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Volumn 43, Issue 1, 2003, Pages 164-178

Cerebrovascular requirement for sealant, anti-coagulant and remodeling molecules that allow for the maintenance of vascular integrity and blood supply

Author keywords

Amyloid ; Anti coagulant; Blood supply; Blood brain barrier; Cerebrovasculature; Hemorrhage; Sealant; Vascular integrity

Indexed keywords

BLOOD BRAIN BARRIER; BLOOD CLOTTING; BRAIN BLOOD VESSEL; BRAIN PERFUSION; CELL DIFFERENTIATION; CELL MEMBRANE; CELL VIABILITY; ENCEPHALITIS; EXTRACELLULAR MATRIX; HUMAN; IMMUNITY; IN VIVO STUDY; MENINGITIS; NERVE CELL; NERVE CELL DIFFERENTIATION; PHYSIOLOGY; PRIORITY JOURNAL; REVIEW; STROKE; THROMBOCYTE AGGREGATION; VACCINATION; VASCULARIZATION;

EID: 0141518676     PISSN: 01650173     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-0173(03)00206-6     Document Type: Review
Times cited : (58)

References (149)
  • 1
    • 0032077567 scopus 로고    scopus 로고
    • Amyloid precursor protein modulates the interaction of nerve growth factor with p75 receptor and potentiates its activation of trkA phosphorylation
    • Akar C.A., Wallace W.C. Amyloid precursor protein modulates the interaction of nerve growth factor with p75 receptor and potentiates its activation of trkA phosphorylation. Mol. Brain Res. 56:(1-2):1998;125-132.
    • (1998) Mol. Brain Res. , vol.56 , Issue.1-2 , pp. 125-132
    • Akar, C.A.1    Wallace, W.C.2
  • 4
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis
    • Atwood C.S., Huang X., Moir R.D., Bacarra N.M., Romano D., Tanzi R.E., Bush A.I. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273:1998;12817-12826.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12817-12826
    • Atwood, C.S.1    Huang, X.2    Moir, R.D.3    Bacarra, N.M.4    Romano, D.5    Tanzi, R.E.6    Bush, A.I.7
  • 5
    • 0032613038 scopus 로고    scopus 로고
    • The role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Interrelations between Free Radicals and Metal Ions in Life Processes
    • A. Sigel, & H. Sigel. New York: Marcel Dekker
    • Atwood C.S., Huang X., Moir R.D., Tanzi R.E., Bush A.I. The role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Sigel A., Sigel H. Interrelations between Free Radicals and Metal Ions in Life Processes. Metal Ions in Biological Systems. vol. 36:1999;309-364 Marcel Dekker, New York.
    • (1999) Metal Ions in Biological Systems , vol.36 , pp. 309-364
    • Atwood, C.S.1    Huang, X.2    Moir, R.D.3    Tanzi, R.E.4    Bush, A.I.5
  • 6
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42
    • Atwood C.S., Scarpa R.C., Huang X., Moir R.D., Jones W.D., Fairlie D.P., Tanzi R.E., Bush A.I. Characterization of copper interactions with Alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42. J. Neurochem. 75:2000;1219-1233.
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 9
    • 0037010308 scopus 로고    scopus 로고
    • Amyloid-beta: A vascular sealant that protects against hemorrhage?
    • Atwood C.S., Bishop G.M., Perry G., Smith M.A. Amyloid-beta: a vascular sealant that protects against hemorrhage? J. Neurosci. Res. 70:2002a;356.
    • (2002) J. Neurosci. Res. , vol.70 , pp. 356
    • Atwood, C.S.1    Bishop, G.M.2    Perry, G.3    Smith, M.A.4
  • 12
    • 0018847124 scopus 로고
    • The vascular system of the cerebral cortex
    • Bar T. The vascular system of the cerebral cortex. Adv. Anat. Embryol. Cell Biol. 59:1980;1-62.
    • (1980) Adv. Anat. Embryol. Cell Biol. , vol.59 , pp. 1-62
    • Bar, T.1
  • 15
    • 0032823830 scopus 로고    scopus 로고
    • Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D): A review of the variety in phenotypic expression
    • Bornebroek M., Haan J., Roos R.A. Hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D): a review of the variety in phenotypic expression. Amyloid. 6:1999;215-224.
    • (1999) Amyloid , vol.6 , pp. 215-224
    • Bornebroek, M.1    Haan, J.2    Roos, R.A.3
  • 16
    • 0027076834 scopus 로고
    • Alpha 2-macroglobulin, a multifunctional binding protein with targeting characteristics
    • Borth W. Alpha 2-macroglobulin, a multifunctional binding protein with targeting characteristics. FASEB J. 6:1992;3345-3353.
    • (1992) FASEB J. , vol.6 , pp. 3345-3353
    • Borth, W.1
  • 17
    • 0034103560 scopus 로고    scopus 로고
    • Cerebrovascular pathology in Alzheimer's disease and leukoaraiosis
    • Brown W.R., Moody D.M., Thore C.R., Challa V.R. Cerebrovascular pathology in Alzheimer's disease and leukoaraiosis. Ann. NY Acad. Sci. 903:2000;39-45.
    • (2000) Ann. NY Acad. Sci. , vol.903 , pp. 39-45
    • Brown, W.R.1    Moody, D.M.2    Thore, C.R.3    Challa, V.R.4
  • 19
    • 0030721487 scopus 로고    scopus 로고
    • Brain microvascular changes in Alzheimer's disease and other dementias
    • Buee L., Hof P.R., Delacourte A. Brain microvascular changes in Alzheimer's disease and other dementias. Ann. NY Acad. Sci. 826:1997;7-24.
    • (1997) Ann. NY Acad. Sci. , vol.826 , pp. 7-24
    • Buee, L.1    Hof, P.R.2    Delacourte, A.3
  • 20
    • 0027407570 scopus 로고
    • Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells
    • Busciglio J., Gabuzda D.H., Matsudaira P., Yankner B.A. Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. USA. 90:1993;2092-2096.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2092-2096
    • Busciglio, J.1    Gabuzda, D.H.2    Matsudaira, P.3    Yankner, B.A.4
  • 22
    • 0028180196 scopus 로고
    • Modulation of A beta adhesiveness and secretase site cleavage by zinc
    • Bush A.I., Pettingell W.H. Jr., Paradis M.D., Tanzi R.E. Modulation of A beta adhesiveness and secretase site cleavage by zinc. J. Biol. Chem. 269:1994;12152-12158.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12152-12158
    • Bush, A.I.1    Pettingell W.H., Jr.2    Paradis, M.D.3    Tanzi, R.E.4
  • 27
    • 0029655250 scopus 로고    scopus 로고
    • Ultrastructural features of the blood-brain barrier in biopsy tissue from Alzheimer's disease patients
    • Claudio L. Ultrastructural features of the blood-brain barrier in biopsy tissue from Alzheimer's disease patients. Acta Neuropathol. (Berl.). 91:1996;6-14.
    • (1996) Acta Neuropathol. (Berl.) , vol.91 , pp. 6-14
    • Claudio, L.1
  • 28
    • 0026022286 scopus 로고
    • Post-traumatic Alzheimer's disease: Preponderance of a single plaque type
    • Clinton J., Ambler M.W., Roberts G.W. Post-traumatic Alzheimer's disease: preponderance of a single plaque type. Neuropathol. Appl. Neurobiol. 17:1991;69-74.
    • (1991) Neuropathol. Appl. Neurobiol. , vol.17 , pp. 69-74
    • Clinton, J.1    Ambler, M.W.2    Roberts, G.W.3
  • 30
    • 0029888642 scopus 로고    scopus 로고
    • Nerve growth factor and ras regulate beta-amyloid precursor protein gene expression in PC12 cells
    • Cosgaya J.M., Latasa M.J., Pascual A. Nerve growth factor and ras regulate beta-amyloid precursor protein gene expression in PC12 cells. J. Neurochem. 67:1996;98-104.
    • (1996) J. Neurochem. , vol.67 , pp. 98-104
    • Cosgaya, J.M.1    Latasa, M.J.2    Pascual, A.3
  • 31
    • 0037474240 scopus 로고    scopus 로고
    • Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid
    • Curtain C.C., Ali F.E., Smith D.G., Bush A.I., Masters C.L., Barnham K.J. Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid. J. Biol. Chem. 278:2003;2977-2982.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2977-2982
    • Curtain, C.C.1    Ali, F.E.2    Smith, D.G.3    Bush, A.I.4    Masters, C.L.5    Barnham, K.J.6
  • 33
    • 0032960553 scopus 로고    scopus 로고
    • Cerebral hypoperfusion yields capillary damage in the hippocampal CA1 area that correlates with spatial memory impairment
    • De Jong G.I., Farkas E., Stienstra C.M., Plass J.R., Keijser J.N., de la Torre J.C., Luiten P.G. Cerebral hypoperfusion yields capillary damage in the hippocampal CA1 area that correlates with spatial memory impairment. Neuroscience. 91:1999;203-210.
    • (1999) Neuroscience , vol.91 , pp. 203-210
    • De Jong, G.I.1    Farkas, E.2    Stienstra, C.M.3    Plass, J.R.4    Keijser, J.N.5    De la Torre, J.C.6    Luiten, P.G.7
  • 34
    • 0030668579 scopus 로고    scopus 로고
    • Hemodynamic consequences of deformed microvessels in the brain in Alzheimer's disease
    • De la Torre J.C. Hemodynamic consequences of deformed microvessels in the brain in Alzheimer's disease. Ann. NY Acad. Sci. 826:1997;75-91.
    • (1997) Ann. NY Acad. Sci. , vol.826 , pp. 75-91
    • De la Torre, J.C.1
  • 35
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
    • Dong J., Atwood C.S., Anderson V.E., Siedlak S.L., Perry G., Smith M.A., Carey P.R. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry. 42:2003;2768-2773.
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Perry, G.5    Smith, M.A.6    Carey, P.R.7
  • 37
    • 0035903270 scopus 로고    scopus 로고
    • Plasmin cleaves Abeta42 in vitro and prevents its aggregation into beta-pleated sheet structures
    • Exley C., Korchazhkina O.V. Plasmin cleaves Abeta42 in vitro and prevents its aggregation into beta-pleated sheet structures. Neuroreport. 12:2001;2967-2970.
    • (2001) Neuroreport , vol.12 , pp. 2967-2970
    • Exley, C.1    Korchazhkina, O.V.2
  • 38
    • 0034603411 scopus 로고    scopus 로고
    • Are Alzheimer's disease, hypertension, and cerebrocapillary damage related?
    • Farkas E., De Vos R.A., Jansen Steur E.N., Luiten P.G. Are Alzheimer's disease, hypertension, and cerebrocapillary damage related? Neurobiol. Aging. 21:2000;235-243.
    • (2000) Neurobiol. Aging , vol.21 , pp. 235-243
    • Farkas, E.1    De Vos, R.A.2    Jansen Steur, E.N.3    Luiten, P.G.4
  • 39
    • 0034987999 scopus 로고    scopus 로고
    • The severity of cortical Alzheimer's type changes is positively correlated with increased amyloid-beta Levels: Resolubilization of amyloid-beta with transition metal ion chelators
    • Fonte J., Miklossy J., Atwood C., Martins R. The severity of cortical Alzheimer's type changes is positively correlated with increased amyloid-beta Levels: Resolubilization of amyloid-beta with transition metal ion chelators. J. Alzheimer's Dis. 1:2001;209-219.
    • (2001) J. Alzheimer's Dis. , vol.1 , pp. 209-219
    • Fonte, J.1    Miklossy, J.2    Atwood, C.3    Martins, R.4
  • 40
    • 0029985732 scopus 로고    scopus 로고
    • Oxidative stress increases production of β-amyloid precursor protein and β-amyloid (A-beta) in mammalian lenses, and A-beta has toxic effects on lens epithelial cells
    • Frederikse P.H., Garland D., Zigler J.S., Piatigorsky J. Oxidative stress increases production of β-amyloid precursor protein and β-amyloid (A-beta) in mammalian lenses, and A-beta has toxic effects on lens epithelial cells. J. Biol. Chem. 271:1996;10169-10174.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10169-10174
    • Frederikse, P.H.1    Garland, D.2    Zigler, J.S.3    Piatigorsky, J.4
  • 41
    • 0029119149 scopus 로고
    • Platelets roll on stimulated endothelium in vivo: An interaction mediated by endothelial P-selectin
    • Frenette P.S., Johnson R.C., Hynes R.O., Wagner D.D. Platelets roll on stimulated endothelium in vivo: an interaction mediated by endothelial P-selectin. Proc. Natl. Acad. Sci. USA. 92:1995;7450-7454.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7450-7454
    • Frenette, P.S.1    Johnson, R.C.2    Hynes, R.O.3    Wagner, D.D.4
  • 43
    • 0026542758 scopus 로고
    • Overexpression of amyloid precursor protein alters its normal processing and is associated with neurotoxicity
    • Fukuchi K., Kamino K., Deeb S.S., Smith A.C., Dang T., Martin G.M. Overexpression of amyloid precursor protein alters its normal processing and is associated with neurotoxicity. Biochem. Biophys. Res. Commun. 182:1992;165-173.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 165-173
    • Fukuchi, K.1    Kamino, K.2    Deeb, S.S.3    Smith, A.C.4    Dang, T.5    Martin, G.M.6
  • 44
    • 0028200649 scopus 로고
    • Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative
    • Gabuzda D., Busciglio J., Chen L.B., Matsudaira P., Yankner B.A. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J. Biol. Chem. 269:1994;13623-13628.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.B.3    Matsudaira, P.4    Yankner, B.A.5
  • 45
    • 0027482350 scopus 로고
    • Beta-amyloid precursor protein (beta APP) as a marker for axonal injury after head injury
    • Gentleman S.M., Nash M.J., Sweeting C.J., Graham D.I., Roberts G.W. Beta-amyloid precursor protein (beta APP) as a marker for axonal injury after head injury. Neurosci. Lett. 160:1993;139-144.
    • (1993) Neurosci. Lett. , vol.160 , pp. 139-144
    • Gentleman, S.M.1    Nash, M.J.2    Sweeting, C.J.3    Graham, D.I.4    Roberts, G.W.5
  • 46
    • 0029033573 scopus 로고
    • Hypoxia-induced brain angiogenesis in the adult rat
    • Harik S.I., Hritz M.A., LaManna J.C. Hypoxia-induced brain angiogenesis in the adult rat. J. Physiol. 485:1995;525-530.
    • (1995) J. Physiol. , vol.485 , pp. 525-530
    • Harik, S.I.1    Hritz, M.A.2    LaManna, J.C.3
  • 48
    • 0034817423 scopus 로고    scopus 로고
    • Advanced glycation end products and the progressive course of renal disease
    • Heidland A., Sebekova K., Schinzel R. Advanced glycation end products and the progressive course of renal disease. Am. J. Kidney Dis. 38:2001;S100-106.
    • (2001) Am. J. Kidney Dis. , vol.38 , pp. 100-106
    • Heidland, A.1    Sebekova, K.2    Schinzel, R.3
  • 54
    • 0018355952 scopus 로고
    • The aging human cerebral cortex: A stereological characterization of changes in the capillary net
    • Hunziker O., Abdel'Al S., Frey H., Veteau M.J., Meier-Ruge W. The aging human cerebral cortex: a stereological characterization of changes in the capillary net. J. Gerontol. 34:1979;345-350.
    • (1979) J. Gerontol. , vol.34 , pp. 345-350
    • Hunziker, O.1    Abdel'Al, S.2    Frey, H.3    Veteau, M.J.4    Meier-Ruge, W.5
  • 55
    • 0035232538 scopus 로고    scopus 로고
    • Beta-amyloid fibrils of Alzheimer's disease: Pathologically altered, basement membrane-associated microfibrils?
    • Inoue S., Kisilevsky R. Beta-amyloid fibrils of Alzheimer's disease: pathologically altered, basement membrane-associated microfibrils? Ital. J. Anat. Embryol. 106:2001;93-102.
    • (2001) Ital. J. Anat. Embryol. , vol.106 , pp. 93-102
    • Inoue, S.1    Kisilevsky, R.2
  • 57
    • 0037010286 scopus 로고    scopus 로고
    • Region-specific reduction of A beta-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging
    • Iwata N., Takaki Y., Fukami S., Tsubuki S., Saido T.C. Region-specific reduction of A beta-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging. J. Neurosci. Res. 70:2002a;493-500.
    • (2002) J. Neurosci. Res. , vol.70 , pp. 493-500
    • Iwata, N.1    Takaki, Y.2    Fukami, S.3    Tsubuki, S.4    Saido, T.C.5
  • 58
    • 0036898083 scopus 로고    scopus 로고
    • Long-term accumulation of amyloid-beta in axons following brain trauma without persistent upregulation of amyloid precursor protein genes
    • Iwata A., Chen X.H., McIntosh T.K., Browne K.D., Smith D. Long-term accumulation of amyloid-beta in axons following brain trauma without persistent upregulation of amyloid precursor protein genes. J. Neuropathol. Exp. Neurol. 61:2002b;1056-1068.
    • (2002) J. Neuropathol. Exp. Neurol. , vol.61 , pp. 1056-1068
    • Iwata, A.1    Chen, X.H.2    McIntosh, T.K.3    Browne, K.D.4    Smith, D.5
  • 59
    • 0025853543 scopus 로고
    • Conservation of the sequence of the Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis
    • Johnstone E.M., Chaney M.O., Norris F.H., Pascual R., Little S.P. Conservation of the sequence of the Alzheimer's disease amyloid peptide in dog, polar bear and five other mammals by cross-species polymerase chain reaction analysis. Mol. Brain Res. 10:1991;299-305.
    • (1991) Mol. Brain Res. , vol.10 , pp. 299-305
    • Johnstone, E.M.1    Chaney, M.O.2    Norris, F.H.3    Pascual, R.4    Little, S.P.5
  • 60
    • 0030452414 scopus 로고    scopus 로고
    • Cerebral vessels in ageing and Alzheimer's disease
    • Kalaria R.N. Cerebral vessels in ageing and Alzheimer's disease. Pharmacol. Ther. 72:1996;193-214.
    • (1996) Pharmacol. Ther. , vol.72 , pp. 193-214
    • Kalaria, R.N.1
  • 62
    • 0033769915 scopus 로고    scopus 로고
    • Capillary changes in hippocampal CA1 and CA3 areas of the aging rhesus monkey
    • Keuker J.I., Luiten P.G., Fuchs E. Capillary changes in hippocampal CA1 and CA3 areas of the aging rhesus monkey. Acta Neuropathol. (Berl.). 100:2000;665-672.
    • (2000) Acta Neuropathol. (Berl.) , vol.100 , pp. 665-672
    • Keuker, J.I.1    Luiten, P.G.2    Fuchs, E.3
  • 63
    • 0028928084 scopus 로고
    • In vitro stimulation of tissue-type plasminogen activator by Alzheimer amyloid beta-peptide analogues
    • Kingston I.B., Castro M.J., Anderson S. In vitro stimulation of tissue-type plasminogen activator by Alzheimer amyloid beta-peptide analogues. Nature Med. 1:1995;138-142.
    • (1995) Nature Med. , vol.1 , pp. 138-142
    • Kingston, I.B.1    Castro, M.J.2    Anderson, S.3
  • 64
    • 0028379203 scopus 로고
    • Inflammation-associated amyloidogenesis. Lessons for Alzheimer's amyloidogenesis
    • Kisilevsky R. Inflammation-associated amyloidogenesis. Lessons for Alzheimer's amyloidogenesis. Mol. Neurobiol. 8:1994;65-66.
    • (1994) Mol. Neurobiol. , vol.8 , pp. 65-66
    • Kisilevsky, R.1
  • 67
    • 0033642957 scopus 로고    scopus 로고
    • Hippocampal capillaries in different age groups of chronically ethanol-intoxicated rats. Morphometrical studies
    • Kraszpulski M., Tukaj C., Wrzolkowa T. Hippocampal capillaries in different age groups of chronically ethanol-intoxicated rats. Morphometrical studies. Folia Morphol. (Warsz.). 59:2000;121-129.
    • (2000) Folia Morphol. (Warsz.) , vol.59 , pp. 121-129
    • Kraszpulski, M.1    Tukaj, C.2    Wrzolkowa, T.3
  • 68
    • 0028176821 scopus 로고
    • Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • Kurochkin I.V., Goto S. Alzheimer's beta-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett. 345:1994;33-37.
    • (1994) FEBS Lett. , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 69
    • 0026761781 scopus 로고
    • Cerebral hemorrhage from amyloid angiopathy and coronary thrombolysis
    • Leblanc R., Haddad G., Robitaille Y. Cerebral hemorrhage from amyloid angiopathy and coronary thrombolysis. Neurosurgery. 31:1992;586-590.
    • (1992) Neurosurgery , vol.31 , pp. 586-590
    • Leblanc, R.1    Haddad, G.2    Robitaille, Y.3
  • 70
    • 0034573026 scopus 로고    scopus 로고
    • Brain plasmin enhances APP alpha-cleavage and Abeta degradation and is reduced in Alzheimer's disease brains
    • Ledesma M.D., Da Silva J.S., Crassaerts K., Delacourte A., De Strooper B., Dotti C.G. Brain plasmin enhances APP alpha-cleavage and Abeta degradation and is reduced in Alzheimer's disease brains. EMBO Rep. 1:2000;530-535.
    • (2000) EMBO Rep. , vol.1 , pp. 530-535
    • Ledesma, M.D.1    Da Silva, J.S.2    Crassaerts, K.3    Delacourte, A.4    De Strooper, B.5    Dotti, C.G.6
  • 72
    • 0033121053 scopus 로고    scopus 로고
    • Understanding the biological activity of amyloid proteins in vitro: From inhibited cellular MTT reduction to altered cellular cholesterol homeostatis
    • Liu Y. Understanding the biological activity of amyloid proteins in vitro: from inhibited cellular MTT reduction to altered cellular cholesterol homeostatis. Prog. Neuropsychopharmacol. Biol. Psychiatry. 23:1999;377-395.
    • (1999) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.23 , pp. 377-395
    • Liu, Y.1
  • 73
    • 0035686804 scopus 로고    scopus 로고
    • Stereological estimates of number and length of capillaries in subdivisions of the human hippocampal region
    • Lokkegaard A., Nyengaard J.R., West M.J. Stereological estimates of number and length of capillaries in subdivisions of the human hippocampal region. Hippocampus. 11:2001;726-740.
    • (2001) Hippocampus , vol.11 , pp. 726-740
    • Lokkegaard, A.1    Nyengaard, J.R.2    West, M.J.3
  • 77
    • 0033576327 scopus 로고    scopus 로고
    • APOE epsilon4 allele and amyloid beta-protein deposition in long term survivors of head injury
    • Macfarlane D.P., Nicoll J.A., Smith C., Graham D.I. APOE epsilon4 allele and amyloid beta-protein deposition in long term survivors of head injury. Neuroreport. 10:1999;3945-3948.
    • (1999) Neuroreport , vol.10 , pp. 3945-3948
    • Macfarlane, D.P.1    Nicoll, J.A.2    Smith, C.3    Graham, D.I.4
  • 78
    • 0028787671 scopus 로고
    • Protease nexin-2/amyloid β-protein precursor inhibits Factor Xa in the prothrombinase complex
    • Mahdi F., Van Nostrand W.E., Schmaier A.H. Protease nexin-2/amyloid β-protein precursor inhibits Factor Xa in the prothrombinase complex. J. Biol. Chem. 270:1995;23468-23474.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23468-23474
    • Mahdi, F.1    Van Nostrand, W.E.2    Schmaier, A.H.3
  • 79
    • 0031982670 scopus 로고    scopus 로고
    • Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease
    • Mattson M.P., Guo Q., Furukawa K., Pedersen W.A. Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease. J. Neurochem. 70:1998;1-14.
    • (1998) J. Neurochem. , vol.70 , pp. 1-14
    • Mattson, M.P.1    Guo, Q.2    Furukawa, K.3    Pedersen, W.A.4
  • 80
    • 0037119577 scopus 로고    scopus 로고
    • Breaking down barriers
    • Miller G. Breaking down barriers. Science. 297:2002;1116-1118.
    • (2002) Science , vol.297 , pp. 1116-1118
    • Miller, G.1
  • 81
    • 0026663993 scopus 로고
    • The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth
    • Milward E.A., Papadopoulos R., Fuller S.J., Moir R.D., Small D., Beyreuther K., Masters C.L. The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron. 9:1992;129-137.
    • (1992) Neuron , vol.9 , pp. 129-137
    • Milward, E.A.1    Papadopoulos, R.2    Fuller, S.J.3    Moir, R.D.4    Small, D.5    Beyreuther, K.6    Masters, C.L.7
  • 82
    • 0141775417 scopus 로고    scopus 로고
    • Oxidative stress induces intracellular accumulation of Alzheimer amyloid-β in human neuroblastoma cells
    • Misonou H., Morioshima-Kawashima M., Ihara Y. Oxidative stress induces intracellular accumulation of Alzheimer amyloid-β in human neuroblastoma cells. Soc. Neurosci. Abstr. 25:1999;340.
    • (1999) Soc. Neurosci. Abstr. , vol.25 , pp. 340
    • Misonou, H.1    Morioshima-Kawashima, M.2    Ihara, Y.3
  • 83
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes
    • Miura T., Suzuki K., Kohata N., Takeuchi H. Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes. Biochemistry. 39:2000;7024-7031.
    • (2000) Biochemistry , vol.39 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 86
    • 0035930452 scopus 로고    scopus 로고
    • Reduced cortical injury and edema in tissue plasminogen activator knockout mice after brain trauma
    • Mori T., Wang X., Kline A.E., Siao C.J., Dixon C.E., Tsirka S.E., Lo E.H. Reduced cortical injury and edema in tissue plasminogen activator knockout mice after brain trauma. Neuroreport. 12:2001;4117-4120.
    • (2001) Neuroreport , vol.12 , pp. 4117-4120
    • Mori, T.1    Wang, X.2    Kline, A.E.3    Siao, C.J.4    Dixon, C.E.5    Tsirka, S.E.6    Lo, E.H.7
  • 89
    • 0025864064 scopus 로고
    • High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan
    • Narindrasorasak S., Lowery D., Gonzalez-DeWhitt P., Poorman R.A., Greenberg B., Kisilevsky R. High affinity interactions between the Alzheimer's beta-amyloid precursor proteins and the basement membrane form of heparan sulfate proteoglycan. J. Biol. Chem. 266:1991;12878-12883.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12878-12883
    • Narindrasorasak, S.1    Lowery, D.2    Gonzalez-DeWhitt, P.3    Poorman, R.A.4    Greenberg, B.5    Kisilevsky, R.6
  • 90
    • 0030611584 scopus 로고    scopus 로고
    • Alpha2-macroglobulin complexes with and mediates the endocytosis of beta-amyloid peptide via cell surface low-density lipoprotein receptor-related protein
    • Narita M., Holtzman D.M., Schwartz A.L., Bu G. Alpha2-macroglobulin complexes with and mediates the endocytosis of beta-amyloid peptide via cell surface low-density lipoprotein receptor-related protein. J. Neurochem. 69:1997;1904-1911.
    • (1997) J. Neurochem. , vol.69 , pp. 1904-1911
    • Narita, M.1    Holtzman, D.M.2    Schwartz, A.L.3    Bu, G.4
  • 91
    • 0028986690 scopus 로고
    • Apolipoprotein E epsilon 4 allele is associated with deposition of amyloid beta-protein following head injury
    • Nicoll J.A., Roberts G.W., Graham D.I. Apolipoprotein E epsilon 4 allele is associated with deposition of amyloid beta-protein following head injury. Nature Med. 1:1995;135-137.
    • (1995) Nature Med. , vol.1 , pp. 135-137
    • Nicoll, J.A.1    Roberts, G.W.2    Graham, D.I.3
  • 93
    • 0026354082 scopus 로고
    • Rapid appearance of beta-amyloid precursor protein immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury
    • Otsuka N., Tomonaga M., Ikeda K. Rapid appearance of beta-amyloid precursor protein immunoreactivity in damaged axons and reactive glial cells in rat brain following needle stab injury. Brain Res. 568:1991;335-338.
    • (1991) Brain Res. , vol.568 , pp. 335-338
    • Otsuka, N.1    Tomonaga, M.2    Ikeda, K.3
  • 95
    • 0025964369 scopus 로고
    • Intracerebral hemorrhage related to cerebral amyloid angiopathy and t-PA treatment
    • Pendlebury W.W., Iole E.D., Tracy R.P., Dill B.A. Intracerebral hemorrhage related to cerebral amyloid angiopathy and t-PA treatment. Ann. Neurol. 29:1991;210-213.
    • (1991) Ann. Neurol. , vol.29 , pp. 210-213
    • Pendlebury, W.W.1    Iole, E.D.2    Tracy, R.P.3    Dill, B.A.4
  • 96
    • 0025341743 scopus 로고
    • Microangiopathy, the vascular basement membrane and Alzheimer's disease: A review
    • Perlmutter L.S., Chui H.C. Microangiopathy, the vascular basement membrane and Alzheimer's disease: a review. Brain Res. Bull. 24:1990;677-686.
    • (1990) Brain Res. Bull. , vol.24 , pp. 677-686
    • Perlmutter, L.S.1    Chui, H.C.2
  • 97
    • 0037062566 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy and cognitive function: The HAAS autopsy study
    • Pfeifer L.A., White L.R., Ross G.W., Petrovitch H., Launer L.J. Cerebral amyloid angiopathy and cognitive function: the HAAS autopsy study. Neurology. 58:2002;1629-1634.
    • (2002) Neurology , vol.58 , pp. 1629-1634
    • Pfeifer, L.A.1    White, L.R.2    Ross, G.W.3    Petrovitch, H.4    Launer, L.J.5
  • 98
    • 0033255377 scopus 로고    scopus 로고
    • Electron microscopy studies on experimental diabetes and cerebral ischemia in the rat brain
    • Piotrowski P., Gajkowska B., Olszewska H., Smialek M. Electron microscopy studies on experimental diabetes and cerebral ischemia in the rat brain. Folia Neuropathol. 37:1999;256-263.
    • (1999) Folia Neuropathol. , vol.37 , pp. 256-263
    • Piotrowski, P.1    Gajkowska, B.2    Olszewska, H.3    Smialek, M.4
  • 99
    • 0033607423 scopus 로고    scopus 로고
    • Ischemic rats as a model in the study of the neurobiological role of human beta-amyloid peptide. Time-dependent disappearing diffuse amyloid plaques in brain
    • Pluta R., Barcikowska M., Misicka A., Lipkowski A.W., Spisacka S., Januszewski S. Ischemic rats as a model in the study of the neurobiological role of human beta-amyloid peptide. Time-dependent disappearing diffuse amyloid plaques in brain. Neuroreport. 10:1999;3615-3619.
    • (1999) Neuroreport , vol.10 , pp. 3615-3619
    • Pluta, R.1    Barcikowska, M.2    Misicka, A.3    Lipkowski, A.W.4    Spisacka, S.5    Januszewski, S.6
  • 100
    • 0034870813 scopus 로고    scopus 로고
    • Permeability of proteins at the blood-brain barrier in the normal adult mouse and double transgenic mouse model of Alzheimer's disease
    • Poduslo J.F., Curran G.L., Wengenack T.M., Malester B., Duff K. Permeability of proteins at the blood-brain barrier in the normal adult mouse and double transgenic mouse model of Alzheimer's disease. Neurobiol. Dis. 8:2001;555-567.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 555-567
    • Poduslo, J.F.1    Curran, G.L.2    Wengenack, T.M.3    Malester, B.4    Duff, K.5
  • 103
    • 0028894661 scopus 로고
    • Multiple, diverse senile plaque-associated proteins are ligands of an apolipoprotein E receptor, the alpha 2-macroglobulin receptor/low-density-lipoprotein receptor-related protein
    • Rebeck G.W., Harr S.D., Strickland D.K., Hyman B.T. Multiple, diverse senile plaque-associated proteins are ligands of an apolipoprotein E receptor, the alpha 2-macroglobulin receptor/low-density-lipoprotein receptor-related protein. Ann. Neurol. 37:1995;211-217.
    • (1995) Ann. Neurol. , vol.37 , pp. 211-217
    • Rebeck, G.W.1    Harr, S.D.2    Strickland, D.K.3    Hyman, B.T.4
  • 105
    • 0028174629 scopus 로고
    • Beta amyloid protein deposition in the brain after severe head injury: Implications for the pathogenesis of Alzheimer's disease
    • Roberts G.W., Gentleman S.M., Lynch A., Murray L., Landon M., Graham D.I. Beta amyloid protein deposition in the brain after severe head injury: implications for the pathogenesis of Alzheimer's disease. J. Neurol. Neurosurg. Psychiatry. 57:1994;419-425.
    • (1994) J. Neurol. Neurosurg. Psychiatry. , vol.57 , pp. 419-425
    • Roberts, G.W.1    Gentleman, S.M.2    Lynch, A.3    Murray, L.4    Landon, M.5    Graham, D.I.6
  • 106
    • 0025840201 scopus 로고
    • Beta A4 amyloid protein deposition in brain after head trauma
    • Roberts G.W., Gentleman S.M., Lynch A., Graham D.I. beta A4 amyloid protein deposition in brain after head trauma. Lancet. 338:1991;1422-1423.
    • (1991) Lancet , vol.338 , pp. 1422-1423
    • Roberts, G.W.1    Gentleman, S.M.2    Lynch, A.3    Graham, D.I.4
  • 107
    • 0028071334 scopus 로고
    • Increase of synaptic density and memory retention by a peptide representing the trophic domain of the amyloid beta/A4 protein precursor
    • Roch J.M., Masliah E., Roch-Levecq A.C., Sundsmo M.P., Otero D.A., Veinbergs I., Saitoh T. Increase of synaptic density and memory retention by a peptide representing the trophic domain of the amyloid beta/A4 protein precursor. Proc. Natl. Acad. Sci. USA. 91:1994;7450-7454.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7450-7454
    • Roch, J.M.1    Masliah, E.2    Roch-Levecq, A.C.3    Sundsmo, M.P.4    Otero, D.A.5    Veinbergs, I.6    Saitoh, T.7
  • 108
    • 0027332081 scopus 로고
    • Beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • Roher A.E., Lowenson J.D., Clarke S., Woods A.S., Cotter R.J., Gowing E., Ball M.J. beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc. Natl. Acad. Sci. USA. 90:1993;10836-10840.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10836-10840
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Woods, A.S.4    Cotter, R.J.5    Gowing, E.6    Ball, M.J.7
  • 109
    • 0035954426 scopus 로고    scopus 로고
    • The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement
    • Sabo S.L., Ikin A.F., Buxbaum J.D., Greengard P. The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J. Cell Biol. 153:2001;1403-1414.
    • (2001) J. Cell Biol. , vol.153 , pp. 1403-1414
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 111
    • 0024395366 scopus 로고
    • Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts
    • Saitoh T., Sundsmo M., Roch J.M., Kimura N., Cole G., Schubert D., Oltersdorf T., Schenk D.B. Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts. Cell. 58:1989;615-622.
    • (1989) Cell , vol.58 , pp. 615-622
    • Saitoh, T.1    Sundsmo, M.2    Roch, J.M.3    Kimura, N.4    Cole, G.5    Schubert, D.6    Oltersdorf, T.7    Schenk, D.B.8
  • 112
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage B., Saldivar E., Ruggeri Z.M. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell. 84:1996;289-297.
    • (1996) Cell , vol.84 , pp. 289-297
    • Savage, B.1    Saldivar, E.2    Ruggeri, Z.M.3
  • 113
    • 0033964859 scopus 로고    scopus 로고
    • In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
    • Sayre L.M., Perry G., Harris P.L., Liu Y., Schubert K.A., Smith M.A. In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J. Neurochem. 74:2000;270-279.
    • (2000) J. Neurochem. , vol.74 , pp. 270-279
    • Sayre, L.M.1    Perry, G.2    Harris, P.L.3    Liu, Y.4    Schubert, K.A.5    Smith, M.A.6
  • 116
    • 0028924689 scopus 로고
    • Factor IXa inhibition by protease nexin-2/amyloid β-protein precursor on phospholipid vesicles and cell membranes
    • Schmaier A.H., Dahl L.D., Hasan A.A.K., Cines D.B., Van Nostrand W.E. Factor IXa inhibition by protease nexin-2/amyloid β-protein precursor on phospholipid vesicles and cell membranes. Biochemistry. 34:1995;1171-1178.
    • (1995) Biochemistry , vol.34 , pp. 1171-1178
    • Schmaier, A.H.1    Dahl, L.D.2    Hasan, A.A.K.3    Cines, D.B.4    Van Nostrand, W.E.5
  • 118
    • 0028587238 scopus 로고
    • Receptor for advanced glycation end products (AGEs) has a central role in vessel wall interactions and gene activation in response to circulating AGE proteins
    • Schmidt A.M., Hasu M., Popov D., Zhang J.H., Chen J., Yan S.D., Brett J., Cao R., Kuwabara K., Costache G., et al. Receptor for advanced glycation end products (AGEs) has a central role in vessel wall interactions and gene activation in response to circulating AGE proteins. Proc. Natl. Acad. Sci. USA. 91:1994;8807-8811.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8807-8811
    • Schmidt, A.M.1    Hasu, M.2    Popov, D.3    Zhang, J.H.4    Chen, J.5    Yan, S.D.6    Brett, J.7    Cao, R.8    Kuwabara, K.9    Costache, G.10
  • 120
    • 0023715001 scopus 로고
    • Direct evidence that complex experience increases capillary branching and surface area in visual cortex of young rats
    • Sirevaag A.M., Black J.E., Shafron D., Greenough W.T. Direct evidence that complex experience increases capillary branching and surface area in visual cortex of young rats. Brain Res. 471:1988;299-304.
    • (1988) Brain Res. , vol.471 , pp. 299-304
    • Sirevaag, A.M.1    Black, J.E.2    Shafron, D.3    Greenough, W.T.4
  • 121
    • 0030885482 scopus 로고    scopus 로고
    • Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
    • Smith M.A., Harris P.L.R., Sayre L.M., Perry G. Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc. Natl. Acad. Sci. USA. 94:1997;9866-9868.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9866-9868
    • Smith, M.A.1    Harris, P.L.R.2    Sayre, L.M.3    Perry, G.4
  • 123
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain
    • Snow A.D., Sekiguchi R., Nochlin D., Fraser P., Kimata K., Mizutani A., Arai M., Schreier W.A., Morgan D.G. An important role of heparan sulfate proteoglycan (Perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain. Neuron. 12:1994;219-234.
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 124
    • 0025147215 scopus 로고
    • Developmental and aging changes in the expression patterns of beta-amyloid in the brains of normal and Down syndrome cases
    • Takashima S., Kuruta H., Mito T., Nishizawa M., Kunishita T., Tabira T. Developmental and aging changes in the expression patterns of beta-amyloid in the brains of normal and Down syndrome cases. Brain Dev. 12:1990;367-371.
    • (1990) Brain Dev. , vol.12 , pp. 367-371
    • Takashima, S.1    Kuruta, H.2    Mito, T.3    Nishizawa, M.4    Kunishita, T.5    Tabira, T.6
  • 125
    • 0033788789 scopus 로고    scopus 로고
    • Tissue plasminogen activator requires plasminogen to modulate amyloid-beta neurotoxicity and deposition
    • Tucker H.M., Kihiko-Ehmann M., Wright S., Rydel R.E., Estus S. Tissue plasminogen activator requires plasminogen to modulate amyloid-beta neurotoxicity and deposition. J. Neurochem. 75:2000a;2172-2177.
    • (2000) J. Neurochem. , vol.75 , pp. 2172-2177
    • Tucker, H.M.1    Kihiko-Ehmann, M.2    Wright, S.3    Rydel, R.E.4    Estus, S.5
  • 128
    • 0037080159 scopus 로고    scopus 로고
    • Repetitive mild brain trauma accelerates Abeta deposition, lipid peroxidation, and cognitive impairment in a transgenic mouse model of Alzheimer amyloidosis
    • Uryu K., Laurer H., McIntosh T., Pratico D., Martinez D., Leight S., Lee V.M., Trojanowski J.Q. Repetitive mild brain trauma accelerates Abeta deposition, lipid peroxidation, and cognitive impairment in a transgenic mouse model of Alzheimer amyloidosis. J. Neurosci. 22:2002;446-454.
    • (2002) J. Neurosci. , vol.22 , pp. 446-454
    • Uryu, K.1    Laurer, H.2    McIntosh, T.3    Pratico, D.4    Martinez, D.5    Leight, S.6    Lee, V.M.7    Trojanowski, J.Q.8
  • 129
    • 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. 38:1999;11570-11576.
    • (1999) Biochemistry , vol.38 , pp. 11570-11576
    • Van Nostrand, W.E.1    Porter, M.2
  • 130
    • 0025371509 scopus 로고
    • Protease nexin-II (amyloid beta-protein precursor): A platelet alpha-granule protein
    • Van Nostrand W.E., Schmaier A.H., Farrow J.S., Cunningham D.D. Protease nexin-II (amyloid beta-protein precursor): a platelet alpha-granule protein. Science. 248:1990a;745-748.
    • (1990) Science , vol.248 , pp. 745-748
    • Van Nostrand, W.E.1    Schmaier, A.H.2    Farrow, J.S.3    Cunningham, D.D.4
  • 131
    • 0034101436 scopus 로고    scopus 로고
    • Cerebrovascular smooth muscle cell surface fibrillar A beta. Alteration of the proteolytic environment in the cerebral vessel wall
    • Van Nostrand W.E., Melchor J., Wagner M., Davis J. Cerebrovascular smooth muscle cell surface fibrillar A beta. Alteration of the proteolytic environment in the cerebral vessel wall. Ann. NY Acad. Sci. 903:2000;89-96.
    • (2000) Ann. NY Acad. Sci. , vol.903 , pp. 89-96
    • Van Nostrand, W.E.1    Melchor, J.2    Wagner, M.3    Davis, J.4
  • 132
    • 0026389694 scopus 로고
    • Platelet protease nexin-2/amyloid beta-protein precursor. Possible pathologic and physiologic functions
    • Van Nostrand W.E., Schmaier A.H., Farrow J.S., Cunningham D.D. Platelet protease nexin-2/amyloid beta-protein precursor. Possible pathologic and physiologic functions. Ann. NY Acad. Sci. 640:1991b;140-144.
    • (1991) Ann. NY Acad. Sci. , vol.640 , pp. 140-144
    • Van Nostrand, W.E.1    Schmaier, A.H.2    Farrow, J.S.3    Cunningham, D.D.4
  • 134
    • 0025357613 scopus 로고
    • Immunopurification and protease inhibitory properties of protease nexin-2/amyloid beta-protein precursor
    • Van Nostrand W.E., Wagner S.L., Farrow J.S., Cunningham D.D. Immunopurification and protease inhibitory properties of protease nexin-2/amyloid beta-protein precursor. J. Biol. Chem. 265:1990b;9591-9594.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9591-9594
    • Van Nostrand, W.E.1    Wagner, S.L.2    Farrow, J.S.3    Cunningham, D.D.4
  • 136
    • 0023254674 scopus 로고
    • Cerebral amyloid angiopathy. A critical review
    • Vinters H.V. Cerebral amyloid angiopathy. A critical review. Stroke. 18:1987;311-324.
    • (1987) Stroke , vol.18 , pp. 311-324
    • Vinters, H.V.1
  • 139
    • 0035930452 scopus 로고    scopus 로고
    • Reduced cortical injury and edema in tissue plasminogen activator knockout mice after brain trauma
    • Mori T., Wang X., Kline A.E., Siao C.J., Dixon C.E., Tsirka S.E., Lo E.H. Reduced cortical injury and edema in tissue plasminogen activator knockout mice after brain trauma. Neuroreport. 12:2001;4117-4120.
    • (2001) Neuroreport , vol.12 , pp. 4117-4120
    • Mori, T.1    Wang, X.2    Kline, A.E.3    Siao, C.J.4    Dixon, C.E.5    Tsirka, S.E.6    Lo, E.H.7
  • 140
    • 0031679480 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy: Amyloid beta accumulates in putative interstitial fluid drainage pathways in Alzheimer's disease
    • Weller R.O., Massey A., Newman T.A., Hutchings M., Kuo Y.M., Roher A.E. Cerebral amyloid angiopathy: amyloid beta accumulates in putative interstitial fluid drainage pathways in Alzheimer's disease. Am. J. Pathol. 153:1998;725-733.
    • (1998) Am. J. Pathol. , vol.153 , pp. 725-733
    • Weller, R.O.1    Massey, A.2    Newman, T.A.3    Hutchings, M.4    Kuo, Y.M.5    Roher, A.E.6
  • 141
    • 0024543836 scopus 로고
    • Amyloid beta protein enhances the survival of hippocampal neurons in vitro. Amyloid beta protein enhances the survival of hippocampal neurons in vitro
    • Whitson J.S., Selkoe D.J., Cotman C.W. Amyloid beta protein enhances the survival of hippocampal neurons in vitro. Amyloid beta protein enhances the survival of hippocampal neurons in vitro. Science. 243:1989;1488-1490.
    • (1989) Science , vol.243 , pp. 1488-1490
    • Whitson, J.S.1    Selkoe, D.J.2    Cotman, C.W.3
  • 142
    • 0028052129 scopus 로고
    • The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein and the receptor-associated protein. An overview
    • Williams S.E., Kounnas M.Z., Argraves K.M., Argraves W.S., Strickland D.K. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein and the receptor-associated protein. An overview. Ann. NY Acad. Sci. 737:1994;1-13.
    • (1994) Ann. NY Acad. Sci. , vol.737 , pp. 1-13
    • Williams, S.E.1    Kounnas, M.Z.2    Argraves, K.M.3    Argraves, W.S.4    Strickland, D.K.5
  • 145
    • 0031079734 scopus 로고    scopus 로고
    • Amyloid beta peptides stimulate tissue-type plasminogen activator but not recombinant prourokinase
    • Wnendt S., Wetzels I., Gunzler W.A. Amyloid beta peptides stimulate tissue-type plasminogen activator but not recombinant prourokinase. Thromb. Res. 85:1997;217-224.
    • (1997) Thromb. Res. , vol.85 , pp. 217-224
    • Wnendt, S.1    Wetzels, I.2    Gunzler, W.A.3
  • 148
    • 0024997546 scopus 로고
    • Neural differentiation increases expression of Alzheimer amyloid protein precursor gene in murine embryonal carcinoma cells
    • Yoshikawa K., Aizawa T., Maruyama K. Neural differentiation increases expression of Alzheimer amyloid protein precursor gene in murine embryonal carcinoma cells. Biochem. Biophys. Res. Commun. 171:1990;204-209.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 204-209
    • Yoshikawa, K.1    Aizawa, T.2    Maruyama, K.3
  • 149
    • 0037096251 scopus 로고    scopus 로고
    • A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage
    • Zou K., Gong J.S., Yanagisawa K., Michikawa M. A novel function of monomeric amyloid beta-protein serving as an antioxidant molecule against metal-induced oxidative damage. J. Neurosci. 22:2002;4833-4841.
    • (2002) J. Neurosci. , vol.22 , pp. 4833-4841
    • Zou, K.1    Gong, J.S.2    Yanagisawa, K.3    Michikawa, M.4


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