고
    • Urea-based two-dimensional electrophoresis of beta-amyloid peptides in human plasma: evidence for novel Abeta species
    • Maler J.M., et al. Urea-based two-dimensional electrophoresis of beta-amyloid peptides in human plasma: evidence for novel Abeta species. Proteomics 2007, 7:3815-3820.
    • (2007) Proteomics , vol.7 , pp. 3815-3820
    • Maler, J.M.1
  • 38
    • 50049128422 scopus 로고    scopus 로고
    • Adherence-dependent shifts in the patterns of beta-amyloid peptides secreted by human mononuclear phagocytes
    • Maler J.M., et al. Adherence-dependent shifts in the patterns of beta-amyloid peptides secreted by human mononuclear phagocytes. Brain Behav. Immun. 2008, 22:1044-1048.
    • (2008) Brain Behav. Immun. , vol.22 , pp. 1044-1048
    • Maler, J.M.1
  • 39
    • 84903820348 scopus 로고    scopus 로고
    • Pyroglutamylated amyloid-beta is associated with hyperphosphorylated tau and severity of Alzheimer's disease
    • Mandler M., et al. Pyroglutamylated amyloid-beta is associated with hyperphosphorylated tau and severity of Alzheimer's disease. Acta Neuropathol. 2014, 128:67-79.
    • (2014) Acta Neuropathol. , vol.128 , pp. 67-79
    • Mandler, M.1
  • 40
    • 0012510759 scopus 로고
    • Amyloid plaque core protein in Alzheimer disease and Down syndrome
    • Masters C.L., et al. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proc. Natl. Acad. Sci. U. S. A. 1985, 82:4245-4249.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 4245-4249
    • Masters, C.L.1
  • 41
    • 84856638194 scopus 로고    scopus 로고
    • BACE1 inhibition induces a specific cerebrospinal fluid beta-amyloid pattern that identifies drug effects in the central nervous system
    • Mattsson N., et al. BACE1 inhibition induces a specific cerebrospinal fluid beta-amyloid pattern that identifies drug effects in the central nervous system. PLoS One 2012, 7:e31084.
    • (2012) PLoS One , vol.7 , pp. e31084
    • Mattsson, N.1
  • 42
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • Miller D.L., et al. Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch. Biochem. Biophys. 1993, 301:41-52.
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 41-52
    • Miller, D.L.1
  • 43
    • 84861330645 scopus 로고    scopus 로고
    • Overlapping profiles of Abeta peptides in the Alzheimer's disease and pathological aging brains
    • Moore B.D., et al. Overlapping profiles of Abeta peptides in the Alzheimer's disease and pathological aging brains. Alzheimers Res. Ther. 2012, 4:18.
    • (2012) Alzheimers Res. Ther. , vol.4 , pp. 18
    • Moore, B.D.1
  • 44
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 1983, 65:55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 45
    • 0037427384 scopus 로고    scopus 로고
    • Astrocytes accumulate A beta 42 and give rise to astrocytic amyloid plaques in Alzheimer disease brains
    • Nagele R.G., et al. Astrocytes accumulate A beta 42 and give rise to astrocytic amyloid plaques in Alzheimer disease brains. Brain Res. 2003, 971:197-209.
    • (2003) Brain Res. , vol.971 , pp. 197-209
    • Nagele, R.G.1
  • 46
    • 84863762839 scopus 로고    scopus 로고
    • Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-beta
    • Nussbaum J.M., et al. Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-beta. Nature 2012, 485:651-655.
    • (2012) Nature , vol.485 , pp. 651-655
    • Nussbaum, J.M.1
  • 47
    • 84874302223 scopus 로고    scopus 로고
    • Endothelin-converting enzymes degrade intracellular beta-amyloid produced within the endosomal/lysosomal pathway and autophagosomes
    • Pacheco-Quinto J., Eckman E.A. Endothelin-converting enzymes degrade intracellular beta-amyloid produced within the endosomal/lysosomal pathway and autophagosomes. J. Biol. Chem. 2013, 288:5606-5615.
    • (2013) J. Biol. Chem. , vol.288 , pp. 5606-5615
    • Pacheco-Quinto, J.1    Eckman, E.A.2
  • 48
    • 84872466519 scopus 로고    scopus 로고
    • Mass spectrometric characterization of amyloid-beta species in the 7PA2 cell model of Alzheimer's disease
    • Portelius E., et al. Mass spectrometric characterization of amyloid-beta species in the 7PA2 cell model of Alzheimer's disease. J. Alzheimers Dis. 2013, 33:85-93.
    • (2013) J. Alzheimers Dis. , vol.33 , pp. 85-93
    • Portelius, E.1
  • 49
    • 0018609164 scopus 로고
    • Thy-1 antigen on astrocytes in long-term cultures of rat central nervous system
    • Pruss R.M. Thy-1 antigen on astrocytes in long-term cultures of rat central nervous system. Nature 1979, 280:688-690.
    • (1979) Nature , vol.280 , pp. 688-690
    • Pruss, R.M.1
  • 50
    • 0000398342 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation
    • Qiu W.Q., et al. Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J. Biol. Chem. 1998, 273:32730-32738.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32730-32738
    • Qiu, W.Q.1
  • 51
    • 17344388652 scopus 로고    scopus 로고
    • BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: implications for Alzheimer's disease therapeutics
    • Roberds S.L., et al. BACE knockout mice are healthy despite lacking the primary beta-secretase activity in brain: implications for Alzheimer's disease therapeutics. Hum. Mol. Genet. 2001, 10(12):1317-1324.
    • (2001) Hum. Mol. Genet. , vol.10 , Issue.12 , pp. 1317-1324
    • Roberds, S.L.1
  • 52
    • 14744281153 scopus 로고    scopus 로고
    • Quantification of the A beta peptide in Alzheimer's plaques by laser dissection microscopy combined with mass spectrometry
    • Rufenacht P., et al. Quantification of the A beta peptide in Alzheimer's plaques by laser dissection microscopy combined with mass spectrometry. J. Mass Spectrom. 2005, 40:193-201.
    • (2005) J. Mass Spectrom. , vol.40 , pp. 193-201
    • Rufenacht, P.1
  • 53
    • 0031969223 scopus 로고    scopus 로고
    • Alzheimer's disease as proteolytic disorders: anabolism and catabolism of beta-amyloid
    • Saido T.C. Alzheimer's disease as proteolytic disorders: anabolism and catabolism of beta-amyloid. Neurobiol. Aging 1998, 19:S69-S75.
    • (1998) Neurobiol. Aging , vol.19 , pp. S69-S75
    • Saido, T.C.1
  • 54
    • 33644853531 scopus 로고    scopus 로고
    • Metabolism of amyloid beta peptide and pathogenesis of Alzheimer's disease. Towards presymptomatic diagnosis, prevention and therapy
    • Saido T.C., Iwata N. Metabolism of amyloid beta peptide and pathogenesis of Alzheimer's disease. Towards presymptomatic diagnosis, prevention and therapy. Neurosci. Res. 2006, 54:235-253.
    • (2006) Neurosci. Res. , vol.54 , pp. 235-253
    • Saido, T.C.1    Iwata, N.2
  • 55
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct beta-amyloid peptide species, A beta N3(pE), in senile plaques
    • Saido T.C., et al. Dominant and differential deposition of distinct beta-amyloid peptide species, A beta N3(pE), in senile plaques. Neuron 1995, 14:457-466.
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1
  • 56
    • 0030582387 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain
    • Saido T.C., et al. Amino- and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain. Neurosci. Lett. 1996, 215:173-176.
    • (1996) Neurosci. Lett. , vol.215 , pp. 173-176
    • Saido, T.C.1
  • 57
    • 78651278930 scopus 로고    scopus 로고
    • Structural design, solid-phase synthesis and activity of membrane-anchored beta-secretase inhibitors on Abeta generation from wild-type and Swedish-mutant APP
    • Schieb H., et al. Structural design, solid-phase synthesis and activity of membrane-anchored beta-secretase inhibitors on Abeta generation from wild-type and Swedish-mutant APP. Chemistry 2010, 16:14412-14423.
    • (2010) Chemistry , vol.16 , pp. 14412-14423
    • Schieb, H.1
  • 58
    • 80053180788 scopus 로고    scopus 로고
    • Beta-amyloid peptide variants in brains and cerebrospinal fluid from amyloid precursor protein (APP) transgenic mice: comparison with human Alzheimer amyloid
    • Schieb H., et al. Beta-amyloid peptide variants in brains and cerebrospinal fluid from amyloid precursor protein (APP) transgenic mice: comparison with human Alzheimer amyloid. J. Biol. Chem. 2011, 286:33747-33758.
    • (2011) J. Biol. Chem. , vol.286 , pp. 33747-33758
    • Schieb, H.1
  • 59
    • 48249145775 scopus 로고    scopus 로고
    • Inhibition of glutaminyl cyclase prevents pGlu-Abeta formation after intracortical/hippocampal microinjection in vivo/in situ
    • Schilling S., et al. Inhibition of glutaminyl cyclase prevents pGlu-Abeta formation after intracortical/hippocampal microinjection in vivo/in situ. J. Neurochem. 2008, 106:1225-1236.
    • (2008) J. Neurochem. , vol.106 , pp. 1225-1236
    • Schilling, S.1
  • 60
    • 0035081475 scopus 로고    scopus 로고
    • Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein
    • Selkoe D.J. Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid beta-protein. J. Alzheimers Dis. 2001, 3:75-80.
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 75-80
    • Selkoe, D.J.1
  • 61
    • 12444337654 scopus 로고    scopus 로고
    • Truncated beta-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach
    • Sergeant N., et al. Truncated beta-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach. J. Neurochem. 2003, 85:1581-1591.
    • (2003) J. Neurochem. , vol.85 , pp. 1581-1591
    • Sergeant, N.1
  • 62
    • 61849084232 scopus 로고    scopus 로고
    • Aminopeptidase A contributes to the N-terminal truncation of amyloid beta-peptide
    • Sevalle J., et al. Aminopeptidase A contributes to the N-terminal truncation of amyloid beta-peptide. J. Neurochem. 2009, 109:248-256.
    • (2009) J. Neurochem. , vol.109 , pp. 248-256
    • Sevalle, J.1
  • 63
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith P.K., et al. Measurement of protein using bicinchoninic acid. Anal. Biochem. 1985, 150:76-85.
    • (1985) Anal. Biochem. , vol.150 , pp. 76-85
    • Smith, P.K.1
  • 64
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins
    • Struhl G., Adachi A. Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins. Mol. Cell 2000, 6:625-636.
    • (2000) Mol. Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 65
    • 53849106834 scopus 로고    scopus 로고
    • Cystatin C-cathepsin B axis regulates amyloid beta levels and associated neuronal deficits in an animal model of Alzheimer's disease
    • Sun B., et al. Cystatin C-cathepsin B axis regulates amyloid beta levels and associated neuronal deficits in an animal model of Alzheimer's disease. Neuron 2008, 60:247-257.
    • (2008) Neuron , vol.60 , pp. 247-257
    • Sun, B.1
  • 66
    • 9444236758 scopus 로고    scopus 로고
    • Amino-truncated amyloid beta-peptide (Abeta5-40/42) produced from caspase-cleaved amyloid precursor protein is deposited in Alzheimer's disease brain
    • Takeda K., et al. Amino-truncated amyloid beta-peptide (Abeta5-40/42) produced from caspase-cleaved amyloid precursor protein is deposited in Alzheimer's disease brain. FASEB J. 2004, 18:1755-1757.
    • (2004) FASEB J. , vol.18 , pp. 1755-1757
    • Takeda, K.1
  • 67
    • 33645226129 scopus 로고    scopus 로고
    • The development of amyloid beta protein deposits in the aged brain
    • Thal D.R., et al. The development of amyloid beta protein deposits in the aged brain. Sci. Aging Knowl. Environ. 2006, re1.
    • (2006) Sci. Aging Knowl. Environ. , pp. re1
    • Thal, D.R.1
  • 68
    • 0037122704 scopus 로고    scopus 로고
    • Design of substrate-based inhibitors of human beta-secretase
    • Tung J.S., et al. Design of substrate-based inhibitors of human beta-secretase. J. Med. Chem. 2002, 45:259-262.
    • (2002) J. Med. Chem. , vol.45 , pp. 259-262
    • Tung, J.S.1
  • 69
    • 0033621048 scopus 로고    scopus 로고
    • Plasmin cleavage of the amyloid beta-protein: alteration of secondary structure and stimulation of tissue plasminogen activator activity
    • Van Nostrand W.E., Porter M. Plasmin cleavage of the amyloid beta-protein: alteration of secondary structure and stimulation of tissue plasminogen activator activity. Biochemistry 1999, 38:11570-11576.
    • (1999) Biochemistry , vol.38 , pp. 11570-11576
    • Van Nostrand, W.E.1    Porter, M.2
  • 70
    • 0035960535 scopus 로고    scopus 로고
    • The functional gamma-secretase inhibitor prevents production of amyloid beta 1-34 in human and murine cell lines
    • Vandermeeren M., et al. The functional gamma-secretase inhibitor prevents production of amyloid beta 1-34 in human and murine cell lines. Neurosci. Lett. 2001, 315:145-148.
    • (2001) Neurosci. Lett. , vol.315 , pp. 145-148
    • Vandermeeren, M.1
  • 71
    • 0033595706 scopus 로고    scopus 로고
    • Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R., et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 1999, 286:735-741.
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 72
    • 84895453516 scopus 로고    scopus 로고
    • Age-dependent, non-cell-autonomous deposition of amyloid from synthesis of β-amyloid by cells other than excitatory neurons
    • Veeraraghavalu, et al. Age-dependent, non-cell-autonomous deposition of amyloid from synthesis of β-amyloid by cells other than excitatory neurons. J. Neurosci. 2014, 34(10):3668-3673.
    • (2014) J. Neurosci. , vol.34 , Issue.10 , pp. 3668-3673
    • Veeraraghavalu1
  • 73
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry
    • Wang R., et al. The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry. J. Biol. Chem. 1996, 271:31894-31902.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31894-31902
    • Wang, R.1
  • 74
    • 0030951595 scopus 로고    scopus 로고
    • Improved electrophoretic separation and immunoblotting of beta-amyloid (A beta) peptides 1-40, 1-42, and 1-43
    • Wiltfang J., et al. Improved electrophoretic separation and immunoblotting of beta-amyloid (A beta) peptides 1-40, 1-42, and 1-43. Electrophoresis 1997, 18:527-532.
    • (1997) Electrophoresis , vol.18 , pp. 527-532
    • Wiltfang, J.1
  • 75
    • 18444393054 scopus 로고    scopus 로고
    • Highly conserved and disease-specific patterns of carboxyterminally truncated Abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation
    • Wiltfang J., et al. Highly conserved and disease-specific patterns of carboxyterminally truncated Abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation. J. Neurochem. 2002, 81:481-496.
    • (2002) J. Neurochem. , vol.81 , pp. 481-496
    • Wiltfang, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.