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Volumn 223, Issue 2, 2010, Pages 299-303

Pathological role of hypoxia in Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid ; Blood brain barrier; Hypoxia; Neuron degeneration; Tau

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; TAU PROTEIN;

EID: 77952549255     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2009.07.033     Document Type: Review
Times cited : (154)

References (61)
  • 3
    • 48749090279 scopus 로고    scopus 로고
    • Mechanism of tau-induced neurodegeneration in Alzheimer disease and related tauopathies
    • Alonso A.C., Li B., Grundke-Iqbal I., Iqbal K. Mechanism of tau-induced neurodegeneration in Alzheimer disease and related tauopathies. Curr. Alzheimer Res. 2008, 5:375-384.
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 375-384
    • Alonso, A.C.1    Li, B.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 7
    • 34247874678 scopus 로고    scopus 로고
    • Iron, oxidative stress and early neurological deterioration in ischemic stroke
    • Carbonell T., Rama R. Iron, oxidative stress and early neurological deterioration in ischemic stroke. Curr. Med. Chem. 2007, 14:857-874.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 857-874
    • Carbonell, T.1    Rama, R.2
  • 8
    • 0142042435 scopus 로고    scopus 로고
    • Transient hypoxia causes Alzheimer-type molecular and biochemical abnormalities in cortical neurons: potential strategies for neuroprotection
    • Chen G.J., Xu J., Lahousse S.A., Caggiano N.L., de M.S. Transient hypoxia causes Alzheimer-type molecular and biochemical abnormalities in cortical neurons: potential strategies for neuroprotection. J. Alzheimers Dis. 2003, 5:209-228.
    • (2003) J. Alzheimers Dis. , vol.5 , pp. 209-228
    • Chen, G.J.1    Xu, J.2    Lahousse, S.A.3    Caggiano, N.L.4    de, M.S.5
  • 10
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-secretase complex
    • De S.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, S.B.1
  • 13
    • 9244263071 scopus 로고    scopus 로고
    • BACE1 and presenilin: two unusual aspartyl proteases involved in Alzheimer's disease
    • Dominguez D.I., Hartmann D., De S.B. BACE1 and presenilin: two unusual aspartyl proteases involved in Alzheimer's disease. Neurodegener. Dis. 2004, 1:168-174.
    • (2004) Neurodegener. Dis. , vol.1 , pp. 168-174
    • Dominguez, D.I.1    Hartmann, D.2    De, S.B.3
  • 15
    • 3242684407 scopus 로고    scopus 로고
    • Experimental cerebral hypoperfusion induces white matter injury and microglial activation in the rat brain
    • Farkas E., Donka G., de Vos R.A., Mihaly A., Bari F., Luiten P.G. Experimental cerebral hypoperfusion induces white matter injury and microglial activation in the rat brain. Acta Neuropathol. 2004, 108:57-64.
    • (2004) Acta Neuropathol. , vol.108 , pp. 57-64
    • Farkas, E.1    Donka, G.2    de Vos, R.A.3    Mihaly, A.4    Bari, F.5    Luiten, P.G.6
  • 16
    • 34547240466 scopus 로고    scopus 로고
    • Effects of hypoxia and oxidative stress on expression of neprilysin in human neuroblastoma cells and rat cortical neurones and astrocytes
    • Fisk L., Nalivaeva N.N., Boyle J.P., Peers C.S., Turner A.J. Effects of hypoxia and oxidative stress on expression of neprilysin in human neuroblastoma cells and rat cortical neurones and astrocytes. Neurochem. Res. 2007, 32:1741-1748.
    • (2007) Neurochem. Res. , vol.32 , pp. 1741-1748
    • Fisk, L.1    Nalivaeva, N.N.2    Boyle, J.P.3    Peers, C.S.4    Turner, A.J.5
  • 17
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 18
    • 51149120624 scopus 로고    scopus 로고
    • Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice
    • Hickman S.E., Allison E.K., El Khoury J. Microglial dysfunction and defective beta-amyloid clearance pathways in aging Alzheimer's disease mice. J. Neurosci. 2008, 28:8354-8360.
    • (2008) J. Neurosci. , vol.28 , pp. 8354-8360
    • Hickman, S.E.1    Allison, E.K.2    El Khoury, J.3
  • 19
    • 13244274911 scopus 로고    scopus 로고
    • Atherosclerosis and AD: analysis of data from the US National Alzheimer's Coordinating Center
    • Honig L.S., Kukull W., Mayeux R. Atherosclerosis and AD: analysis of data from the US National Alzheimer's Coordinating Center. Neurology 2005, 64:494-500.
    • (2005) Neurology , vol.64 , pp. 494-500
    • Honig, L.S.1    Kukull, W.2    Mayeux, R.3
  • 21
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F.M. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. Neurosci. 2002, 3:862-872.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 22
    • 0037102626 scopus 로고    scopus 로고
    • Oxidative DNA damage induced by copper and hydrogen peroxide promotes CG->TT tandem mutations at methylated CpG dinucleotides in nucleotide excision repair-deficient cells
    • Lee D.H., O'Commor T.R., Pfeifer G.P. Oxidative DNA damage induced by copper and hydrogen peroxide promotes CG->TT tandem mutations at methylated CpG dinucleotides in nucleotide excision repair-deficient cells. Nucleic Acids Res. 2002, 30:3566-3573.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3566-3573
    • Lee, D.H.1    O'Commor, T.R.2    Pfeifer, G.P.3
  • 23
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring M.A., Farris W., Chang A.Y., Walsh D.M., Wu X., Sun X., Frosch M.P., Selkoe D.J. Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 2003, 40:1087-1093.
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 24
    • 64349114305 scopus 로고    scopus 로고
    • Hypoxia increases Abeta generation by altering beta- and gamma-cleavage of APP
    • Li L., Zhang X., Yang D., Luo G., Chen S., Le W. Hypoxia increases Abeta generation by altering beta- and gamma-cleavage of APP. Neurobiol. Aging 2009, 30:1091-1098.
    • (2009) Neurobiol. Aging , vol.30 , pp. 1091-1098
    • Li, L.1    Zhang, X.2    Yang, D.3    Luo, G.4    Chen, S.5    Le, W.6
  • 25
    • 0036627214 scopus 로고    scopus 로고
    • Circulating amyloid-beta peptide crosses the blood-brain barrier in aged monkeys and contributes to Alzheimer's disease lesions
    • Mackic J.B., Bading J., Ghiso J., Walker L., Wisniewski T., Frangione B., Zlokovic B.V. Circulating amyloid-beta peptide crosses the blood-brain barrier in aged monkeys and contributes to Alzheimer's disease lesions. Vascul. Pharmacol. 2002, 38:303-313.
    • (2002) Vascul. Pharmacol. , vol.38 , pp. 303-313
    • Mackic, J.B.1    Bading, J.2    Ghiso, J.3    Walker, L.4    Wisniewski, T.5    Frangione, B.6    Zlokovic, B.V.7
  • 26
    • 50249143450 scopus 로고    scopus 로고
    • Amyloid beta-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin
    • Malito E., Hulse R.E., Tang W.J. Amyloid beta-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin. Cell. Mol. Life Sci. 2008, 65:2574-2585.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2574-2585
    • Malito, E.1    Hulse, R.E.2    Tang, W.J.3
  • 27
    • 0036931159 scopus 로고    scopus 로고
    • Tau neurofibrillary pathology and microtubule stability
    • Michaelis M.L., Dobrowsky R.T., Li G. Tau neurofibrillary pathology and microtubule stability. J. Mol. Neurosci. 2002, 19:289-293.
    • (2002) J. Mol. Neurosci. , vol.19 , pp. 289-293
    • Michaelis, M.L.1    Dobrowsky, R.T.2    Li, G.3
  • 28
    • 0036227489 scopus 로고    scopus 로고
    • Substitution at codon 22 reduces clearance of Alzheimer's amyloid-beta peptide from the cerebrospinal fluid and prevents its transport from the central nervous system into blood
    • Monro O.R., Mackic J.B., Yamada S., Segal M.B., Ghiso J., Maurer C., Calero M., Frangione B., Zlokovic B.V. Substitution at codon 22 reduces clearance of Alzheimer's amyloid-beta peptide from the cerebrospinal fluid and prevents its transport from the central nervous system into blood. Neurobiol. Aging 2002, 23:405-412.
    • (2002) Neurobiol. Aging , vol.23 , pp. 405-412
    • Monro, O.R.1    Mackic, J.B.2    Yamada, S.3    Segal, M.B.4    Ghiso, J.5    Maurer, C.6    Calero, M.7    Frangione, B.8    Zlokovic, B.V.9
  • 29
    • 2942625603 scopus 로고    scopus 로고
    • Neuroprotectin D1: a docosahexaenoic acid-derived docosatriene protects human retinal pigment epithelial cells from oxidative stress
    • Mukherjee P.K., Marcheselli V.L., Serhan C.N., Bazan N.G. Neuroprotectin D1: a docosahexaenoic acid-derived docosatriene protects human retinal pigment epithelial cells from oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:8491-8496.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8491-8496
    • Mukherjee, P.K.1    Marcheselli, V.L.2    Serhan, C.N.3    Bazan, N.G.4
  • 31
    • 58149388879 scopus 로고    scopus 로고
    • Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: a mechanistic link between Abeta and tau pathology
    • Oddo S., Caccamo A., Tseng B., Cheng D., Vasilevko V., Cribbs D.H., LaFerla F.M. Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: a mechanistic link between Abeta and tau pathology. J. Neurosci. 2008, 28:12163-12175.
    • (2008) J. Neurosci. , vol.28 , pp. 12163-12175
    • Oddo, S.1    Caccamo, A.2    Tseng, B.3    Cheng, D.4    Vasilevko, V.5    Cribbs, D.H.6    LaFerla, F.M.7
  • 32
    • 37549011413 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates neuronal expression of the receptor for advanced glycation end products following hypoxia/ischemia
    • Pichiule P., Chavez J.C., Schmidt A.M., Vannucci S.J. Hypoxia-inducible factor-1 mediates neuronal expression of the receptor for advanced glycation end products following hypoxia/ischemia. J. Biol. Chem. 2007, 282:36330-36340.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36330-36340
    • Pichiule, P.1    Chavez, J.C.2    Schmidt, A.M.3    Vannucci, S.J.4
  • 33
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner F., Angelo M., Giese K.P. The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J. Biol. Chem. 2006, 281:25457-25465.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 34
    • 26044455494 scopus 로고    scopus 로고
    • Pathological opening of the blood-brain barrier to horseradish peroxidase and amyloid precursor protein following ischemia-reperfusion brain injury
    • Pluta R. Pathological opening of the blood-brain barrier to horseradish peroxidase and amyloid precursor protein following ischemia-reperfusion brain injury. Chemotherapy 2005, 51:223-226.
    • (2005) Chemotherapy , vol.51 , pp. 223-226
    • Pluta, R.1
  • 35
    • 0032239951 scopus 로고    scopus 로고
    • Cerebral accumulation of beta-amyloid following ischemic brain injury with long-term survival
    • Pluta R., Barcikowska M., Mossakowski M.J., Zelman I. Cerebral accumulation of beta-amyloid following ischemic brain injury with long-term survival. Acta Neurochir. Suppl. 1998, 71:206-208.
    • (1998) Acta Neurochir. Suppl. , vol.71 , pp. 206-208
    • Pluta, R.1    Barcikowska, M.2    Mossakowski, M.J.3    Zelman, I.4
  • 37
    • 0343384322 scopus 로고    scopus 로고
    • Differential association of tau with subsets of microtubules containing posttranslationally-modified tubulin variants in neuroblastoma cells
    • Saragoni L., Hernandez P., Maccioni R.B. Differential association of tau with subsets of microtubules containing posttranslationally-modified tubulin variants in neuroblastoma cells. Neurochem. Res. 2000, 25:59-70.
    • (2000) Neurochem. Res. , vol.25 , pp. 59-70
    • Saragoni, L.1    Hernandez, P.2    Maccioni, R.B.3
  • 39
    • 3042522883 scopus 로고    scopus 로고
    • The role of iron neurotoxicity in ischemic stroke
    • Selim M.H., Ratan R.R. The role of iron neurotoxicity in ischemic stroke. Ageing Res. Rev. 2004, 3:345-353.
    • (2004) Ageing Res. Rev. , vol.3 , pp. 345-353
    • Selim, M.H.1    Ratan, R.R.2
  • 41
    • 0027243585 scopus 로고
    • A new perspective on ischemic brain damage?
    • Siesjo B.K. A new perspective on ischemic brain damage?. Prog. Brain Res. 1993, 96:1-9.
    • (1993) Prog. Brain Res. , vol.96 , pp. 1-9
    • Siesjo, B.K.1
  • 42
    • 0036833572 scopus 로고    scopus 로고
    • Nitric oxide and hydroxyl radical-induced retinal lipid peroxidation in vitro
    • Siu A.W., To C.H. Nitric oxide and hydroxyl radical-induced retinal lipid peroxidation in vitro. Clin. Exp. Optom. 2002, 85:378-382.
    • (2002) Clin. Exp. Optom. , vol.85 , pp. 378-382
    • Siu, A.W.1    To, C.H.2
  • 44
    • 0026646280 scopus 로고
    • Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat
    • Stephenson D.T., Rash K., Clemens J.A. Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischemia in the rat. Brain Res. 1992, 593:128-135.
    • (1992) Brain Res. , vol.593 , pp. 128-135
    • Stephenson, D.T.1    Rash, K.2    Clemens, J.A.3
  • 46
    • 38449107280 scopus 로고    scopus 로고
    • Pathogenesis of Alzheimer's disease
    • Swerdlow R.H. Pathogenesis of Alzheimer's disease. Clin. Interv. Aging 2007, 2:347-359.
    • (2007) Clin. Interv. Aging , vol.2 , pp. 347-359
    • Swerdlow, R.H.1
  • 47
    • 0036139570 scopus 로고    scopus 로고
    • Blood-brain barrier disruption in white matter lesions in a rat model of chronic cerebral hypoperfusion
    • Ueno M., Tomimoto H., Akiguchi I., Wakita H., Sakamoto H. Blood-brain barrier disruption in white matter lesions in a rat model of chronic cerebral hypoperfusion. J. Cereb. Blood Flow Metab. 2002, 22:97-104.
    • (2002) J. Cereb. Blood Flow Metab. , vol.22 , pp. 97-104
    • Ueno, M.1    Tomimoto, H.2    Akiguchi, I.3    Wakita, H.4    Sakamoto, H.5
  • 48
    • 0030833577 scopus 로고    scopus 로고
    • Cerebrovascular smooth muscle cells internalize Alzheimer amyloid beta protein via a lipoprotein pathway: implications for cerebral amyloid angiopathy
    • Urmoneit B., Prikulis I., Wihl G., D'Urso D., Frank R., Heeren J., Beisiegel U., Prior R. Cerebrovascular smooth muscle cells internalize Alzheimer amyloid beta protein via a lipoprotein pathway: implications for cerebral amyloid angiopathy. Lab. Invest. 1997, 77:157-166.
    • (1997) Lab. Invest. , vol.77 , pp. 157-166
    • Urmoneit, B.1    Prikulis, I.2    Wihl, G.3    D'Urso, D.4    Frank, R.5    Heeren, J.6    Beisiegel, U.7    Prior, R.8
  • 49
    • 33845674064 scopus 로고    scopus 로고
    • Transcriptional regulation of APH-1A and increased gamma-secretase cleavage of APP and Notch by HIF-1 and hypoxia
    • Wang R., Zhang Y.W., Zhang X., Liu R., Zhang X., Hong S., Xia K., Xia J., Zhang Z., Xu H. Transcriptional regulation of APH-1A and increased gamma-secretase cleavage of APP and Notch by HIF-1 and hypoxia. FASEB J. 2006, 20:1275-1277.
    • (2006) FASEB J. , vol.20 , pp. 1275-1277
    • Wang, R.1    Zhang, Y.W.2    Zhang, X.3    Liu, R.4    Zhang, X.5    Hong, S.6    Xia, K.7    Xia, J.8    Zhang, Z.9    Xu, H.10
  • 50
    • 11144251210 scopus 로고    scopus 로고
    • Hypoxic pulmonary vasoconstriction: redox events in oxygen sensing
    • Waypa G.B., Schumacker P.T. Hypoxic pulmonary vasoconstriction: redox events in oxygen sensing. J. Appl. Physiol. 2005, 98:404-414.
    • (2005) J. Appl. Physiol. , vol.98 , pp. 404-414
    • Waypa, G.B.1    Schumacker, P.T.2
  • 51
    • 2542428253 scopus 로고    scopus 로고
    • Transient cerebral ischemia induces aberrant neuronal cell cycle re-entry and Alzheimer's disease-like tauopathy in female rats
    • Wen Y., Yang S., Liu R., Brun-Zinkernagel A.M., Koulen P., Simpkins J.W. Transient cerebral ischemia induces aberrant neuronal cell cycle re-entry and Alzheimer's disease-like tauopathy in female rats. J. Biol. Chem. 2004, 279:22684-22692.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22684-22692
    • Wen, Y.1    Yang, S.2    Liu, R.3    Brun-Zinkernagel, A.M.4    Koulen, P.5    Simpkins, J.W.6
  • 52
    • 18244398919 scopus 로고    scopus 로고
    • NF-kappaB activation plays a role in superoxide-mediated cerebral endothelial dysfunction after hypoxia/reoxygenation
    • Xie H., Ray P.E., Short B.L. NF-kappaB activation plays a role in superoxide-mediated cerebral endothelial dysfunction after hypoxia/reoxygenation. Stroke 2005, 36:1047-1052.
    • (2005) Stroke , vol.36 , pp. 1047-1052
    • Xie, H.1    Ray, P.E.2    Short, B.L.3
  • 53
    • 0036169830 scopus 로고    scopus 로고
    • Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells
    • Yamamoto T., Maruyama W., Kato Y., Yi H., Shamoto-Nagai M., Tanaka M., Sato Y., Naoi M. Selective nitration of mitochondrial complex I by peroxynitrite: involvement in mitochondria dysfunction and cell death of dopaminergic SH-SY5Y cells. J. Neural. Transm. 2002, 109:1-13.
    • (2002) J. Neural. Transm. , vol.109 , pp. 1-13
    • Yamamoto, T.1    Maruyama, W.2    Kato, Y.3    Yi, H.4    Shamoto-Nagai, M.5    Tanaka, M.6    Sato, Y.7    Naoi, M.8
  • 54
    • 33947512432 scopus 로고    scopus 로고
    • Interferon-gamma and tumor necrosis factor-alpha regulate amyloid-beta plaque deposition and beta-secretase expression in Swedish mutant APP transgenic mice
    • Yamamoto M., Kiyota T., Horiba M., Buescher J.L., Walsh S.M., Gendelman H.E., Ikezu T. Interferon-gamma and tumor necrosis factor-alpha regulate amyloid-beta plaque deposition and beta-secretase expression in Swedish mutant APP transgenic mice. Am. J. Pathol. 2007, 170:680-692.
    • (2007) Am. J. Pathol. , vol.170 , pp. 680-692
    • Yamamoto, M.1    Kiyota, T.2    Horiba, M.3    Buescher, J.L.4    Walsh, S.M.5    Gendelman, H.E.6    Ikezu, T.7
  • 56
    • 54149084726 scopus 로고    scopus 로고
    • Effects of ginkgo biloba extract EGb761 on expression of RAGE and LRP-1 in cerebral microvascular endothelial cells under chronic hypoxia and hypoglycemia
    • Yan F.L., Zheng Y., Zhao F.D. Effects of ginkgo biloba extract EGb761 on expression of RAGE and LRP-1 in cerebral microvascular endothelial cells under chronic hypoxia and hypoglycemia. Acta Neuropathol. 2008, 116:529-535.
    • (2008) Acta Neuropathol. , vol.116 , pp. 529-535
    • Yan, F.L.1    Zheng, Y.2    Zhao, F.D.3
  • 58
    • 33846021307 scopus 로고    scopus 로고
    • Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Abeta42 accumulation in amyloid model mice
    • Zerbinatti C.V., Wahrle S.E., Kim H., Cam J.A., Bales K., Paul S.M., Holtzman D.M., Bu G. Apolipoprotein E and low density lipoprotein receptor-related protein facilitate intraneuronal Abeta42 accumulation in amyloid model mice. J. Biol. Chem. 2006, 281:36180-36186.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36180-36186
    • Zerbinatti, C.V.1    Wahrle, S.E.2    Kim, H.3    Cam, J.A.4    Bales, K.5    Paul, S.M.6    Holtzman, D.M.7    Bu, G.8
  • 59
    • 34249727115 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha)-mediated hypoxia increases BACE1 expression and beta-amyloid generation
    • Zhang X., Zhou K., Wang R., Cui J., Lipton S.A., Liao F.F., Xu H., Zhang Y.W. Hypoxia-inducible factor 1alpha (HIF-1alpha)-mediated hypoxia increases BACE1 expression and beta-amyloid generation. J. Biol. Chem. 2007, 282:10873-10880.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10873-10880
    • Zhang, X.1    Zhou, K.2    Wang, R.3    Cui, J.4    Lipton, S.A.5    Liao, F.F.6    Xu, H.7    Zhang, Y.W.8
  • 60
    • 33750982682 scopus 로고    scopus 로고
    • Cathepsin D-mediated proteolysis of apolipoprotein E: possible role in Alzheimer's disease
    • Zhou W., Scott S.A., Shelton S.B., Crutcher K.A. Cathepsin D-mediated proteolysis of apolipoprotein E: possible role in Alzheimer's disease. Neuroscience 2006, 143:689-701.
    • (2006) Neuroscience , vol.143 , pp. 689-701
    • Zhou, W.1    Scott, S.A.2    Shelton, S.B.3    Crutcher, K.A.4
  • 61


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