메뉴 건너뛰기




Volumn 22, Issue 7, 2008, Pages 2115-2133

Molecular and cellular aspects of protein misfolding and disease

Author keywords

Aggregation; Alzheimer's disease; Amyloid; Atherosclerosis; Protein structure; Therapy

Indexed keywords

AL 108; AMYLIN ANTIBODY; AMYLOID BETA PROTEIN[25-35]; AMYLOID PRECURSOR PROTEIN; ANTIDIABETIC AGENT; ATG Z1; AZD 103; BAPINEUZUMAB; BI 204; CAD 106; CARDIOVASCULAR AGENT; HOMOTAURINE; INSULIN; N2 [2 (3,5 DIFLUOROPHENYL) 2 HYDROXYACETYL] N1 (6,7 DIHYDRO 5 METHYL 6 OXO 5H DIBENZ[B,D]AZEPIN 7 YL)ALANINAMIDE; NEUROPROTECTIVE AGENT; NOX A42; PAZ 417; PF 4494700; PRION PROTEIN; PROTEIN ANTIBODY; SERUM AMYLOID A; TAU PROTEIN; TTP 4000;

EID: 46749117136     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-099671     Document Type: Review
Times cited : (170)

References (281)
  • 1
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D., and Wolynes, P. G. (1995) Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21, 167-195
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 2
    • 28244437028 scopus 로고    scopus 로고
    • The yin and yang of protein folding
    • Jahn, T. R., and Radford, S. E. (2005) The yin and yang of protein folding. FEBS J. 272, 5962-5970
    • (2005) FEBS J , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 3
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold, P. E., Montal, M., and Onuchic, J. N. (1992) Protein folding funnels: a kinetic approach to the sequence-structure relationship. Proc. Natl. Acad. Sci. U. S. A. 89, 8721-8725
    • (1992) Proc. Natl. Acad. Sci. U. S. A , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 4
    • 0030733858 scopus 로고    scopus 로고
    • Local interactions and the optimization of protein folding
    • Doyle, R., Simons, K., Qian, H., and Baker, D. (1997) Local interactions and the optimization of protein folding. Proteins 29, 282-291
    • (1997) Proteins , vol.29 , pp. 282-291
    • Doyle, R.1    Simons, K.2    Qian, H.3    Baker, D.4
  • 7
    • 4143133235 scopus 로고    scopus 로고
    • A comparative study of the relationship between protein structure and β-aggregation in globular and intrinsically disordered proteins
    • Linding, R., Schymkowitz, J., Rousseau, F., Diella, F., and Serrano, L. (2004) A comparative study of the relationship between protein structure and β-aggregation in globular and intrinsically disordered proteins. J. Mol. Biol. 342, 345-353
    • (2004) J. Mol. Biol , vol.342 , pp. 345-353
    • Linding, R.1    Schymkowitz, J.2    Rousseau, F.3    Diella, F.4    Serrano, L.5
  • 8
    • 0034886526 scopus 로고    scopus 로고
    • Proteolysis of AA amyloid fibril proteins by matrix metalloproteinases-1, -2, and -3
    • Stix, B., Kahne, T., Sletten, K., Raynes, J., Roessner, A., and Rocken, C. (2001) Proteolysis of AA amyloid fibril proteins by matrix metalloproteinases-1, -2, and -3. Am. J. Pathol. 159, 561-570
    • (2001) Am. J. Pathol , vol.159 , pp. 561-570
    • Stix, B.1    Kahne, T.2    Sletten, K.3    Raynes, J.4    Roessner, A.5    Rocken, C.6
  • 9
    • 0030728039 scopus 로고    scopus 로고
    • Deadly conformations - protein misfolding in prion disease
    • Horwich, A. L., and Weissman, J. S. (1997) Deadly conformations - protein misfolding in prion disease. Cell 89, 499-510
    • (1997) Cell , vol.89 , pp. 499-510
    • Horwich, A.L.1    Weissman, J.S.2
  • 10
    • 33749825259 scopus 로고    scopus 로고
    • Conformational change and assembly through edge β strands in transthyretin and other amyloid proteins
    • Laidman, J., Forse, G. J., and Yeates, T. O. (2006) Conformational change and assembly through edge β strands in transthyretin and other amyloid proteins. Acc. Chem. Res. 39, 576-583
    • (2006) Acc. Chem. Res , vol.39 , pp. 576-583
    • Laidman, J.1    Forse, G.J.2    Yeates, T.O.3
  • 11
    • 0346786219 scopus 로고    scopus 로고
    • The systemic amyloidoses
    • Buxbaum, J. N. (2004) The systemic amyloidoses. Curr. Opin. Rheumatol. 16, 67-75
    • (2004) Curr. Opin. Rheumatol , vol.16 , pp. 67-75
    • Buxbaum, J.N.1
  • 12
    • 32344448608 scopus 로고    scopus 로고
    • Protein aggregation and amyloidosis: Confusion of the kinds?
    • Rousseau, F., Schymkowitz, J., and Serrano, L. (2006) Protein aggregation and amyloidosis: confusion of the kinds? Curr. Opin. Struct. Biol. 16, 118-126
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 118-126
    • Rousseau, F.1    Schymkowitz, J.2    Serrano, L.3
  • 13
    • 0034680781 scopus 로고    scopus 로고
    • Alternate aggregation pathways of the Alzheimer β-amyloid peptide: An in vitro model of preamyloid
    • Huang, T. H., Yang, D. S., Fraser, P. E., and Chakrabartty, A. (2000) Alternate aggregation pathways of the Alzheimer β-amyloid peptide: an in vitro model of preamyloid. J. Biol. Chem. 275, 36436-36440
    • (2000) J. Biol. Chem , vol.275 , pp. 36436-36440
    • Huang, T.H.1    Yang, D.S.2    Fraser, P.E.3    Chakrabartty, A.4
  • 14
    • 33749824175 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of amyloid fibril assembly
    • Wetzel, R. (2006) Kinetics and thermodynamics of amyloid fibril assembly. Acc. Chem. Res. 39, 671-679
    • (2006) Acc. Chem. Res , vol.39 , pp. 671-679
    • Wetzel, R.1
  • 15
    • 0015918914 scopus 로고
    • X-ray diffraction and infrared studies of an α-helical fragment from α-keratin
    • Suzuki, E., Crewther, W. G., Fraser, R. D., MacRae, T. P., and McKern, N. M. (1973) X-ray diffraction and infrared studies of an α-helical fragment from α-keratin. J. Mol. Biol. 73, 275-278
    • (1973) J. Mol. Biol , vol.73 , pp. 275-278
    • Suzuki, E.1    Crewther, W.G.2    Fraser, R.D.3    MacRae, T.P.4    McKern, N.M.5
  • 16
    • 34347240979 scopus 로고    scopus 로고
    • Quantification of cerebral amyloid angiopathy and parenchymal amyloid plaques with Congo red histochemical stain
    • Wilcock, D. M., Gordon, M. N., and Morgan, D. (2006) Quantification of cerebral amyloid angiopathy and parenchymal amyloid plaques with Congo red histochemical stain. Nat. Protoc. 1, 1591-1595
    • (2006) Nat. Protoc , vol.1 , pp. 1591-1595
    • Wilcock, D.M.1    Gordon, M.N.2    Morgan, D.3
  • 17
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H., III (1993) Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404-410
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 18
    • 33748688511 scopus 로고    scopus 로고
    • Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins
    • Meredith, S. C. (2005) Protein denaturation and aggregation: cellular responses to denatured and aggregated proteins. Ann. N. Y. Acad. Sci. 1066, 181-221
    • (2005) Ann. N. Y. Acad. Sci , vol.1066 , pp. 181-221
    • Meredith, S.C.1
  • 19
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation and the structure of the seed globulins
    • Astbury, W. T., and Dickinson, S. (1935) The X-ray interpretation of denaturation and the structure of the seed globulins. Biochem. J. 29, 2351-2360
    • (1935) Biochem. J , vol.29 , pp. 2351-2360
    • Astbury, W.T.1    Dickinson, S.2
  • 20
    • 0037818986 scopus 로고
    • The proteins of the mammalian epidermis
    • Rudall, K. M. (1952) The proteins of the mammalian epidermis. Adv. Protein Chem. 7, 253-290
    • (1952) Adv. Protein Chem , vol.7 , pp. 253-290
    • Rudall, K.M.1
  • 21
    • 0035543109 scopus 로고    scopus 로고
    • The architecture of parallel βa-helices and related folds
    • Jenkins, J., and Pickersgill, R. (2001) The architecture of parallel βa-helices and related folds. Prog. Biophys. Mol. Biol. 77, 111-175
    • (2001) Prog. Biophys. Mol. Biol , vol.77 , pp. 111-175
    • Jenkins, J.1    Pickersgill, R.2
  • 22
    • 23244449092 scopus 로고    scopus 로고
    • Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p
    • Chan, J. C., Oyler, N. A., Yau, W. M., and Tycko, R. (2005) Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. Biochemistry 44, 10669-10680
    • (2005) Biochemistry , vol.44 , pp. 10669-10680
    • Chan, J.C.1    Oyler, N.A.2    Yau, W.M.3    Tycko, R.4
  • 24
    • 0031593854 scopus 로고    scopus 로고
    • Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease
    • Chaney, M. O., Webster, S. D., Kuo, Y. M., and Roher, A. E. (1998) Molecular modeling of the Aβ1-42 peptide from Alzheimer's disease. Protein Eng. 11, 761-767
    • (1998) Protein Eng , vol.11 , pp. 761-767
    • Chaney, M.O.1    Webster, S.D.2    Kuo, Y.M.3    Roher, A.E.4
  • 28
    • 0038204547 scopus 로고
    • Dutch, Flemish, Italian, and Arctic mutations of APP and resistance of Aβ to physiologically relevant proteolytic degradation
    • 2003
    • Tsubuki, S., Takaki, Y., and Saido, T. C. (2003) Dutch, Flemish, Italian, and Arctic mutations of APP and resistance of Aβ to physiologically relevant proteolytic degradation. Lancet 361, 1957-1958
    • (1957) Lancet , vol.361
    • Tsubuki, S.1    Takaki, Y.2    Saido, T.C.3
  • 29
    • 0036037356 scopus 로고    scopus 로고
    • Unfolding and aggregation during the thermal denaturation of streptokinase
    • Azuaga, A. I., Dobson, C. M., Mateo, P. L., and Conejero-Lara, F. (2002) Unfolding and aggregation during the thermal denaturation of streptokinase. Eur. J. Biochem. 269, 4121-4133
    • (2002) Eur. J. Biochem , vol.269 , pp. 4121-4133
    • Azuaga, A.I.1    Dobson, C.M.2    Mateo, P.L.3    Conejero-Lara, F.4
  • 30
    • 0029924648 scopus 로고    scopus 로고
    • Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
    • Iametti, S., De, G. B., Vecchio, G., and Bonomi, F. (1996) Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. Eur. J. Biochem. 237, 106-112
    • (1996) Eur. J. Biochem , vol.237 , pp. 106-112
    • Iametti, S.1    De, G.B.2    Vecchio, G.3    Bonomi, F.4
  • 31
    • 33845982898 scopus 로고    scopus 로고
    • pH-dependent self-assembly of polyalanine peptides
    • Giri, K., Bhattacharyya, N. P., and Basak, S. (2007) pH-dependent self-assembly of polyalanine peptides. Biophys. J. 92, 293-302
    • (2007) Biophys. J , vol.92 , pp. 293-302
    • Giri, K.1    Bhattacharyya, N.P.2    Basak, S.3
  • 33
    • 34247330236 scopus 로고    scopus 로고
    • Effects of pH and polyanions on the thermal stability of fibroblast growth factor 20
    • Fan, H., Vitharana, S. N., Chen, T., O'Keefe, D., and Middaugh, C. R. (2007) Effects of pH and polyanions on the thermal stability of fibroblast growth factor 20. Mol. Pharmacol. 4, 232-240
    • (2007) Mol. Pharmacol , vol.4 , pp. 232-240
    • Fan, H.1    Vitharana, S.N.2    Chen, T.3    O'Keefe, D.4    Middaugh, C.R.5
  • 34
    • 0035808359 scopus 로고    scopus 로고
    • Low pH-induced conformational changes in vesicular stomatitis virus glycoprotein involve dramatic structure reorganization
    • Carneiro, F. A., Ferradosa, A. S., and Da Poian, A. T. (2001) Low pH-induced conformational changes in vesicular stomatitis virus glycoprotein involve dramatic structure reorganization. J. Biol. Chem. 276, 62-67
    • (2001) J. Biol. Chem , vol.276 , pp. 62-67
    • Carneiro, F.A.1    Ferradosa, A.S.2    Da Poian, A.T.3
  • 35
    • 9444299029 scopus 로고    scopus 로고
    • Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure
    • De Felice, F. G., Vieira, M. N., Meirelles, M. N., Morozova-Roche, L. A., Dobson, C. M., and Ferreira, S. T. (2004) Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure. FASEB J. 18, 1099-1101
    • (2004) FASEB J , vol.18 , pp. 1099-1101
    • De Felice, F.G.1    Vieira, M.N.2    Meirelles, M.N.3    Morozova-Roche, L.A.4    Dobson, C.M.5    Ferreira, S.T.6
  • 36
    • 1842557395 scopus 로고    scopus 로고
    • High pressure promotes circularly shaped insulin amyloid
    • Jansen, R., Grudzielanek, S., Dzwolak, W., and Winter, R. (2004) High pressure promotes circularly shaped insulin amyloid. J. Mol. Biol. 338, 203-206
    • (2004) J. Mol. Biol , vol.338 , pp. 203-206
    • Jansen, R.1    Grudzielanek, S.2    Dzwolak, W.3    Winter, R.4
  • 38
    • 0027327488 scopus 로고
    • Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide
    • Mantyh, P. W., Ghilardi, J. R., Rogers, S., DeMaster, E., Allen, C. J., Stimson, E. R., and Maggio, J. E. (1993) Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide. J. Neurochem. 61, 1171-1174
    • (1993) J. Neurochem , vol.61 , pp. 1171-1174
    • Mantyh, P.W.1    Ghilardi, J.R.2    Rogers, S.3    DeMaster, E.4    Allen, C.J.5    Stimson, E.R.6    Maggio, J.E.7
  • 39
    • 33749008521 scopus 로고    scopus 로고
    • Effect of ionic strength on folding and aggregation of the hemolytic peptide melittin in solution
    • Raghuraman, H., and Chattopadhyay, A. (2006) Effect of ionic strength on folding and aggregation of the hemolytic peptide melittin in solution. Biopolymers 83, 111-121
    • (2006) Biopolymers , vol.83 , pp. 111-121
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 40
    • 25444512708 scopus 로고    scopus 로고
    • Ultrasonication-induced amyloid fibril formation of β2-microglobulin
    • Ohhashi, Y., Kihara, M., Naiki, H., and Goto, Y. (2005) Ultrasonication-induced amyloid fibril formation of β2-microglobulin. J. Biol. Chem. 280, 32843-32848
    • (2005) J. Biol. Chem , vol.280 , pp. 32843-32848
    • Ohhashi, Y.1    Kihara, M.2    Naiki, H.3    Goto, Y.4
  • 41
    • 33748450346 scopus 로고    scopus 로고
    • Amyloid fibrils of glucagon characterized by high-resolution atomic force microscopy
    • De Jong, K. L., Incledon, B., Yip, C. M., and DeFelippis, M. R. (2006) Amyloid fibrils of glucagon characterized by high-resolution atomic force microscopy. Biophys. J. 91, 1905-1914
    • (2006) Biophys. J , vol.91 , pp. 1905-1914
    • De Jong, K.L.1    Incledon, B.2    Yip, C.M.3    DeFelippis, M.R.4
  • 43
    • 0032796425 scopus 로고    scopus 로고
    • Amyloid-β-sheet formation at the air-water interface
    • Schladitz, C., Vieira, E. P., Hermel, H., and Mohwald, H. (1999) Amyloid-β-sheet formation at the air-water interface. Biophys. J. 77, 3305-3310
    • (1999) Biophys. J , vol.77 , pp. 3305-3310
    • Schladitz, C.1    Vieira, E.P.2    Hermel, H.3    Mohwald, H.4
  • 45
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao, H., Tuominen, E. K., and Kinnunen, P. K. (2004) Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 43, 10302-10307
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.2    Kinnunen, P.K.3
  • 46
    • 14344250143 scopus 로고    scopus 로고
    • Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers
    • Zhao, H., Jutila, A., Nurminen, T., Wickstrom, S. A., Keski-Oja, J., and Kinnunen, P. K. (2005) Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers. Biochemistry 44, 2857-2863
    • (2005) Biochemistry , vol.44 , pp. 2857-2863
    • Zhao, H.1    Jutila, A.2    Nurminen, T.3    Wickstrom, S.A.4    Keski-Oja, J.5    Kinnunen, P.K.6
  • 47
    • 32144460539 scopus 로고    scopus 로고
    • ε-Glycation, APP and Aβ in ageing and Alzheimer disease: A hypothesis
    • Schmitt, H. P. (2006) ε-Glycation, APP and Aβ in ageing and Alzheimer disease: a hypothesis. Med. Hypotheses 66, 898-906
    • (2006) Med. Hypotheses , vol.66 , pp. 898-906
    • Schmitt, H.P.1
  • 52
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • Merlini, G., and Bellotti, V. (2003) Molecular mechanisms of amyloidosis. N. Engl. J. Med. 349, 583-596
    • (2003) N. Engl. J. Med , vol.349 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 54
    • 33845940990 scopus 로고    scopus 로고
    • Therapy and management of systemic AL (primary) amyloidosis
    • Palladini, G., Perfetti, V., and Merlini, G. (2006) Therapy and management of systemic AL (primary) amyloidosis. Swiss Med. Wkly. 136, 715-720
    • (2006) Swiss Med. Wkly , vol.136 , pp. 715-720
    • Palladini, G.1    Perfetti, V.2    Merlini, G.3
  • 55
    • 1042288322 scopus 로고    scopus 로고
    • Therapy for immunoglobulin light chain amyloidosis: The new and the old
    • Gertz, M. A., Lacy, M. Q., and Dispenzieri, A. (2004) Therapy for immunoglobulin light chain amyloidosis: the new and the old. Blood Rev. 18, 17-37
    • (2004) Blood Rev , vol.18 , pp. 17-37
    • Gertz, M.A.1    Lacy, M.Q.2    Dispenzieri, A.3
  • 56
    • 0028036274 scopus 로고
    • Expression, purification and characterization of a Kunitz-type protease inhibitor domain from human amyloid precursor protein homolog
    • Petersen, L. C., Bjorn, S. E., Norris, F., Norris, K., Sprecher, C., and Foster, D. C. (1994) Expression, purification and characterization of a Kunitz-type protease inhibitor domain from human amyloid precursor protein homolog. FEBS Lett. 338, 53-57
    • (1994) FEBS Lett , vol.338 , pp. 53-57
    • Petersen, L.C.1    Bjorn, S.E.2    Norris, F.3    Norris, K.4    Sprecher, C.5    Foster, D.C.6
  • 57
    • 2542519087 scopus 로고    scopus 로고
    • Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone
    • Caille, I., Allinquant, B., Dupont, E., Bouillot, C., Langer, A., Muller, U., and Prochiantz, A. (2004) Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone. Development 131, 2173-2181
    • (2004) Development , vol.131 , pp. 2173-2181
    • Caille, I.1    Allinquant, B.2    Dupont, E.3    Bouillot, C.4    Langer, A.5    Muller, U.6    Prochiantz, A.7
  • 58
    • 0036191784 scopus 로고    scopus 로고
    • The biological role of the Alzheimer amyloid precursor protein in epithelial cells
    • Schmitz, A., Tikkanen, R., Kirfel, G., and Herzog, V. (2002) The biological role of the Alzheimer amyloid precursor protein in epithelial cells. Histochem. Cell. Biol. 117, 171-180
    • (2002) Histochem. Cell. Biol , vol.117 , pp. 171-180
    • Schmitz, A.1    Tikkanen, R.2    Kirfel, G.3    Herzog, V.4
  • 59
    • 0036949283 scopus 로고    scopus 로고
    • The secretory β-amyloid precursor protein is a mitogen for human epidermal keratinocytes
    • Kirfel, G., Borm, B., Rigort, A., and Herzog, V. (2002) The secretory β-amyloid precursor protein is a mitogen for human epidermal keratinocytes. Eur. J. Cell. Biol. 81, 664-676
    • (2002) Eur. J. Cell. Biol , vol.81 , pp. 664-676
    • Kirfel, G.1    Borm, B.2    Rigort, A.3    Herzog, V.4
  • 61
    • 0025899041 scopus 로고
    • Amyloid deposition as the central event in the aetiology of Alzheimer's disease
    • Hardy, J., and Allsop, D. (1991) Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol. Sci. 12, 383-388
    • (1991) Trends Pharmacol. Sci , vol.12 , pp. 383-388
    • Hardy, J.1    Allsop, D.2
  • 62
    • 33846101613 scopus 로고    scopus 로고
    • Filling the gaps in the aβ cascade hypothesis of Alzheimer's disease
    • Golde, T. E., Dickson, D., and Hutton, M. (2006) Filling the gaps in the aβ cascade hypothesis of Alzheimer's disease. Curr. Alzheimer Res. 3, 421-430
    • (2006) Curr. Alzheimer Res , vol.3 , pp. 421-430
    • Golde, T.E.1    Dickson, D.2    Hutton, M.3
  • 63
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T. A. (1994) Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76, 301-314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 64
    • 84910078370 scopus 로고    scopus 로고
    • Risk factors for atherosclerosis in young individuals
    • Misra, A. (2000) Risk factors for atherosclerosis in young individuals. J. Cardiovasc. Risk 7, 215-229
    • (2000) J. Cardiovasc. Risk , vol.7 , pp. 215-229
    • Misra, A.1
  • 65
    • 1642399003 scopus 로고    scopus 로고
    • Genetic risk factors for stroke and carotid atherosclerosis: Insights into pathophysiology from candidate gene approaches
    • Humphries, S. E., and Morgan, L. (2004) Genetic risk factors for stroke and carotid atherosclerosis: insights into pathophysiology from candidate gene approaches. Lancet Neurol. 3, 227-235
    • (2004) Lancet Neurol , vol.3 , pp. 227-235
    • Humphries, S.E.1    Morgan, L.2
  • 67
    • 33748519935 scopus 로고    scopus 로고
    • Untangling the role of amyloid in atherosclerosis
    • Howlett, G. J., and Moore, K. J. (2006) Untangling the role of amyloid in atherosclerosis. Curr. Opin. Lipidol. 17, 541-547
    • (2006) Curr. Opin. Lipidol , vol.17 , pp. 541-547
    • Howlett, G.J.1    Moore, K.J.2
  • 68
    • 33644543347 scopus 로고    scopus 로고
    • Impact of oxidized low density lipoprotein on vascular cells
    • Galle, J., Hansen-Hagge, T., Wanner, C., and Seibold, S. (2006) Impact of oxidized low density lipoprotein on vascular cells. Atherosclerosis 185, 219-226
    • (2006) Atherosclerosis , vol.185 , pp. 219-226
    • Galle, J.1    Hansen-Hagge, T.2    Wanner, C.3    Seibold, S.4
  • 69
    • 34248184152 scopus 로고    scopus 로고
    • Therapeutical potential of direct thrombin inhibitors for atherosclerotic vascular disease
    • Husmann, M., and Barton, M. (2007) Therapeutical potential of direct thrombin inhibitors for atherosclerotic vascular disease. Expert Opin. Investig. Drugs 16, 563-567
    • (2007) Expert Opin. Investig. Drugs , vol.16 , pp. 563-567
    • Husmann, M.1    Barton, M.2
  • 70
    • 33846008765 scopus 로고    scopus 로고
    • Endothelial dysfunction, oxidative stress and inflammation in atherosclerosis: Beneficial effects of statins
    • Lahera, V., Goicoechea, M., de Vinuesa, S. G., Miana, M., de las Heras, N., Cachofeiro, V., and Luno, J. (2007) Endothelial dysfunction, oxidative stress and inflammation in atherosclerosis: beneficial effects of statins. Curr. Med. Chem. 14, 243-248
    • (2007) Curr. Med. Chem , vol.14 , pp. 243-248
    • Lahera, V.1    Goicoechea, M.2    de Vinuesa, S.G.3    Miana, M.4    de las Heras, N.5    Cachofeiro, V.6    Luno, J.7
  • 74
    • 0024559479 scopus 로고
    • Physiological functions of platelets
    • Holmsen, H. (1989) Physiological functions of platelets. Ann. Med. 21, 23-30
    • (1989) Ann. Med , vol.21 , pp. 23-30
    • Holmsen, H.1
  • 75
    • 0018323116 scopus 로고
    • The contractile system of blood platelets and its function
    • Cohen, I. (1979) The contractile system of blood platelets and its function. Methods Achiev. Exp. Pathol. 9, 40-86
    • (1979) Methods Achiev. Exp. Pathol , vol.9 , pp. 40-86
    • Cohen, I.1
  • 76
    • 25444437966 scopus 로고    scopus 로고
    • Platelets: Physiology and biochemistry
    • Jurk, K., and Kehrel, B. E. (2005) Platelets: physiology and biochemistry. Semin. Thromb. Hemost. 31, 381-392
    • (2005) Semin. Thromb. Hemost , vol.31 , pp. 381-392
    • Jurk, K.1    Kehrel, B.E.2
  • 79
    • 0028558473 scopus 로고
    • β-Amyloid protein induces platelet aggregation and supports platelet adhesion
    • Kowalska, M. A., and Badellino, K. (1994) β-Amyloid protein induces platelet aggregation and supports platelet adhesion. Biochem. Biophys. Res. Commun. 205, 1829-1835
    • (1994) Biochem. Biophys. Res. Commun , vol.205 , pp. 1829-1835
    • Kowalska, M.A.1    Badellino, K.2
  • 84
    • 0035907290 scopus 로고    scopus 로고
    • Skovronsky, D. M., Lee, V. M., and Pratico, D. (2001) Amyloid precursor protein and amyloid β peptide in human platelets: role of cyclooxygenase and protein kinase C. J. Biol. Chem. 276, 17036-17043
    • Skovronsky, D. M., Lee, V. M., and Pratico, D. (2001) Amyloid precursor protein and amyloid β peptide in human platelets: role of cyclooxygenase and protein kinase C. J. Biol. Chem. 276, 17036-17043
  • 86
    • 30044435708 scopus 로고    scopus 로고
    • Clinically apparent atherosclerotic disease in diabetes is associated with an increase in platelet microparticle levels
    • Tan, K. T., Tayebjee, M. H., Lim, H. S., and Lip, G. Y. (2005) Clinically apparent atherosclerotic disease in diabetes is associated with an increase in platelet microparticle levels. Diabet. Med. 22, 1657-1662
    • (2005) Diabet. Med , vol.22 , pp. 1657-1662
    • Tan, K.T.1    Tayebjee, M.H.2    Lim, H.S.3    Lip, G.Y.4
  • 87
    • 33645024970 scopus 로고    scopus 로고
    • Elevated levels of remnant lipoproteins are associated with plasma platelet microparticles in patients with type-2 diabetes mellitus without obstructive coronary artery disease
    • Koga, H., Sugiyama, S., Kugiyama, K., Fukushima, H., Watanabe, K., Sakamoto, T., Yoshimura, M., Jinnouchi, H., and Ogawa, H. (2006) Elevated levels of remnant lipoproteins are associated with plasma platelet microparticles in patients with type-2 diabetes mellitus without obstructive coronary artery disease. Eur. Heart J. 27, 817-823
    • (2006) Eur. Heart J , vol.27 , pp. 817-823
    • Koga, H.1    Sugiyama, S.2    Kugiyama, K.3    Fukushima, H.4    Watanabe, K.5    Sakamoto, T.6    Yoshimura, M.7    Jinnouchi, H.8    Ogawa, H.9
  • 89
    • 0033803763 scopus 로고    scopus 로고
    • β Amyloid fragments derived from activated platelets deposit in cerebrovascular endothelium: Usage of a novel blood brain barrier endothelial cell model system
    • Davies, T. A., Long, H. J., Eisenhauer, P. B., Hastey, R., Cribbs, D. H., Fine, R. E., and Simons, E. R. (2000) β Amyloid fragments derived from activated platelets deposit in cerebrovascular endothelium: usage of a novel blood brain barrier endothelial cell model system. Amyloid 7, 153-165
    • (2000) Amyloid , vol.7 , pp. 153-165
    • Davies, T.A.1    Long, H.J.2    Eisenhauer, P.B.3    Hastey, R.4    Cribbs, D.H.5    Fine, R.E.6    Simons, E.R.7
  • 90
    • 33749015483 scopus 로고    scopus 로고
    • Update on hypertension and Alzheimer's disease
    • Skoog, I., and Gustafson, D. (2006) Update on hypertension and Alzheimer's disease. Neurol. Res. 28, 605-611
    • (2006) Neurol. Res , vol.28 , pp. 605-611
    • Skoog, I.1    Gustafson, D.2
  • 91
    • 0029554287 scopus 로고
    • The role of free radicals in toxicity and disease
    • Stohs, S. J. (1995) The role of free radicals in toxicity and disease. J. Basic Clin. Physiol. Pharmacol. 6, 205-228
    • (1995) J. Basic Clin. Physiol. Pharmacol , vol.6 , pp. 205-228
    • Stohs, S.J.1
  • 92
    • 0029869755 scopus 로고    scopus 로고
    • Glucose regulation and cognitive functions: Relation to Alzheimer's disease and diabetes
    • Messier, C., and Gagnon, M. (1996) Glucose regulation and cognitive functions: relation to Alzheimer's disease and diabetes. Behav. Brain Res. 75, 1-11
    • (1996) Behav. Brain Res , vol.75 , pp. 1-11
    • Messier, C.1    Gagnon, M.2
  • 93
    • 11244284810 scopus 로고    scopus 로고
    • Glucose, glycation and aging
    • Suji, G., and Sivakami, S. (2004) Glucose, glycation and aging. Biogerontology 5, 365-373
    • (2004) Biogerontology , vol.5 , pp. 365-373
    • Suji, G.1    Sivakami, S.2
  • 94
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier, T. C. (2001) Oxidative stress and protein aggregation during biological aging. Exp. Gerontol. 36, 1539-1550
    • (2001) Exp. Gerontol , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 95
    • 0031026879 scopus 로고    scopus 로고
    • Atherosclerosis, apolipoprotein E, and prevalence of dementia and Alzheimer's disease in the Rotterdam Study
    • Hofman, A., Ott, A., Breteler, M. M., Bots, M. L., Slooter, A. J., van, H. F., van Duijn, C. N., Van, B. C., and Grobbee, D. E. (1997) Atherosclerosis, apolipoprotein E, and prevalence of dementia and Alzheimer's disease in the Rotterdam Study. Lancet 349, 151-154
    • (1997) Lancet , vol.349 , pp. 151-154
    • Hofman, A.1    Ott, A.2    Breteler, M.M.3    Bots, M.L.4    Slooter, A.J.5    van, H.F.6    van Duijn, C.N.7    Van, B.C.8    Grobbee, D.E.9
  • 96
    • 1842528400 scopus 로고    scopus 로고
    • Convergence of atherosclerosis and Alzheimer's disease: Inflammation, cholesterol, and misfolded proteins
    • Casserly, I., and Topol, E. (2004) Convergence of atherosclerosis and Alzheimer's disease: inflammation, cholesterol, and misfolded proteins. Lancet 363, 1139-1146
    • (2004) Lancet , vol.363 , pp. 1139-1146
    • Casserly, I.1    Topol, E.2
  • 97
    • 2442424380 scopus 로고    scopus 로고
    • Diabetes mellitus and risk of Alzheimer disease and decline in cognitive function
    • Arvanitakis, Z., Wilson, R. S., Bienias, J. L., Evans, D. A., and Bennett, D. A. (2004) Diabetes mellitus and risk of Alzheimer disease and decline in cognitive function. Arch. Neurol. 61, 661-666
    • (2004) Arch. Neurol , vol.61 , pp. 661-666
    • Arvanitakis, Z.1    Wilson, R.S.2    Bienias, J.L.3    Evans, D.A.4    Bennett, D.A.5
  • 101
    • 0034746287 scopus 로고    scopus 로고
    • Pathogenesis of β2-microglobulin amyloidosis
    • Ohashi, K. (2001) Pathogenesis of β2-microglobulin amyloidosis. Pathol. Int. 51, 1-10
    • (2001) Pathol. Int , vol.51 , pp. 1-10
    • Ohashi, K.1
  • 103
    • 0038466351 scopus 로고    scopus 로고
    • Hereditary systemic amyloidosis with renal involvement
    • Hawkins, P. N. (2003) Hereditary systemic amyloidosis with renal involvement. J. Nephrol. 16, 443-448
    • (2003) J. Nephrol , vol.16 , pp. 443-448
    • Hawkins, P.N.1
  • 105
    • 0032012657 scopus 로고    scopus 로고
    • Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide
    • Kiuru, S. (1998) Gelsolin-related familial amyloidosis, Finnish type (FAF), and its variants found worldwide. Amyloid 5, 55-66
    • (1998) Amyloid , vol.5 , pp. 55-66
    • Kiuru, S.1
  • 107
    • 33646586054 scopus 로고    scopus 로고
    • Hereditary cystatin C amyloid angiopathy: Genetic, clinical, and pathological aspects
    • Palsdottir, A., Snorradottir, A. O., and Thorsteinsson, L. (2006) Hereditary cystatin C amyloid angiopathy: genetic, clinical, and pathological aspects. Brain Pathol. 16, 55-59
    • (2006) Brain Pathol , vol.16 , pp. 55-59
    • Palsdottir, A.1    Snorradottir, A.O.2    Thorsteinsson, L.3
  • 108
    • 0036400208 scopus 로고    scopus 로고
    • Examination of insulin injection sites: An unexpected finding of localized amyloidosis
    • Swift, B. (2002) Examination of insulin injection sites: an unexpected finding of localized amyloidosis. Diabet. Med. 19, 881-882
    • (2002) Diabet. Med , vol.19 , pp. 881-882
    • Swift, B.1
  • 110
    • 0027405851 scopus 로고
    • Seminal vesicle amyloidosis: Morphological, histochemical and immunohistochemical observations
    • Coyne, J. D., and Kealy, W. F. (1993) Seminal vesicle amyloidosis: morphological, histochemical and immunohistochemical observations. Histopathology 22, 173-176
    • (1993) Histopathology , vol.22 , pp. 173-176
    • Coyne, J.D.1    Kealy, W.F.2
  • 113
    • 0942276377 scopus 로고    scopus 로고
    • Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation
    • Meehan, S., Berry, Y., Luisi, B., Dobson, C. M., Carver, J. A., and MacPhee, C. E. (2004) Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation. J. Biol. Chem. 279, 3413-3419
    • (2004) J. Biol. Chem , vol.279 , pp. 3413-3419
    • Meehan, S.1    Berry, Y.2    Luisi, B.3    Dobson, C.M.4    Carver, J.A.5    MacPhee, C.E.6
  • 115
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner, G. G., and Wong, C. W. (1984) Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122, 1131-1135
    • (1984) Biochem. Biophys. Res. Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 116
    • 0030931864 scopus 로고    scopus 로고
    • Alzheimer disease hyperphosphorylated tau aggregates hydrophobically
    • Ruben, G. C., Ciardelli, T. L., Grundke-Iqbal, I., and Iqbal, K. (1997) Alzheimer disease hyperphosphorylated tau aggregates hydrophobically. Synapse 27, 208-229
    • (1997) Synapse , vol.27 , pp. 208-229
    • Ruben, G.C.1    Ciardelli, T.L.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 117
    • 0142062098 scopus 로고    scopus 로고
    • Aggregation of α-synuclein in the pathogenesis of Parkinson's disease
    • III11-III14
    • Iwatsubo, T. (2003) Aggregation of α-synuclein in the pathogenesis of Parkinson's disease. J. Neurol. 250(Suppl. 3), III11-III14
    • (2003) J. Neurol , vol.250 , Issue.SUPPL. 3
    • Iwatsubo, T.1
  • 119
    • 0035997016 scopus 로고    scopus 로고
    • Protein aggregation in Huntington's disease
    • Hoffner, G., and Djian, P. (2002) Protein aggregation in Huntington's disease. Biochimie (Paris) 84, 273-278
    • (2002) Biochimie (Paris) , vol.84 , pp. 273-278
    • Hoffner, G.1    Djian, P.2
  • 120
    • 0032585594 scopus 로고    scopus 로고
    • Creutzfeldt-Jakob disease and related transmissible spongiform encephalopathies
    • Johnson, R. T., and Gibbs, C. J., Jr. (1998) Creutzfeldt-Jakob disease and related transmissible spongiform encephalopathies. N. Engl. J. Med. 339, 1994-2004
    • (1998) N. Engl. J. Med , vol.339 , pp. 1994-2004
    • Johnson, R.T.1    Gibbs Jr., C.J.2
  • 121
    • 0032828301 scopus 로고    scopus 로고
    • Disease associated prion protein may deposit in the peripheral nervous system in human transmissible spongiform encephalopathies
    • Hainfellner, J. A., and Budka, H. (1999) Disease associated prion protein may deposit in the peripheral nervous system in human transmissible spongiform encephalopathies. Acta Neuropathol. (Berl.) 98, 458-460
    • (1999) Acta Neuropathol. (Berl.) , vol.98 , pp. 458-460
    • Hainfellner, J.A.1    Budka, H.2
  • 123
    • 0011766298 scopus 로고
    • Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of α-trace basic protein (cystatin C)
    • Ghiso, J., Jensson, O., and Frangione, B. (1986) Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of α-trace basic protein (cystatin C). Proc. Natl. Acad. Sci. U. S. A. 83, 2974-2978
    • (1986) Proc. Natl. Acad. Sci. U. S. A , vol.83 , pp. 2974-2978
    • Ghiso, J.1    Jensson, O.2    Frangione, B.3
  • 127
    • 33947245436 scopus 로고    scopus 로고
    • Transthyretin and familial amyloidotic polyneuropathy. Recent progress in understanding the molecular mechanism of neurodegeneration
    • Hou, X., Aguilar, M. I., and Small, D. H. (2007) Transthyretin and familial amyloidotic polyneuropathy. Recent progress in understanding the molecular mechanism of neurodegeneration. FEBS J. 274, 1637-1650
    • (2007) FEBS J , vol.274 , pp. 1637-1650
    • Hou, X.1    Aguilar, M.I.2    Small, D.H.3
  • 129
    • 0024342752 scopus 로고
    • Islet amyloid, islet-amyloid polypeptide, and diabetes mellitus
    • Johnson, K. H., O'Brien, T. D., Betsholtz, C., and Westermark, P. (1989) Islet amyloid, islet-amyloid polypeptide, and diabetes mellitus. N. Engl. J. Med. 321, 513-518
    • (1989) N. Engl. J. Med , vol.321 , pp. 513-518
    • Johnson, K.H.1    O'Brien, T.D.2    Betsholtz, C.3    Westermark, P.4
  • 132
    • 0015441947 scopus 로고
    • Thermal (or endothermic) aggregation of sickle cell hemoglobin (Hb S) during sickling
    • Murayama, M. (1972) Thermal (or endothermic) aggregation of sickle cell hemoglobin (Hb S) during sickling. Adv. Exp. Med. Biol. 28, 243-251
    • (1972) Adv. Exp. Med. Biol , vol.28 , pp. 243-251
    • Murayama, M.1
  • 133
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 134
    • 0025992417 scopus 로고
    • In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity
    • Pike, C. J., Walencewicz, A. J., Glabe, C. G., and Cotman, C. W. (1991) In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res. 563, 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
  • 135
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., and Selkoe, D. J. (1999) Protofibrillar intermediates of amyloid β-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19, 8876-8884
    • (1999) J. Neurosci , vol.19 , 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
  • 136
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
    • Geula, C., Wu, C. K., Saroff, D., Lorenzo, A., Yuan, M., and Yankner, B. A. (1998) Aging renders the brain vulnerable to amyloid β-protein neurotoxicity. Nat. Med. 4, 827-831
    • (1998) Nat. Med , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6
  • 137
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 140
    • 0028096074 scopus 로고
    • Stability of cell size and nucleolar size in Lewy body containing neurons of substantia nigra in Parkinson's disease
    • Gertz, H. J., Siegers, A., and Kuchinke, J. (1994) Stability of cell size and nucleolar size in Lewy body containing neurons of substantia nigra in Parkinson's disease. Brain Res. 637, 339-341
    • (1994) Brain Res , vol.637 , pp. 339-341
    • Gertz, H.J.1    Siegers, A.2    Kuchinke, J.3
  • 141
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: Evidence for toxicity of nonfibrillar aggregates
    • Sousa, M. M., Cardoso, I., Fernandes, R., Guimaraes, A., and Saraiva, M. J. (2001) Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am. J. Pathol. 159, 1993-2000
    • (2001) Am. J. Pathol , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 142
    • 0036381074 scopus 로고    scopus 로고
    • Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules
    • Kourie, J. I., and Henry, C. L. (2002) Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules. Clin. Exp. Pharmacol. Physiol. 29, 741-753
    • (2002) Clin. Exp. Pharmacol. Physiol , vol.29 , pp. 741-753
    • Kourie, J.I.1    Henry, C.L.2
  • 143
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao, R. V., and Bredesen, D. E. (2004) Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr. Opin. Cell Biol. 16, 653-662
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 144
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation
    • Soreghan, B., Kosmoski, J., and Glabe, C. (1994) Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation. J. Biol. Chem. 269, 28551-28554
    • (1994) J. Biol. Chem , vol.269 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 145
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., and Lansbury, P. T., Jr. (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418, 291
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 146
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov, T. A., Lin, M. C., and Kagan, B. L. (1996) Pore formation by the cytotoxic islet amyloid peptide amylin. J. Biol. Chem. 271, 1988-1992
    • (1996) J. Biol. Chem , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 147
    • 33646126948 scopus 로고    scopus 로고
    • Membrane permeabilization: A common mechanism in protein-misfolding diseases
    • Lashuel, H. A. (2005) Membrane permeabilization: a common mechanism in protein-misfolding diseases. Sci. Aging Knowledge Environ. 2005, e28
    • (2005) Sci. Aging Knowledge Environ , vol.2005
    • Lashuel, H.A.1
  • 148
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., and Glabe, C. G. (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280, 17294-17300
    • (2005) J. Biol. Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 149
    • 33645141853 scopus 로고    scopus 로고
    • ER stress and neurodegenerative diseases
    • Lindholm, D., Wootz, H., and Korhonen, L. (2006) ER stress and neurodegenerative diseases. Cell Death Differ. 13, 385-392
    • (2006) Cell Death Differ , vol.13 , pp. 385-392
    • Lindholm, D.1    Wootz, H.2    Korhonen, L.3
  • 150
    • 34548356689 scopus 로고    scopus 로고
    • Causes of oxidative stress in Alzheimer disease
    • Zhu, X., Su, B., Wang, X., Smith, M. A., and Perry, G. (2007) Causes of oxidative stress in Alzheimer disease. Cell. Mol. Life Sci. 64, 2202-2210
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 2202-2210
    • Zhu, X.1    Su, B.2    Wang, X.3    Smith, M.A.4    Perry, G.5
  • 151
    • 1642483509 scopus 로고    scopus 로고
    • Neurodegenerative diseases and oxidative stress
    • Emerit, J., Edeas, M., and Bricaire, F. (2004) Neurodegenerative diseases and oxidative stress. Biomed. Pharmacother. 58, 39-46
    • (2004) Biomed. Pharmacother , vol.58 , pp. 39-46
    • Emerit, J.1    Edeas, M.2    Bricaire, F.3
  • 152
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M., and Dobson, C. M. (2003) Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81, 678-699
    • (2003) J. Mol. Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 153
    • 0035478618 scopus 로고    scopus 로고
    • β-Amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima, Y., Gotoh, Y., Zieg, J., Barrett, T., Takano, H., Flavell, R., Davis, R. J., Shirasaki, Y., and Greenberg, M. E. (2001) β-Amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. J. Neurosci. 21, 7551-7560
    • (2001) J. Neurosci , vol.21 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6    Davis, R.J.7    Shirasaki, Y.8    Greenberg, M.E.9
  • 155
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal, M. F. (2002) Oxidatively modified proteins in aging and disease. Free. Radic. Biol. Med. 32, 797-803
    • (2002) Free. Radic. Biol. Med , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 156
    • 33750058573 scopus 로고    scopus 로고
    • Oxidative stress-induced intestinal epithelial cell apoptosis is mediated by p38 MAPK
    • Zhou, Y., Wang, Q., Mark, E. B., and Chung, D. H. (2006) Oxidative stress-induced intestinal epithelial cell apoptosis is mediated by p38 MAPK. Biochem. Biophys. Res. Commun. 350, 860-865
    • (2006) Biochem. Biophys. Res. Commun , vol.350 , pp. 860-865
    • Zhou, Y.1    Wang, Q.2    Mark, E.B.3    Chung, D.H.4
  • 157
    • 3242729360 scopus 로고    scopus 로고
    • Mechanisms of hormesis through mild heat stress on human cells
    • Rattan, S. I. (2004) Mechanisms of hormesis through mild heat stress on human cells. Ann. N. Y. Acad. Sci. 1019, 554-558
    • (2004) Ann. N. Y. Acad. Sci , vol.1019 , pp. 554-558
    • Rattan, S.I.1
  • 158
    • 33846981910 scopus 로고    scopus 로고
    • IL-1β stimulates rat cardiac fibroblast migration via MAP kinase pathways
    • Mitchell, M. D., Laird, R. E., Brown, R. D., and Long, C. S. (2007) IL-1β stimulates rat cardiac fibroblast migration via MAP kinase pathways. Am. J. Physiol. 292, H1139-H1147
    • (2007) Am. J. Physiol , vol.292
    • Mitchell, M.D.1    Laird, R.E.2    Brown, R.D.3    Long, C.S.4
  • 159
    • 34147096369 scopus 로고    scopus 로고
    • Systemic inflammation, infection, ApoE alleles, and Alzheimer disease: A position paper
    • Finch, C. E., and Morgan, T. E. (2007) Systemic inflammation, infection, ApoE alleles, and Alzheimer disease: a position paper. Curr. Alzheimer Res. 4, 185-189
    • (2007) Curr. Alzheimer Res , vol.4 , pp. 185-189
    • Finch, C.E.1    Morgan, T.E.2
  • 160
    • 33847613885 scopus 로고    scopus 로고
    • Inflammatory processes in Alzheimer's disease
    • Heneka, M. T., and O'Banion, M. K. (2007) Inflammatory processes in Alzheimer's disease. J. Neuroimmunol. 184, 69-91
    • (2007) J. Neuroimmunol , vol.184 , pp. 69-91
    • Heneka, M.T.1    O'Banion, M.K.2
  • 161
    • 0034612175 scopus 로고    scopus 로고
    • Akiyama, H., Barger, S., Barnum, S., Bradt, B., Bauer, J., Cole, G. M., Cooper, N. R., Eikelenboom, P., Emmerling, M., Fiebich, B. L., Finch, C. E., Frautschy, S., Griffin, W. S., Hampel, H., Hull, M., Landreth, G., Lue, L., Mrak, R., Mackenzie, I. R., McGeer, P. L., O'Banion, M. K., Pachter, J., Pasinetti, G., Plata-Salaman, C., Rogers, J., Rydel, R., Shen, Y., Streit, W., Strohmeyer, R., Tooyoma, I., Van Muiswinkel, F. L., Veerhuis, R., Walker, D., Webster, S., Wegrzyniak, B., Wenk, G., and Wyss-Coray, T. (2000) Inflammation and Alzheimer's disease. Neurobiol. Aging 21, 383-421
    • Akiyama, H., Barger, S., Barnum, S., Bradt, B., Bauer, J., Cole, G. M., Cooper, N. R., Eikelenboom, P., Emmerling, M., Fiebich, B. L., Finch, C. E., Frautschy, S., Griffin, W. S., Hampel, H., Hull, M., Landreth, G., Lue, L., Mrak, R., Mackenzie, I. R., McGeer, P. L., O'Banion, M. K., Pachter, J., Pasinetti, G., Plata-Salaman, C., Rogers, J., Rydel, R., Shen, Y., Streit, W., Strohmeyer, R., Tooyoma, I., Van Muiswinkel, F. L., Veerhuis, R., Walker, D., Webster, S., Wegrzyniak, B., Wenk, G., and Wyss-Coray, T. (2000) Inflammation and Alzheimer's disease. Neurobiol. Aging 21, 383-421
  • 163
    • 34250712274 scopus 로고    scopus 로고
    • Inflammatory mechanisms of diabetic complications
    • Williams, M. D., and Nadler, J. L. (2007) Inflammatory mechanisms of diabetic complications. Curr. Diab. Rep. 7, 242-248
    • (2007) Curr. Diab. Rep , vol.7 , pp. 242-248
    • Williams, M.D.1    Nadler, J.L.2
  • 164
    • 33748857338 scopus 로고    scopus 로고
    • Pathogenesis of prion diseases: Current status and future outlook
    • Aguzzi, A., and Heikenwalder, M. (2006) Pathogenesis of prion diseases: current status and future outlook. Nat. Rev. Microbiol. 4, 765-775
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 765-775
    • Aguzzi, A.1    Heikenwalder, M.2
  • 165
    • 0030758270 scopus 로고    scopus 로고
    • Evolution of a strain of CJD that induces BSE-like plaques
    • Manuelidis, L., Fritch, W., and Xi, Y. G. (1997) Evolution of a strain of CJD that induces BSE-like plaques. Science 277, 94-98
    • (1997) Science , vol.277 , pp. 94-98
    • Manuelidis, L.1    Fritch, W.2    Xi, Y.G.3
  • 166
    • 34250214950 scopus 로고    scopus 로고
    • The macrophage at the crossroads of insulin resistance and atherosclerosis
    • Liang, C. P., Han, S., Senokuchi, T., and Tall, A. R. (2007) The macrophage at the crossroads of insulin resistance and atherosclerosis. Circ. Res. 100, 1546-1555
    • (2007) Circ. Res , vol.100 , pp. 1546-1555
    • Liang, C.P.1    Han, S.2    Senokuchi, T.3    Tall, A.R.4
  • 168
    • 0037184995 scopus 로고    scopus 로고
    • Pattern recognition receptors: Doubling up for the innate immune response
    • Gordon, S. (2002) Pattern recognition receptors: doubling up for the innate immune response. Cell 111, 927-930
    • (2002) Cell , vol.111 , pp. 927-930
    • Gordon, S.1
  • 169
    • 33846194125 scopus 로고    scopus 로고
    • Innate immunity - cross-talk with adaptive immunity through pattern recognition receptors and cytokines
    • Kabelitz, D., and Medzhitov, R. (2007) Innate immunity - cross-talk with adaptive immunity through pattern recognition receptors and cytokines. Curr. Opin. Immunol. 19, 1-3
    • (2007) Curr. Opin. Immunol , vol.19 , pp. 1-3
    • Kabelitz, D.1    Medzhitov, R.2
  • 170
    • 0034833822 scopus 로고    scopus 로고
    • CD36: A class B scavenger receptor involved in angiogenesis, atherosclerosis, inflammation, and lipid metabolism
    • Febbraio, M., Hajjar, D. P., and Silverstein, R. L. (2001) CD36: a class B scavenger receptor involved in angiogenesis, atherosclerosis, inflammation, and lipid metabolism. J. Clin. Invest. 108, 785-791
    • (2001) J. Clin. Invest , vol.108 , pp. 785-791
    • Febbraio, M.1    Hajjar, D.P.2    Silverstein, R.L.3
  • 172
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz, J., and Strickland, D. K. (2001) LRP: a multifunctional scavenger and signaling receptor. J. Clin. Invest. 108, 779-784
    • (2001) J. Clin. Invest , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 173
    • 7644225312 scopus 로고    scopus 로고
    • RAGE (yin) versus LRP (yang) balance regulates Alzheimer amyloid β-peptide clearance through transport across the blood-brain barrier
    • Deane, R., Wu, Z., and Zlokovic, B. V. (2004) RAGE (yin) versus LRP (yang) balance regulates Alzheimer amyloid β-peptide clearance through transport across the blood-brain barrier. Stroke 35, 2628-2631
    • (2004) Stroke , vol.35 , pp. 2628-2631
    • Deane, R.1    Wu, Z.2    Zlokovic, B.V.3
  • 175
    • 16844363404 scopus 로고    scopus 로고
    • Tissue plasminogen activator in central nervous system physiology and pathology
    • Melchor, J. P., and Strickland, S. (2005) Tissue plasminogen activator in central nervous system physiology and pathology. Thromb. Haemost. 93, 655-660
    • (2005) Thromb. Haemost , vol.93 , pp. 655-660
    • Melchor, J.P.1    Strickland, S.2
  • 176
    • 14644392228 scopus 로고    scopus 로고
    • Amyloid-β-stimulated plasminogen activation by tissue-type plasminogen activator results in processing of neuroendocrine factors
    • Kranenburg, O., Gent, Y. Y., Romijn, E. P., Voest, E. E., Heck, A. J., and Gebbink, M. F. (2005) Amyloid-β-stimulated plasminogen activation by tissue-type plasminogen activator results in processing of neuroendocrine factors. Neuroscience 131, 877-886
    • (2005) Neuroscience , vol.131 , pp. 877-886
    • Kranenburg, O.1    Gent, Y.Y.2    Romijn, E.P.3    Voest, E.E.4    Heck, A.J.5    Gebbink, M.F.6
  • 177
  • 179
    • 0028265646 scopus 로고
    • Formation of amyloid-like substance from β-2-microglobulin in vitro: Role of serum amyloid P component: a preliminary study
    • Ono, K., and Uchino, F. (1994) Formation of amyloid-like substance from β-2-microglobulin in vitro: role of serum amyloid P component: a preliminary study. Nephron 66, 404-407
    • (1994) Nephron , vol.66 , pp. 404-407
    • Ono, K.1    Uchino, F.2
  • 181
    • 0029932195 scopus 로고    scopus 로고
    • Localization and cell association of C1q in Alzheimer's disease brain
    • Afagh, A., Cummings, B. J., Cribbs, D. H., Cotman, C. W., and Tenner, A. J. (1996) Localization and cell association of C1q in Alzheimer's disease brain. Exp. Neurol. 138, 22-32
    • (1996) Exp. Neurol , vol.138 , pp. 22-32
    • Afagh, A.1    Cummings, B.J.2    Cribbs, D.H.3    Cotman, C.W.4    Tenner, A.J.5
  • 183
    • 0028178458 scopus 로고
    • β-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain
    • Jiang, H., Burdick, D., Glabe, C. G., Cotman, C. W., and Tenner, A. J. (1994) β-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain. J. Immunol. 152, 5050-5059
    • (1994) J. Immunol , vol.152 , pp. 5050-5059
    • Jiang, H.1    Burdick, D.2    Glabe, C.G.3    Cotman, C.W.4    Tenner, A.J.5
  • 184
    • 15544372950 scopus 로고    scopus 로고
    • Complement protein C1q recognizes a conformationally modified form of the prion protein
    • Blanquet-Grossard, F., Thielens, N. M., Vendrely, C., Jamin, M., and Arlaud, G. J. (2005) Complement protein C1q recognizes a conformationally modified form of the prion protein. Biochemistry 44, 4349-4356
    • (2005) Biochemistry , vol.44 , pp. 4349-4356
    • Blanquet-Grossard, F.1    Thielens, N.M.2    Vendrely, C.3    Jamin, M.4    Arlaud, G.J.5
  • 187
    • 34547823043 scopus 로고    scopus 로고
    • The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures
    • Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., and Wilson, M. R. (2007) The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures. FASEB J. 21, 2312-2322
    • (2007) FASEB J , vol.21 , pp. 2312-2322
    • Yerbury, J.J.1    Poon, S.2    Meehan, S.3    Thompson, B.4    Kumita, J.R.5    Dobson, C.M.6    Wilson, M.R.7
  • 188
    • 8644230195 scopus 로고    scopus 로고
    • Glycoxidized low-density lipoprotein regulates the expression of scavenger receptors in THP-1 macrophages
    • Lam, M. C., Tan, K. C., and Lam, K. S. (2004) Glycoxidized low-density lipoprotein regulates the expression of scavenger receptors in THP-1 macrophages. Atherosclerosis 177, 313-320
    • (2004) Atherosclerosis , vol.177 , pp. 313-320
    • Lam, M.C.1    Tan, K.C.2    Lam, K.S.3
  • 190
    • 0035670769 scopus 로고    scopus 로고
    • Scavenger receptor-like receptors for the binding of lipopolysaccharide and lipoteichoic acid to liver endothelial and Kupffer cells
    • Van Oosten, M., van Amersfoort, E. S., Van Berkel, T. J., and Kuiper, J. (2001) Scavenger receptor-like receptors for the binding of lipopolysaccharide and lipoteichoic acid to liver endothelial and Kupffer cells. J. Endotoxin Res. 7, 381-384
    • (2001) J. Endotoxin Res , vol.7 , pp. 381-384
    • Van Oosten, M.1    van Amersfoort, E.S.2    Van Berkel, T.J.3    Kuiper, J.4
  • 191
    • 0030702820 scopus 로고    scopus 로고
    • The macrophage scavenger receptor type A is expressed by activated macrophages and protects the host against lethal endotoxic shock
    • Haworth, R., Platt, N., Keshav, S., Hughes, D., Darley, E., Suzuki, H., Kurihara, Y., Kodama, T., and Gordon, S. (1997) The macrophage scavenger receptor type A is expressed by activated macrophages and protects the host against lethal endotoxic shock. J. Exp. Med. 186, 1431-1439
    • (1997) J. Exp. Med , vol.186 , pp. 1431-1439
    • Haworth, R.1    Platt, N.2    Keshav, S.3    Hughes, D.4    Darley, E.5    Suzuki, H.6    Kurihara, Y.7    Kodama, T.8    Gordon, S.9
  • 192
    • 0034598314 scopus 로고    scopus 로고
    • Protection from lethal gram-positive infection by macrophage scavenger receptor-dependent phagocytosis
    • Thomas, C. A., Li, Y., Kodama, T., Suzuki, H., Silverstein, S. C., and El Khoury, J. (2000) Protection from lethal gram-positive infection by macrophage scavenger receptor-dependent phagocytosis. J. Exp. Med. 191, 147-156
    • (2000) J. Exp. Med , vol.191 , pp. 147-156
    • Thomas, C.A.1    Li, Y.2    Kodama, T.3    Suzuki, H.4    Silverstein, S.C.5    El Khoury, J.6
  • 193
    • 0033018443 scopus 로고    scopus 로고
    • Class A scavenger receptors and the phagocytosis of apoptotic cells
    • Platt, N., da Silva, R. P., and Gordon, S. (1999) Class A scavenger receptors and the phagocytosis of apoptotic cells. Immunol. Lett. 65, 15-19
    • (1999) Immunol. Lett , vol.65 , pp. 15-19
    • Platt, N.1    da Silva, R.P.2    Gordon, S.3
  • 194
    • 0036701873 scopus 로고    scopus 로고
    • Scavenger receptors that recognize advanced glycation end products
    • Miyazaki, A., Nakayama, H., and Horiuchi, S. (2002) Scavenger receptors that recognize advanced glycation end products. Trends Cardiovasc. Med. 12, 258-262
    • (2002) Trends Cardiovasc. Med , vol.12 , pp. 258-262
    • Miyazaki, A.1    Nakayama, H.2    Horiuchi, S.3
  • 195
    • 13544273816 scopus 로고    scopus 로고
    • Expression of class A scavenger receptor is enhanced by high glucose in vitro and under diabetic conditions in vivo: One mechanism for an increased rate of atherosclerosis in diabetes
    • Fukuhara-Takaki, K., Sakai, M., Sakamoto, Y., Takeya, M., and Horiuchi, S. (2005) Expression of class A scavenger receptor is enhanced by high glucose in vitro and under diabetic conditions in vivo: one mechanism for an increased rate of atherosclerosis in diabetes. J. Biol. Chem. 280, 3355-3364
    • (2005) J. Biol. Chem , vol.280 , pp. 3355-3364
    • Fukuhara-Takaki, K.1    Sakai, M.2    Sakamoto, Y.3    Takeya, M.4    Horiuchi, S.5
  • 196
    • 1542615079 scopus 로고    scopus 로고
    • Reduced infiltration of class A scavenger receptor positive antigen-presenting cells is associated with prostate cancer progression
    • Yang, G., Addai, J., Tian, W. H., Frolov, A., Wheeler, T. M., and Thompson, T. C. (2004) Reduced infiltration of class A scavenger receptor positive antigen-presenting cells is associated with prostate cancer progression. Cancer Res. 64, 2076-2082
    • (2004) Cancer Res , vol.64 , pp. 2076-2082
    • Yang, G.1    Addai, J.2    Tian, W.H.3    Frolov, A.4    Wheeler, T.M.5    Thompson, T.C.6
  • 197
    • 0024230760 scopus 로고
    • Identification of platelet membrane thrombospondin binding molecules using an anti-thrombospondin antibody
    • Kieffer, N., Nurden, A. T., Hasitz, M., Titeux, M., and Breton-Gorius, J. (1988) Identification of platelet membrane thrombospondin binding molecules using an anti-thrombospondin antibody. Biochim. Biophys. Acta 967, 408-415
    • (1988) Biochim. Biophys. Acta , vol.967 , pp. 408-415
    • Kieffer, N.1    Nurden, A.T.2    Hasitz, M.3    Titeux, M.4    Breton-Gorius, J.5
  • 198
    • 33751519372 scopus 로고    scopus 로고
    • Oxidized phosphatidylserine-CD36 interactions play an essential role in macrophage-dependent phagocytosis of apoptotic cells
    • Greenberg, M. E., Sun, M., Zhang, R., Febbraio, M., Silverstein, R., and Hazen, S. L. (2006) Oxidized phosphatidylserine-CD36 interactions play an essential role in macrophage-dependent phagocytosis of apoptotic cells. J. Exp. Med. 203, 2613-2625
    • (2006) J. Exp. Med , vol.203 , pp. 2613-2625
    • Greenberg, M.E.1    Sun, M.2    Zhang, R.3    Febbraio, M.4    Silverstein, R.5    Hazen, S.L.6
  • 199
    • 0029918601 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte membrane protein 1 is a parasitized erythrocyte receptor for adherence to CD36, thrombospondin, and intercellular adhesion molecule 1
    • Baruch, D. I., Gormely, J. A., Ma, C., Howard, R. J., and Pasloske, B. L. (1996) Plasmodium falciparum erythrocyte membrane protein 1 is a parasitized erythrocyte receptor for adherence to CD36, thrombospondin, and intercellular adhesion molecule 1. Proc. Natl. Acad. Sci. U. S. A. 93, 3497-3502
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 3497-3502
    • Baruch, D.I.1    Gormely, J.A.2    Ma, C.3    Howard, R.J.4    Pasloske, B.L.5
  • 201
    • 0028997232 scopus 로고
    • The class B scavenger receptors SR-BI and CD36 are receptors for anionic phospholipids
    • Rigotti, A., Acton, S. L., and Krieger, M. (1995) The class B scavenger receptors SR-BI and CD36 are receptors for anionic phospholipids. J. Biol. Chem. 270, 16221-16224
    • (1995) J. Biol. Chem , vol.270 , pp. 16221-16224
    • Rigotti, A.1    Acton, S.L.2    Krieger, M.3
  • 202
    • 33750613413 scopus 로고    scopus 로고
    • Intraretinal lipid transport is dependent on high density lipoprotein-like particles and class B scavenger receptors
    • Tserentsoodol, N., Gordiyenko, N. V., Pascual, I., Lee, J. W., Fliesler, S. J., and Rodriguez, I. R. (2006) Intraretinal lipid transport is dependent on high density lipoprotein-like particles and class B scavenger receptors. Mol. Vis. 12, 1319-1333
    • (2006) Mol. Vis , vol.12 , pp. 1319-1333
    • Tserentsoodol, N.1    Gordiyenko, N.V.2    Pascual, I.3    Lee, J.W.4    Fliesler, S.J.5    Rodriguez, I.R.6
  • 203
  • 204
    • 33847692795 scopus 로고    scopus 로고
    • CD36 is a receptor for oxidized high density lipoprotein: Implications for the development of atherosclerosis
    • Thorne, R. F., Mhaidat, N. M., Ralston, K. J., and Burns, G. F. (2007) CD36 is a receptor for oxidized high density lipoprotein: implications for the development of atherosclerosis. FEBS Lett. 581, 1227-1232
    • (2007) FEBS Lett , vol.581 , pp. 1227-1232
    • Thorne, R.F.1    Mhaidat, N.M.2    Ralston, K.J.3    Burns, G.F.4
  • 205
    • 34548420275 scopus 로고    scopus 로고
    • Atherogenic scavenger receptor modulation in the tubulointerstitium in response to chronic renal injury
    • Okamura, D. M., Lopez-Guisa, J. M., Koelsch, K., Collins, S. J., and Eddy, A. A. (2007) Atherogenic scavenger receptor modulation in the tubulointerstitium in response to chronic renal injury. Am. J. Physiol. 293, F575-F585
    • (2007) Am. J. Physiol , vol.293
    • Okamura, D.M.1    Lopez-Guisa, J.M.2    Koelsch, K.3    Collins, S.J.4    Eddy, A.A.5
  • 206
    • 0035993485 scopus 로고    scopus 로고
    • LOX-1, the receptor for oxidized low-density lipoprotein identified from endothelial cells: Implications in endothelial dysfunction and atherosclerosis
    • Chen, M., Masaki, T., and Sawamura, T. (2002) LOX-1, the receptor for oxidized low-density lipoprotein identified from endothelial cells: implications in endothelial dysfunction and atherosclerosis. Pharmacol. Ther. 95, 89-100
    • (2002) Pharmacol. Ther , vol.95 , pp. 89-100
    • Chen, M.1    Masaki, T.2    Sawamura, T.3
  • 207
    • 0346100518 scopus 로고    scopus 로고
    • Scavenger receptors for oxidized and glycated proteins
    • Horiuchi, S., Sakamoto, Y., and Sakai, M. (2003) Scavenger receptors for oxidized and glycated proteins. Amino Acids 25, 283-292
    • (2003) Amino Acids , vol.25 , pp. 283-292
    • Horiuchi, S.1    Sakamoto, Y.2    Sakai, M.3
  • 208
    • 33746058246 scopus 로고    scopus 로고
    • Lectin-like oxidized low-density lipoprotein receptor-1-mediated autophagy in human granulosa cells as an alternative of programmed cell death
    • Duerrschmidt, N., Zabirnyk, O., Nowicki, M., Ricken, A., Hmeidan, F. A., Blumenauer, V., Borlak, J., and Spanel-Borowski, K. (2006) Lectin-like oxidized low-density lipoprotein receptor-1-mediated autophagy in human granulosa cells as an alternative of programmed cell death. Endocrinology 147, 3851-3860
    • (2006) Endocrinology , vol.147 , pp. 3851-3860
    • Duerrschmidt, N.1    Zabirnyk, O.2    Nowicki, M.3    Ricken, A.4    Hmeidan, F.A.5    Blumenauer, V.6    Borlak, J.7    Spanel-Borowski, K.8
  • 209
    • 0034602694 scopus 로고    scopus 로고
    • A platele-tendothelium interaction mediated by lectin-like oxidized low-density lipoprotein receptor-1
    • Kakutani, M., Masaki, T., and Sawamura, T. (2000) A platele-tendothelium interaction mediated by lectin-like oxidized low-density lipoprotein receptor-1. Proc. Natl. Acad. Sci. U. S. A. 97, 360-364
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 360-364
    • Kakutani, M.1    Masaki, T.2    Sawamura, T.3
  • 211
    • 33947616359 scopus 로고    scopus 로고
    • Lectin-like oxidized LDL receptor-1 (LOX-1) expression is associated with atherosclerotic plaque instability-analysis in hypercholesterolemic rabbits
    • Ishino, S., Mukai, T., Kume, N., Asano, D., Ogawa, M., Kuge, Y., Minami, M., Kita, T., Shiomi, M., and Saji, H. (2007) Lectin-like oxidized LDL receptor-1 (LOX-1) expression is associated with atherosclerotic plaque instability-analysis in hypercholesterolemic rabbits. Atherosclerosis 195, 48-56
    • (2007) Atherosclerosis , vol.195 , pp. 48-56
    • Ishino, S.1    Mukai, T.2    Kume, N.3    Asano, D.4    Ogawa, M.5    Kuge, Y.6    Minami, M.7    Kita, T.8    Shiomi, M.9    Saji, H.10
  • 212
    • 0034277471 scopus 로고    scopus 로고
    • Atherosclerosis and diabetes: The RAGE connection
    • Schmidt, A. M., and Stern, D. (2000) Atherosclerosis and diabetes: the RAGE connection. Curr. Atheroscler. Rep. 2, 430-436
    • (2000) Curr. Atheroscler. Rep , vol.2 , pp. 430-436
    • Schmidt, A.M.1    Stern, D.2
  • 213
    • 0036566144 scopus 로고    scopus 로고
    • Stimulation of erythroleukaemia cell differentiation by extracellular high-mobility group-box protein 1 is independent of the receptor for advanced glycation end-products
    • Sparatore, B., Pedrazzi, M., Passalacqua, M., Gaggero, D., Patrone, M., Pontremoli, S., and Melloni, E. (2002) Stimulation of erythroleukaemia cell differentiation by extracellular high-mobility group-box protein 1 is independent of the receptor for advanced glycation end-products. Biochem. J. 363, 529-535
    • (2002) Biochem. J , vol.363 , pp. 529-535
    • Sparatore, B.1    Pedrazzi, M.2    Passalacqua, M.3    Gaggero, D.4    Patrone, M.5    Pontremoli, S.6    Melloni, E.7
  • 214
    • 1842421190 scopus 로고    scopus 로고
    • S100B causes apoptosis in a myoblast cell line in a RAGE-independent manner
    • Sorci, G., Riuzzi, F., Agneletti, A. L., Marchetti, C., and Donato, R. (2004) S100B causes apoptosis in a myoblast cell line in a RAGE-independent manner. J. Cell. Physiol. 199, 274-283
    • (2004) J. Cell. Physiol , vol.199 , pp. 274-283
    • Sorci, G.1    Riuzzi, F.2    Agneletti, A.L.3    Marchetti, C.4    Donato, R.5
  • 216
    • 0342646984 scopus 로고    scopus 로고
    • Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor κ-B (NF-κ-B) activation
    • Sousa, M. M., Yan, S. D., Stern, D., and Saraiva, M. J. (2000) Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor κ-B (NF-κ-B) activation. Lab. Invest. 80, 1101-1110
    • (2000) Lab. Invest , vol.80 , pp. 1101-1110
    • Sousa, M.M.1    Yan, S.D.2    Stern, D.3    Saraiva, M.J.4
  • 217
    • 0034840664 scopus 로고    scopus 로고
    • Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: Identification of a cellular activation mechanism
    • Lue, L. F., Walker, D. G., Brachova, L., Beach, T. G., Rogers, J., Schmidt, A. M., Stern, D. M., and Yan, S. D. (2001) Involvement of microglial receptor for advanced glycation endproducts (RAGE) in Alzheimer's disease: identification of a cellular activation mechanism. Exp. Neurol. 171, 29-45
    • (2001) Exp. Neurol , vol.171 , pp. 29-45
    • Lue, L.F.1    Walker, D.G.2    Brachova, L.3    Beach, T.G.4    Rogers, J.5    Schmidt, A.M.6    Stern, D.M.7    Yan, S.D.8
  • 218
    • 32544440202 scopus 로고    scopus 로고
    • Rheumatoid arthritis: Links with cardiovascular disease and the receptor for advanced glycation end products
    • Carroll, L., Hannawi, S., Marwick, T., and Thomas, R. (2006) Rheumatoid arthritis: links with cardiovascular disease and the receptor for advanced glycation end products. Wien. Med. Wochenschr. 156, 42-52
    • (2006) Wien. Med. Wochenschr , vol.156 , pp. 42-52
    • Carroll, L.1    Hannawi, S.2    Marwick, T.3    Thomas, R.4
  • 219
    • 0029118511 scopus 로고
    • LDL receptor-related protein: A multiligand receptor for lipoprotein and proteinase catabolism
    • Strickland, D. K., Kounnas, M. Z., and Argraves, W. S. (1995) LDL receptor-related protein: a multiligand receptor for lipoprotein and proteinase catabolism. FASEB J. 9, 890-898
    • (1995) FASEB J , vol.9 , pp. 890-898
    • Strickland, D.K.1    Kounnas, M.Z.2    Argraves, W.S.3
  • 220
    • 0030716260 scopus 로고    scopus 로고
    • The efficient catabolism of thrombin-protease nexin 1 complexes is a synergistic mechanism that requires both the LDL receptor-related protein and cell surface heparins
    • Knauer, M. F., Kridel, S. J., Hawley, S. B., and Knauer, D. J. (1997) The efficient catabolism of thrombin-protease nexin 1 complexes is a synergistic mechanism that requires both the LDL receptor-related protein and cell surface heparins. J. Biol. Chem. 272, 29039-29045
    • (1997) J. Biol. Chem , vol.272 , pp. 29039-29045
    • Knauer, M.F.1    Kridel, S.J.2    Hawley, S.B.3    Knauer, D.J.4
  • 221
    • 0029007213 scopus 로고
    • Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1
    • Godyna, S., Liau, G., Popa, I., Stefansson, S., and Argraves, W. S. (1995) Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1. J. Cell Biol. 129, 1403-1410
    • (1995) J. Cell Biol , vol.129 , pp. 1403-1410
    • Godyna, S.1    Liau, G.2    Popa, I.3    Stefansson, S.4    Argraves, W.S.5
  • 222
    • 0028988551 scopus 로고
    • 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein
    • Bu, G., Geuze, H. J., Strous, G. J., and Schwartz, A. L. (1995) 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein. EMBO J. 14, 2269-2280
    • (1995) EMBO J , vol.14 , pp. 2269-2280
    • Bu, G.1    Geuze, H.J.2    Strous, G.J.3    Schwartz, A.L.4
  • 225
    • 20444374712 scopus 로고    scopus 로고
    • LRP and Alzheimer's disease
    • Zerbinatti, C. V. and Bu, G. (2005) LRP and Alzheimer's disease. Rev. Neurosci. 16, 123-135
    • (2005) Rev. Neurosci , vol.16 , pp. 123-135
    • Zerbinatti, C.V.1    Bu, G.2
  • 226
    • 0027459457 scopus 로고
    • Initial interaction between fibrin and tissue plasminogen activator (t-PA): The Gly-Pro-Arg-Pro binding site on fibrin(ogen) is important for t-PA activity
    • Kaczmarek, E., Lee, M. H., and McDonagh, J. (1993) Initial interaction between fibrin and tissue plasminogen activator (t-PA): the Gly-Pro-Arg-Pro binding site on fibrin(ogen) is important for t-PA activity. J. Biol. Chem. 268, 2474-2479
    • (1993) J. Biol. Chem , vol.268 , pp. 2474-2479
    • Kaczmarek, E.1    Lee, M.H.2    McDonagh, J.3
  • 228
    • 0001886135 scopus 로고
    • Plasma concentration of endogenous tissue plasminogen activator and the occurrence of future cardiovascular events
    • Ridker, P. M. (1994) Plasma concentration of endogenous tissue plasminogen activator and the occurrence of future cardiovascular events. J. Thromb. Thrombolysis 1, 35-40
    • (1994) J. Thromb. Thrombolysis , vol.1 , pp. 35-40
    • Ridker, P.M.1
  • 229
    • 0031019170 scopus 로고    scopus 로고
    • Characterization of the binding of serum amyloid P to laminin
    • Zahedi, K. (1997) Characterization of the binding of serum amyloid P to laminin. J. Biol. Chem. 272, 2143-2148
    • (1997) J. Biol. Chem , vol.272 , pp. 2143-2148
    • Zahedi, K.1
  • 230
    • 0030434792 scopus 로고    scopus 로고
    • The interaction of C-reactive protein and serum amyloid P component with nuclear antigens
    • Du Clos, T. W. (1996) The interaction of C-reactive protein and serum amyloid P component with nuclear antigens. Mol. Biol. Rep. 23, 253-260
    • (1996) Mol. Biol. Rep , vol.23 , pp. 253-260
    • Du Clos, T.W.1
  • 231
    • 0028108537 scopus 로고
    • Binding of pentraxins to different nuclear structures: C-reactive protein binds to small nuclear ribonucleoprotein particles, serum amyloid P component binds to chromatin and nucleoli
    • Pepys, M. B., Booth, S. E., Tennent, G. A., Butler, P. J., and Williams, D. G. (1994) Binding of pentraxins to different nuclear structures: C-reactive protein binds to small nuclear ribonucleoprotein particles, serum amyloid P component binds to chromatin and nucleoli. Clin. Exp. Immunol. 97, 152-157
    • (1994) Clin. Exp. Immunol , vol.97 , pp. 152-157
    • Pepys, M.B.1    Booth, S.E.2    Tennent, G.A.3    Butler, P.J.4    Williams, D.G.5
  • 233
    • 0034106274 scopus 로고    scopus 로고
    • Serum amyloid P component bound to gram-negative bacteria prevents lipopolysaccharide-mediated classical pathway complement activation
    • De Haas, C. J., van Leeuwen, E. M., van Bommel, T., Verhoef, J., van Kessel, K. P., and van Strijp, J. A. (2000) Serum amyloid P component bound to gram-negative bacteria prevents lipopolysaccharide-mediated classical pathway complement activation. Infect. Immun. 68, 1753-1759
    • (2000) Infect. Immun , vol.68 , pp. 1753-1759
    • De Haas, C.J.1    van Leeuwen, E.M.2    van Bommel, T.3    Verhoef, J.4    van Kessel, K.P.5    van Strijp, J.A.6
  • 234
    • 0033485355 scopus 로고    scopus 로고
    • New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein
    • De Haas, C. J. (1999) New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein. FEMS Immunol. Med. Microbiol. 26, 197-202
    • (1999) FEMS Immunol. Med. Microbiol , vol.26 , pp. 197-202
    • De Haas, C.J.1
  • 235
  • 236
    • 0142011170 scopus 로고    scopus 로고
    • Serum amyloid P component induces neuronal apoptosis and β-amyloid immunoreactivity
    • Urbanyi, Z., Laszlo, L., Tomasi, T. B., Toth, E., Mekes, E., Sass, M., and Pazmany, T. (2003) Serum amyloid P component induces neuronal apoptosis and β-amyloid immunoreactivity. Brain Res. 988, 69-77
    • (2003) Brain Res , vol.988 , pp. 69-77
    • Urbanyi, Z.1    Laszlo, L.2    Tomasi, T.B.3    Toth, E.4    Mekes, E.5    Sass, M.6    Pazmany, T.7
  • 238
    • 0035575742 scopus 로고    scopus 로고
    • β-Amyloid fibrils activate the C1 complex of complement under physiological conditions: Evidence for a binding site for Aβ on the C1q globular regions
    • Tacnet-Delorme, P., Chevallier, S., and Arlaud, G. J. (2001) β-Amyloid fibrils activate the C1 complex of complement under physiological conditions: evidence for a binding site for Aβ on the C1q globular regions. J. Immunol. 167, 6374-6381
    • (2001) J. Immunol , vol.167 , pp. 6374-6381
    • Tacnet-Delorme, P.1    Chevallier, S.2    Arlaud, G.J.3
  • 239
    • 1842610580 scopus 로고    scopus 로고
    • Down syndrome and β-amyloid deposition
    • Head, E., and Lott, I. T. (2004) Down syndrome and β-amyloid deposition. Curr. Opin. Neurol. 17, 95-100
    • (2004) Curr. Opin. Neurol , vol.17 , pp. 95-100
    • Head, E.1    Lott, I.T.2
  • 240
    • 3242766671 scopus 로고    scopus 로고
    • Absence of C1q leads to less neuropathology in transgenic mouse models of Alzheimer's disease
    • Fonseca, M. I., Zhou, J., Botto, M., and Tenner, A. J. (2004) Absence of C1q leads to less neuropathology in transgenic mouse models of Alzheimer's disease. J. Neurosci. 24, 6457-6465
    • (2004) J. Neurosci , vol.24 , pp. 6457-6465
    • Fonseca, M.I.1    Zhou, J.2    Botto, M.3    Tenner, A.J.4
  • 241
    • 0030250394 scopus 로고    scopus 로고
    • Relationship between multifunctional protein "clusterin" and Alzheimer disease
    • Choi-Miura, N. H., and Oda, T. (1996) Relationship between multifunctional protein "clusterin" and Alzheimer disease. Neurobiol. Aging 17, 717-722
    • (1996) Neurobiol. Aging , vol.17 , pp. 717-722
    • Choi-Miura, N.H.1    Oda, T.2
  • 242
    • 0029845259 scopus 로고    scopus 로고
    • Clusterin, a putative complement regulator, binds to the cell surface of Staphylococcus aureus clinical isolates
    • Partridge, S. R., Baker, M. S., Walker, M. J., and Wilson, M. R. (1996) Clusterin, a putative complement regulator, binds to the cell surface of Staphylococcus aureus clinical isolates. Infect. Immun. 64, 4324-4329
    • (1996) Infect. Immun , vol.64 , pp. 4324-4329
    • Partridge, S.R.1    Baker, M.S.2    Walker, M.J.3    Wilson, M.R.4
  • 245
    • 0036829661 scopus 로고    scopus 로고
    • Trougakos, I. P., Gonos, E. S. (2002) Clusterin/apolipoprotein J in human aging and cancer. Int. J. Biochem. Cell. Biol. 34, 1430-1448
    • Trougakos, I. P., Gonos, E. S. (2002) Clusterin/apolipoprotein J in human aging and cancer. Int. J. Biochem. Cell. Biol. 34, 1430-1448
  • 248
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 249
    • 0038612852 scopus 로고    scopus 로고
    • Amyloid as a natural product
    • Kelly, J. W., and Balch, W. E. (2003) Amyloid as a natural product. J. Cell Biol. 161, 461-462
    • (2003) J. Cell Biol , vol.161 , pp. 461-462
    • Kelly, J.W.1    Balch, W.E.2
  • 250
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
    • Litvinovich, S. V., Brew, S. A., Aota, S., Akiyama, S. K., Haudenschild, C., and Ingham, K. C. (1998) Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J. Mol. Biol. 280, 245-258
    • (1998) J. Mol. Biol , vol.280 , pp. 245-258
    • Litvinovich, S.V.1    Brew, S.A.2    Aota, S.3    Akiyama, S.K.4    Haudenschild, C.5    Ingham, K.C.6
  • 251
    • 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
    • Kallijarvi, J., Haltia, M., and Baumann, M. H. (2001) 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. Biochemistry 40, 10032-10037
    • (2001) Biochemistry , vol.40 , pp. 10032-10037
    • Kallijarvi, J.1    Haltia, M.2    Baumann, M.H.3
  • 254
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson, J. F., Theos, A. C., Harper, D. C., Tenza, D., Raposo, G., and Marks, M. S. (2003) Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol. 161, 521-533
    • (2003) J. Cell Biol , vol.161 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 260
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct
    • Necula, M., Kayed, R., Milton, S., and Glabe, C. G. (2007) Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282, 10311-10324
    • (2007) J. Biol. Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 261
    • 33947644267 scopus 로고    scopus 로고
    • Heparan sulfate as a therapeutic target in amyloidogenesis: Prospects and possible complications
    • Kisilevsky, R., Ancsin, J. B., Szarek, W. A., and Petanceska, S. (2007) Heparan sulfate as a therapeutic target in amyloidogenesis: prospects and possible complications. Amyloid 14, 21-32
    • (2007) Amyloid , vol.14 , pp. 21-32
    • Kisilevsky, R.1    Ancsin, J.B.2    Szarek, W.A.3    Petanceska, S.4
  • 263
    • 0035818516 scopus 로고    scopus 로고
    • Support for the multigenic hypothesis of amyloidosis: The binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro
    • White, J. T., and Kelly, J. W. (2001) Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro. Proc. Natl. Acad. Sci. U. S. A. 98, 13019-13024
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 13019-13024
    • White, J.T.1    Kelly, J.W.2
  • 264
    • 0033783730 scopus 로고    scopus 로고
    • Vaccination for the prevention and treatment of Alzheimer's disease
    • Solomon, B., and Frenkel, D. (2000) Vaccination for the prevention and treatment of Alzheimer's disease. Drugs Today (Barc.) 36, 655-663
    • (2000) Drugs Today (Barc.) , vol.36 , pp. 655-663
    • Solomon, B.1    Frenkel, D.2
  • 265
    • 33645220400 scopus 로고    scopus 로고
    • Targeting amyloid-β peptide (Aβ) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Aβ precursor protein (APP) transgenic mice
    • Lee, E. B., Leng, L. Z., Zhang, B., Kwong, L., Trojanowski, J. Q., Abel, T., and Lee, V. M. (2006) Targeting amyloid-β peptide (Aβ) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Aβ precursor protein (APP) transgenic mice. J. Biol. Chem. 281, 4292-4299
    • (2006) J. Biol. Chem , vol.281 , pp. 4292-4299
    • Lee, E.B.1    Leng, L.Z.2    Zhang, B.3    Kwong, L.4    Trojanowski, J.Q.5    Abel, T.6    Lee, V.M.7
  • 266
    • 0842269766 scopus 로고    scopus 로고
    • Anti-Aβ: The good, the bad, and the unforeseen
    • Broytman, O., and Malter, J. S. (2004) Anti-Aβ: the good, the bad, and the unforeseen. J. Neurosci. Res. 75, 301-306
    • (2004) J. Neurosci. Res , vol.75 , pp. 301-306
    • Broytman, O.1    Malter, J.S.2
  • 270
    • 0036260808 scopus 로고    scopus 로고
    • Toxicity of β-amyloid vaccination in patients with Alzheimer's disease
    • Imbimbo, B. P. (2002) Toxicity of β-amyloid vaccination in patients with Alzheimer's disease. Ann. Neurol. 51, 794
    • (2002) Ann. Neurol , vol.51 , pp. 794
    • Imbimbo, B.P.1
  • 271
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain, B., and Wetzel, R. (2002) Conformational Abs recognizing a generic amyloid fibril epitope. Proc. Natl. Acad. Sci. U. S. A. 99, 1485-1490
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 272
    • 34250004883 scopus 로고    scopus 로고
    • Clinical immunologic approaches for the treatment of Alzheimer's disease
    • Solomon, B. (2007) Clinical immunologic approaches for the treatment of Alzheimer's disease. Expert Opin. Investig. Drugs 16, 819-828
    • (2007) Expert Opin. Investig. Drugs , vol.16 , pp. 819-828
    • Solomon, B.1
  • 273
    • 0029738444 scopus 로고    scopus 로고
    • The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-β2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway: Implications for the pathogenesis of dialysis-related amyloidosis
    • Miyata, T., Hori, O., Zhang, J., Yan, S. D., Ferran, L., Iida, Y., and Schmidt, A. M. (1996) The receptor for advanced glycation end products (RAGE) is a central mediator of the interaction of AGE-β2microglobulin with human mononuclear phagocytes via an oxidant-sensitive pathway: implications for the pathogenesis of dialysis-related amyloidosis. J. Clin. Invest. 98, 1088-1094
    • (1996) J. Clin. Invest , vol.98 , pp. 1088-1094
    • Miyata, T.1    Hori, O.2    Zhang, J.3    Yan, S.D.4    Ferran, L.5    Iida, Y.6    Schmidt, A.M.7
  • 274
    • 33745741894 scopus 로고    scopus 로고
    • Soluble receptor for advanced glycation end products: From disease marker to potential therapeutic target
    • Geroldi, D., Falcone, C., and Emanuele, E. (2006) Soluble receptor for advanced glycation end products: from disease marker to potential therapeutic target. Curr. Med. Chem. 13, 1971-1978
    • (2006) Curr. Med. Chem , vol.13 , pp. 1971-1978
    • Geroldi, D.1    Falcone, C.2    Emanuele, E.3
  • 280
    • 0033788789 scopus 로고    scopus 로고
    • Tissue plasminogen activator requires plasminogen to modulate amyloid-β neurotoxicity and deposition
    • Tucker, H. M., Kihiko-Ehmann, M., Wright, S., Rydel, R. E., and Estus, S. (2000) Tissue plasminogen activator requires plasminogen to modulate amyloid-β neurotoxicity and deposition. J. Neurochem. 75, 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
  • 281
    • 25144499286 scopus 로고    scopus 로고
    • A role for the plasminogen activator system in inflammation and neurodegeneration in the central nervous system during experimental allergic encephalomyelitis
    • East, E., Baker, D., Pryce, G., Lijnen, H. R., Cuzner, M. L., and Gveric, D. (2005) A role for the plasminogen activator system in inflammation and neurodegeneration in the central nervous system during experimental allergic encephalomyelitis. Am. J. Pathol. 167, 545-554
    • (2005) Am. J. Pathol , vol.167 , pp. 545-554
    • East, E.1    Baker, D.2    Pryce, G.3    Lijnen, H.R.4    Cuzner, M.L.5    Gveric, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.