메뉴 건너뛰기




Volumn 1814, Issue 5, 2011, Pages 592-609

Binding studies of truncated variants of the Aβ peptide to the V-domain of the RAGE receptor reveal Aβ residues responsible for binding

Author keywords

Alzheimer's disease; Amyloid peptide; Fluorescence; Mass spectrometry; Receptor for advanced glycation endproducts

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; TRYPTOPHAN;

EID: 79955115531     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.02.011     Document Type: Article
Times cited : (34)

References (85)
  • 1
    • 0000858425 scopus 로고
    • Über eine eigenartige Erkrankung der Hirnrinde
    • A. Alzheimer Über eine eigenartige Erkrankung der Hirnrinde Neurologisches Centralblatt 23 1907 1129 1136
    • (1907) Neurologisches Centralblatt , vol.23 , pp. 1129-1136
    • Alzheimer, A.1
  • 2
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • D.J. Selkoe The molecular pathology of Alzheimer's disease Neuron 6 1991 487 498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 3
    • 0028218871 scopus 로고
    • Neuropathological changes in Alzheimer disease
    • R.D. Terry Neuropathological changes in Alzheimer disease Prog. Brain Res. 101 1994 383 390 (Pubitemid 24084762)
    • (1994) Progress in Brain Research , vol.101 , pp. 383-390
    • Terry, R.D.1
  • 4
    • 0027332081 scopus 로고
    • Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: Implications for the pathology of Alzheimer disease
    • A.E. Roher, J.D. Lowenson, S. Clarke, A.S. Woods, R.J. Cotter, E. Gowing, and M.J. Ball 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
  • 5
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • G.G. Glenner, and C.W. Wong Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein Biochem. Biophys. Res. Commun. 122 1984 1131 1135 (Pubitemid 14027629)
    • (1984) Biochemical and Biophysical Research Communications , vol.122 , Issue.3 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 6
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta-and gammasecretases
    • J. Nunan, and D.H. Small Regulation of APP cleavage by alpha-, beta-and gammasecretases FEBS Lett. 483 2000 6 10
    • (2000) FEBS Lett. , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 7
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid beta protein: Reversal by tachykinin neuropeptides
    • B.A. Yankner, L.K. Duffy, and D.A. Kirschner Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides Science 250 1990 279 282
    • (1990) Science , vol.250 , pp. 279-282
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3
  • 8
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to 26 β-protein neurotoxicity
    • DOI 10.1038/nm0798-827
    • C. Geula, C.K. Wu, D. Saroff, A. Lorenzo, M. Yuan, and B.A. Yankner Aging renders the brain vulnerable to amyloid beta-protein neurotoxicity Nat. Med. 4 1998 827 831 (Pubitemid 28331025)
    • (1998) Nature Medicine , vol.4 , Issue.7 , pp. 827-831
    • Geula, C.1    Wu, C.-K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6
  • 9
    • 0032014664 scopus 로고    scopus 로고
    • The neurotoxicity of amyloid beta protein in aged primates
    • A.C. McKee, N.W. Kowall, J.S. Schumacher, and M.F. Beal The neurotoxicity of amyloid beta protein in aged primates Amyloid 5 1998 1 9 (Pubitemid 128691210)
    • (1998) Amyloid , vol.5 , Issue.1 , pp. 1-9
    • McKee, A.C.1    Kowall, N.W.2    Schumacher, J.S.3    Beal, M.F.4
  • 10
    • 0025992417 scopus 로고
    • In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity
    • C.J. Pike, A.J. Walencewicz, C.G. Glabe, and C.W. Cotman In vitro aging of beta-amyloid protein causes peptide aggregation and neurotoxicity Brain Res. 563 1991 311 314
    • (1991) Brain Res. , vol.563 , pp. 311-314
    • Pike, C.J.1    Walencewicz, A.J.2    Glabe, C.G.3    Cotman, C.W.4
  • 11
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • J.A. Hardy, and G.A. Higgins Alzheimer's disease: the amyloid cascade hypothesis Science 256 1992 184 185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 12
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • D.J. Selkoe Translating cell biology into therapeutic advances in Alzheimer's disease Nature 399 1999 A23 A31
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 13
    • 0035313923 scopus 로고    scopus 로고
    • Alzheimer's disease: β-amyloid hypothesis strengthened!
    • R. Gerlai Alzheimer's disease: beta-amyloid hypothesis strengthened! Trends Neurosci. 24 2001 199 (Pubitemid 32204369)
    • (2001) Trends in Neurosciences , vol.24 , Issue.4 , pp. 199
    • Gerlai, R.1
  • 14
    • 0035433962 scopus 로고    scopus 로고
    • Alzheimer's disease and Aβ toxicity: From top to bottom
    • DOI 10.1038/35086072
    • D.H. Small, S.S. Mok, and J.C. Bornstein Alzheimer's disease and Abeta toxicity: from top to bottom Nat. Rev. Neurosci. 2 2001 595 598 (Pubitemid 33679833)
    • (2001) Nature Reviews Neuroscience , vol.2 , Issue.8 , pp. 595-598
    • Small, D.H.1    Mok, S.S.2    Bornstein, J.C.3
  • 15
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small A β oligomers: The solution to an Alzheimer's disease conundrum?
    • DOI 10.1016/S0166-2236(00)01749-5, PII S0166223600017495
    • W.L. Klein, G.A. Krafft, and C.E. Finch Targeting small Abeta oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. 24 2001 219 224 (Pubitemid 32204378)
    • (2001) Trends in Neurosciences , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 16
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • D.M. Walsh, I. Klyubin, J.V. Fadeeva, W.K. Cullen, R. Anwyl, M.S. Wolfe, M.J. Rowan, and D.J. Selkoe Naturally secreted oligomers of amyloid β-protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 2002 535 539 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 17
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • D.M. Hartley, D.M. Walsh, C.P. Ye, T. Diehl, S. Vasquez, P.M. Vassilev, D.B. Teplow, and D.J. Selkoe Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons J. Neurosci. 19 1999 8876 8884 (Pubitemid 30226709)
    • (1999) Journal of Neuroscience , vol.19 , Issue.20 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 19
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid β-peptide
    • DOI 10.1038/nrm2101, PII NRM2101
    • C. Haass, and D.J. Selkoe Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide Nature Reviews. Mol. Cell. Biol. 8 2007 101 112 (Pubitemid 46432529)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 24
    • 0022156464 scopus 로고
    • Neuronal origin of a cerebral amyloid: Neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • C.L. Masters, G. Multhaup, G. Simms, J. Pottgiesser, R.N. Martins, and K. Beyreuther Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels EMBO J. 4 1985 2757 2763
    • (1985) EMBO J. , vol.4 , pp. 2757-2763
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 25
    • 0024723475 scopus 로고
    • Expression of beta-amyloid precursor protein in reactive astrocytes following neuronal damage
    • R. Siman, J.P. Card, R.B. Nelson, and L.G. Davis Expression of beta-amyloid precursor protein in reactive astrocytes following neuronal damage Neuron 3 1989 275 285
    • (1989) Neuron , vol.3 , pp. 275-285
    • Siman, R.1    Card, J.P.2    Nelson, R.B.3    Davis, L.G.4
  • 26
    • 0030628788 scopus 로고    scopus 로고
    • Can blood-brain barrier play a role in the development of cerebral amyloidosis and Alzheimer's disease pathology
    • B.V. Zlokovic Can blood-brain barrier play a role in the development of cerebral amyloidosis and Alzheimer's disease pathology Neurobiol. Dis. 4 1997 23 26
    • (1997) Neurobiol. Dis. , vol.4 , pp. 23-26
    • Zlokovic, B.V.1
  • 27
    • 0032529151 scopus 로고    scopus 로고
    • Human blood-brain barrier receptors for Alzheimer's amyloid-β 1-40. Asymmetrical binding, endocytosis, and transcytosis at the apical side of brain microvascular endothelial cell monolayer
    • J.B. Mackic, M. Stins, J.G. McComb, M. Calero, J. Ghiso, K.S. Kim, S.D. Yan, D. Stern, A.M. Schmidt, B. Frangione, and B.V. Zlokovic Human blood-brain barrier receptors for Alzheimer amyloid-β1-40 assymetrical binding, endocytosis and transcytosis at the apical side of brain microvascular endothelial cell monolayer J. Clin. Invest. 102 1998 734 743 (Pubitemid 28399606)
    • (1998) Journal of Clinical Investigation , vol.102 , Issue.4 , pp. 734-743
    • Mackic, J.B.1    Stins, M.2    McComb, J.G.3    Calero, M.4    Ghiso, J.5    Kim, K.S.6    Yan, S.D.7    Stern, D.8    Schmidt, A.M.9    Frangione, B.10    Zlokovic, B.V.11
  • 31
    • 65649105035 scopus 로고    scopus 로고
    • Clearance of amyloid-beta peptide across the blood-brain barrier: Implication for therapies in Alzheimer's disease
    • R. Deane, R.D. Bell, A. Sagare, and B.V. Zlokovic Clearance of amyloid-beta peptide across the blood-brain barrier: implication for therapies in Alzheimer's disease CNS Neurol. Disord. Drug Targets 8 2009 16 30
    • (2009) CNS Neurol. Disord. Drug Targets , vol.8 , pp. 16-30
    • Deane, R.1    Bell, R.D.2    Sagare, A.3    Zlokovic, B.V.4
  • 32
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • F.M. LaFerla, K.N. Green, and S. Oddo Intracellular amyloid-beta in Alzheimer's disease Nat. Rev. Neurosci. 8 7 2007 Jul 499 509
    • (2007) Nat. Rev. Neurosci. , vol.8 , Issue.7 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 33
    • 67349093525 scopus 로고    scopus 로고
    • Clearance mechanisms of Alzheimer's amyloid-beta peptide: Implications for therapeutic design and diagnostic tests
    • K.A. Bates, G. Verdile, Q.S. Li, D. Ames, P. Hudson, C.L. Masters, and R.N. Martins Clearance mechanisms of Alzheimer's amyloid-beta peptide: implications for therapeutic design and diagnostic tests Mol. Psychiatry 14 2009 469 486
    • (2009) Mol. Psychiatry , vol.14 , pp. 469-486
    • Bates, K.A.1    Verdile, G.2    Li, Q.S.3    Ames, D.4    Hudson, P.5    Masters, C.L.6    Martins, R.N.7
  • 35
    • 2542475986 scopus 로고    scopus 로고
    • Clearing amyloid through the blood-brain barrier
    • DOI 10.1111/j.1471-4159.2004.02385.x
    • B.V. Zlokovic Clearing amyloid through the blood-brain barrier J. Neurochem. 89 4 2004 807 811 (Pubitemid 38684728)
    • (2004) Journal of Neurochemistry , vol.89 , Issue.4 , pp. 807-811
    • Zlokovic, B.V.1
  • 36
    • 0026650438 scopus 로고
    • Isolation and characterisation of binding proteins for advanced glycosylation endproducts from lung tissue which are present on the endothelial cell surface
    • A.M. Schmidt, M. Vianna, M. Gerlach, J. Brett, J. Ryan, J. Kao, C. Esposito, H. Hegarty, W. Hurley, and M. Clauss Isolation and characterisation of binding proteins for advanced glycosylation endproducts from lung tissue which are present on the endothelial cell surface J. Biol. Chem. 267 1992 14987 14997
    • (1992) J. Biol. Chem. , vol.267 , pp. 14987-14997
    • Schmidt, A.M.1    Vianna, M.2    Gerlach, M.3    Brett, J.4    Ryan, J.5    Kao, J.6    Esposito, C.7    Hegarty, H.8    Hurley, W.9    Clauss, M.10
  • 38
    • 0034795140 scopus 로고    scopus 로고
    • The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
    • DOI 10.1172/JCI200114002
    • A.M. Schmidt, S.D. Yan, S.F. Yan, and D.M. Stern The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses J. Clin. Invest. 108 2001 949 955 (Pubitemid 32946067)
    • (2001) Journal of Clinical Investigation , vol.108 , Issue.7 , pp. 949-955
    • Schmidt, A.M.1    Yan, S.D.2    Yan, S.F.3    Stern, D.M.4
  • 41
    • 41549089757 scopus 로고    scopus 로고
    • Receptor for advanced glycation end product-dependent activation of p38 mitogen-activated protein kinase contributes to amyloid-β-mediated cortical synaptic dysfunction
    • DOI 10.1523/JNEUROSCI.0204-08.2008
    • N. Origlia, M. Righi, S. Capsoni, A. Cattaneo, F. Fang, D.M. Stern, J.X. Chen, A.M. Schmidt, O. Arancio, S.D. Yan, and L. Domenici Receptor for advanced glycation end product-dependent activation of p38 mitogen-activated protein kinase contributes to amyloid-b-mediated cortical synaptic dysfunction J. Neurosci. 28 2008 3521 3530 (Pubitemid 351469321)
    • (2008) Journal of Neuroscience , vol.28 , Issue.13 , pp. 3521-3530
    • Origlia, N.1    Righi, M.2    Capsoni, S.3    Cattaneo, A.4    Fang, F.5    Stern, D.M.6    Chen, J.X.7    Schmidt, A.M.8    Arancio, O.9    Shi, D.Y.10    Domenici, L.11
  • 43
    • 0026659883 scopus 로고
    • Cloning and expression of RAGE: A cell surface receptor for advanced glycosylation end products of proteins
    • M. Neeper, A.M. Schmidt, J. Brett, S.D. Yan, F. Wang, Y.C. Pan, K. Elliston, D. Stern, and A. Shaw Cloning and expression of RAGE: a cell surface receptor for advanced glycosylation end products of proteins J. Biol. Chem. 267 1992 14998 15004
    • (1992) J. Biol. Chem. , vol.267 , pp. 14998-15004
    • Neeper, M.1    Schmidt, A.M.2    Brett, J.3    Yan, S.D.4    Wang, F.5    Pan, Y.C.6    Elliston, K.7    Stern, D.8    Shaw, A.9
  • 44
    • 34250171731 scopus 로고    scopus 로고
    • The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units
    • DOI 10.1021/bi7003735
    • B.M. Dattilo, G. Fritz, E. Leclerc, C.W. Kooi, C.W. Heizmann, and W.J. Chazin The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units Biochemistry 46 2007 6957 6970 (Pubitemid 46906424)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6957-6970
    • Dattilo, B.M.1    Fritz, G.2    Leclerc, E.3    Vander Kooi, C.W.4    Heizmann, C.W.5    Chazin, W.J.6
  • 47
    • 0024708229 scopus 로고
    • Molecular genetic analysis of a plant virus polyprotein cleavage site: A model
    • W.G. Dougherty, S.M. Cary, and T.D. Parks Molecular genetic analysis of a plant virus polyprotein cleavage site: a model Virology 171 1989 356 364
    • (1989) Virology , vol.171 , pp. 356-364
    • Dougherty, W.G.1    Cary, S.M.2    Parks, T.D.3
  • 48
    • 8544230613 scopus 로고    scopus 로고
    • Alzheimer's disease Aβ peptide fragment 10-30 forms a spectrum of metastable oligomers with marked preference for N to N and C to C monomer termini proximity
    • DOI 10.1016/j.jmb.2004.09.083, PII S0022283604012392
    • A. Jabłonowska, M. Bakun, A. Kupniewska-Kozak, and M. Dadlez Alzheimer's disease Abeta peptide fragment 10-30 forms a spectrum of metastable oligomers with marked preference for N to N and C to C monomer termini proximity J. Mol. Biol. 344 2004 1037 1049 (Pubitemid 39491248)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.4 , pp. 1037-1049
    • Jablonowska, A.1    Bakun, M.2    Kupniewska-Kozak, A.3    Dadlez, M.4
  • 49
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins
    • H. Mach, C.R. Middaugh, and R.V. Lewis Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins Anal. Biochem. 200 1992 74 80
    • (1992) Anal. Biochem. , vol.200 , pp. 74-80
    • MacH, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 50
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-ligand interactions
    • M.R. Eftink Fluorescence methods for studying equilibrium macromolecule-ligand interactions Methods Enzymol. 278 1997 221 258
    • (1997) Methods Enzymol. , vol.278 , pp. 221-258
    • Eftink, M.R.1
  • 52
    • 79955635713 scopus 로고    scopus 로고
    • www.macbiophotonics.ca/ImageJ.
  • 54
    • 0019434346 scopus 로고
    • Formation of the intrachain disulfide bond in the constant fragment of the immunoglobulin light chain
    • DOI 10.1016/0022-2836(81)90391-0
    • Y. Goto, and K. Hamaguchi Formation of the intrachain disulphide bond in the constant fragment of the immunoglobulin light chain J. Mol. Biol. 146 1981 321 340 (Pubitemid 11106646)
    • (1981) Journal of Molecular Biology , vol.146 , Issue.3 , pp. 321-340
    • Goto, Y.1    Hamaguchi, K.2
  • 55
    • 0029162633 scopus 로고
    • Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1
    • C. Frech, and F.X. Schmidt Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1 J. Mol. Biol. 251 1995 135 149
    • (1995) J. Mol. Biol. , vol.251 , pp. 135-149
    • Frech, C.1    Schmidt, F.X.2
  • 56
    • 0032479326 scopus 로고    scopus 로고
    • Contribution of individual residues to formation of the native-like tertiary topology in the α-lactalbumin molten globule
    • DOI 10.1006/jmbi.1998.1826
    • J. Song, P. Bai, L. Luo, and Z. Peng Contribution of individual residues to formation of the native-like tertiary topology in the α-lactalbumin molten globule J. Mol. Biol. 280 1998 167 174 (Pubitemid 28312814)
    • (1998) Journal of Molecular Biology , vol.280 , Issue.1 , pp. 167-174
    • Song, J.1    Bai, P.2    Luo, L.3    Peng, Z.-Y.4
  • 57
    • 0030468993 scopus 로고    scopus 로고
    • Rapid formation of the native 14-38 disulfide bond in the early stages of BPTI folding
    • DOI 10.1021/bi9616054
    • M. Dadlez, and P.S. Kim Rapid formation of the native 14-38 disulfide bond in the early stages of BPTI folding Biochemistry 35 1996 16153 16164 (Pubitemid 27044077)
    • (1996) Biochemistry , vol.35 , Issue.50 , pp. 16153-16164
    • Dadlez, M.1    Kim, P.S.2
  • 58
    • 0030929829 scopus 로고    scopus 로고
    • Hydrophobic interactions accelerate early stages of the folding of BPTI
    • DOI 10.1021/bi962407f
    • M. Dadlez Hydrophobic interactions accelerate early stages of the folding of BPTI Biochemistry 36 1997 2788 2797 (Pubitemid 27138560)
    • (1997) Biochemistry , vol.36 , Issue.10 , pp. 2788-2797
    • Dadlez, M.1
  • 60
    • 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
    • F.L. Yan, Y. Zheng, and F.D. Zhao 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. 116 2008 529 535
    • (2008) Acta Neuropathol. , vol.116 , pp. 529-535
    • Yan, F.L.1    Zheng, Y.2    Zhao, F.D.3
  • 61
    • 84935851672 scopus 로고    scopus 로고
    • Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid β protein
    • K.K. Kandimalla, O.G. Scott, S. Fulzele, M.W. Davidson, and J.F. Poduslo Mechanism of neuronal versus endothelial cell uptake of Alzheimer's disease amyloid β protein PLoS ONE 4 2009 4627 4647
    • (2009) PLoS ONE , vol.4 , pp. 4627-4647
    • Kandimalla, K.K.1    Scott, O.G.2    Fulzele, S.3    Davidson, M.W.4    Poduslo, J.F.5
  • 63
    • 45549097081 scopus 로고    scopus 로고
    • Site-specific blockade of RAGE-Vd prevents amyloid-β oligomer neurotoxicity
    • E. Sturchler, A. Galichet, M. Weibel, E. Leclerc, and C.W. Heizmann Site-specific blockade of RAGE-Vd prevents amyloid-β oligomer neurotoxicity J. Neurosci. 28 2008 5149 5158
    • (2008) J. Neurosci. , vol.28 , pp. 5149-5158
    • Sturchler, E.1    Galichet, A.2    Weibel, M.3    Leclerc, E.4    Heizmann, C.W.5
  • 65
    • 0033615356 scopus 로고    scopus 로고
    • N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression
    • T. Kislinger, C. Fu, B. Huber, W. Qu, A. Taguchi, S.D. Yan, M. Hofmann, S.F. Yan, M. Pischetsrieder, D. Stern, and A.M. Schmidt N(epsilon)- (carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression J. Biol. Chem. 274 1999 31740 31749
    • (1999) J. Biol. Chem. , vol.274 , pp. 31740-31749
    • Kislinger, T.1    Fu, C.2    Huber, B.3    Qu, W.4    Taguchi, A.5    Yan, S.D.6    Hofmann, M.7    Yan, S.F.8    Pischetsrieder, M.9    Stern, D.10    Schmidt, A.M.11
  • 66
    • 35748967902 scopus 로고    scopus 로고
    • S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE (receptor for advanced glycation end products) immunoglobulin domains
    • DOI 10.1074/jbc.M703951200
    • E. Leclerc, G. Fritz, M. Weibel, C.W. Heizmann, and A. Galichet S100B and S100A6 differentially modulate cell survival by interacting with distinct RAGE immunoglobulin domains J. Biol. Chem. 282 2007 31317 31331 (Pubitemid 350044892)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31317-31331
    • Leclerc, E.1    Fritz, G.2    Weibel, M.3    Heizmann, C.W.4    Galichet, A.5
  • 67
    • 37049036195 scopus 로고    scopus 로고
    • 23-54, and an Aβ-RAGE complex in PC-12 cells
    • DOI 10.2174/156720507783018325
    • S. Mruthinti, N. Capito, A. Sood, and J.J. Buccafusc Cytotoxicity of Abeta1-42, RAGE23-54 and an Abeta-RAGE complex in PC-12 cells Curr. Alzheimer Res. 4 2007 581 586 (Pubitemid 350248397)
    • (2007) Current Alzheimer Research , vol.4 , Issue.5 , pp. 581-586
    • Mruthinti, S.1    Capito, N.2    Sood, A.3    Buccafusco, J.J.4
  • 70
    • 39649124929 scopus 로고    scopus 로고
    • Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's β-amyloid peptide
    • DOI 10.1021/bi701415b
    • B.M. Austen, K.E. Paleologou, S.A. Ali, M.M. Qureshi, D. Allsop, and O.M. El-Agnaf Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's beta-amyloid peptide Biochemistry 47 2008 1984 1992 (Pubitemid 351287124)
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 1984-1992
    • Austen, B.M.1    Paleologou, K.E.2    Ali, S.A.E.3    Qureshi, M.M.4    Allsop, D.5    El-Agnaf, O.M.A.6
  • 71
    • 34548410504 scopus 로고    scopus 로고
    • Peptide inhibitors of beta-amyloid aggregation
    • A.J. Doig Peptide inhibitors of beta-amyloid aggregation Curr. Opin. Drug. Discov. Develop. 10 2007 533 539
    • (2007) Curr. Opin. Drug. Discov. Develop. , vol.10 , pp. 533-539
    • Doig, A.J.1
  • 72
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
    • DOI 10.1523/JNEUROSCI.4391-04.2005
    • D.M. Walsh, M. Townsend, M.B. Podlisny, G.M. Shankar, J.V. Fadeeva, O. El Agnaf, D.M. Hartley, and D.J. Selkoe Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation J. Neurosci. 25 2005 2455 2462 (Pubitemid 40365155)
    • (2005) Journal of Neuroscience , vol.25 , Issue.10 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisny, M.B.3    Shankar, G.M.4    Fadeeva, J.V.5    El Agnaf, O.6    Hartley, D.M.7    Selkoe, D.J.8
  • 76
    • 0037102393 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products-binding COOH-terminal motif of amphoterin inhibits invasive migration and metastasis
    • H.J. Huttunen, C. Fages, J. Kuja-Panula, A.J. Ridley, and H. Rauvala Receptor for advanced glycation end products-binding COOH-terminal motif of amphoterin inhibits invasive migration and metastasis Cancer Res. 62 2002 4805 4811
    • (2002) Cancer Res. , vol.62 , pp. 4805-4811
    • Huttunen, H.J.1    Fages, C.2    Kuja-Panula, J.3    Ridley, A.J.4    Rauvala, H.5
  • 77
    • 0035964405 scopus 로고    scopus 로고
    • Amphoterin includes a sequence motif which is homologous to the Alzheimer's β-amyloid peptide (Aβ), forms amyloid fibrils in vitro, and binds avidly to Aβ
    • DOI 10.1021/bi002095n
    • J. Kallijarvi, M. Haltia, and M.H. Baumann Amphoterin includes a sequence motif which is homologous to the Alzheimer's beta-amyloid peptide (Abeta), forms amyloid fibrils in vitro, and binds avidly to Abeta Biochemistry 40 2001 10032 10037 (Pubitemid 32800110)
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10032-10037
    • Kallijarvi, J.1    Haltia, M.2    Baumann, M.H.3
  • 78
    • 0030248270 scopus 로고    scopus 로고
    • Microglial cells internalize aggregates of the Alzheimer's disease amyloid β-protein via a scavenger receptor
    • DOI 10.1016/S0896-6273(00)80187-7
    • D.M. Paresce, R.N. Ghosh, and F.R. Maxfield Microglial cells internalise aggregates of the Alzheimer's disease amyloid beta-protein via a scavenger receptor Neuron 17 1996 553 565 (Pubitemid 26322226)
    • (1996) Neuron , vol.17 , Issue.3 , pp. 553-565
    • Paresce, D.M.1    Ghosh, R.N.2    Maxfield, F.R.3
  • 82
    • 34247506244 scopus 로고    scopus 로고
    • Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins E and J in the mouse central nervous system
    • DOI 10.1038/sj.jcbfm.9600419, PII 9600419
    • R.D. Bell, A.P. Sagare, A.E. Friedman, G.S. Bedi, D.M. Holtzman, R. Deane, and B.V. Zlokovic Transport pathways for clearance of human Alzheimer's amyloid beta-peptide and apolipoproteins E and J in the mouse central nervous system J. Cereb. Blood Flow Metab. 27 2007 909 918 (Pubitemid 46659038)
    • (2007) Journal of Cerebral Blood Flow and Metabolism , vol.27 , Issue.5 , pp. 909-918
    • Bell, R.D.1    Sagare, A.P.2    Friedman, A.E.3    Bedi, G.S.4    Holtzman, D.M.5    Deane, R.6    Zlokovic, B.V.7
  • 85
    • 7644225312 scopus 로고    scopus 로고
    • RAGE (Yin) versus LRP (Yang) balance regulates Alzheimer amyloid β-peptide clearance through transport across the blood-brain barrier
    • DOI 10.1161/01.STR.0000143452.85382.d1
    • R. Deane, Z. Wu, and B.V. Zlokovic RAGE (Yin) versus LRP (Yang) balance regulates Alzheimer amyloid-beta peptide clearance through transport across the blood-brain barrier Stroke 35 suppl. I 2004 2628 2631 (Pubitemid 39458354)
    • (2004) Stroke , vol.35 , Issue.11 SUPPL. 1 , pp. 2628-2631
    • Deane, R.1    Wu, Z.2    Zlokovic, B.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.