메뉴 건너뛰기




Volumn 24, Issue 11, 2010, Pages 4250-4261

Modulation of Aβ42 fibrillogenesis by glycosaminoglycan structure

Author keywords

Alzheimer's disease; Amyloid fibril structure; Fibrillogenesis enhancers and inhibitors; Polysaccharides

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN[1-42]; CHITOSAN; GLYCOSAMINOGLYCAN; HYALURONIC ACID; PEPTIDE; POLY(VINYL SULFATE); POLYVINYL DERIVATIVE; PROTEINASE; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

EID: 78649898216     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-153551     Document Type: Article
Times cited : (64)

References (78)
  • 1
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy, J. A., and Higgins, G. A. (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256, 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 2
    • 0036150827 scopus 로고    scopus 로고
    • Alzheimer's disease - Do tauists and baptists finally shake hands?
    • Mudher, A., and Lovestone, S. (2002) Alzheimer's disease - do tauists and baptists finally shake hands? Trends Neurosci. 25, 22-26
    • (2002) Trends Neurosci. , vol.25 , pp. 22-26
    • Mudher, A.1    Lovestone, S.2
  • 4
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson, M. P. (2004) Pathways towards and away from Alzheimer's disease. Nature 430, 631-639
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 5
    • 0032473596 scopus 로고    scopus 로고
    • Amyloid-β peptide activates cultured astrocytes: Morphological alterations, cytokine induction and nitric oxide release
    • Hu, J., Akama, K. T., Krafft, G. A., Chromy, B. A., and Van Eldik, L. J. (1998) Amyloid-β peptide activates cultured astrocytes: morphological alterations, cytokine induction and nitric oxide release. Brain Res. 785, 195-206
    • (1998) Brain Res. , vol.785 , pp. 195-206
    • Hu, J.1    Akama, K.T.2    Krafft, G.A.3    Chromy, B.A.4    Van Eldik, L.J.5
  • 6
    • 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
  • 7
    • 34249092704 scopus 로고    scopus 로고
    • Calcium and neurodegeneration
    • Mattson, M. P. (2007) Calcium and neurodegeneration. Aging Cell. 6, 337-350
    • (2007) Aging Cell. , vol.6 , pp. 337-350
    • Mattson, M.P.1
  • 9
    • 0003374626 scopus 로고    scopus 로고
    • Tau protein pathology in neurodegenerative diseases
    • Spillantini, M. G., and Goedert, M. (1998) Tau protein pathology in neurodegenerative diseases. Trends Neurosci. 21, 428-433
    • (1998) Trends Neurosci. , vol.21 , pp. 428-433
    • Spillantini, M.G.1    Goedert, M.2
  • 10
    • 0042508791 scopus 로고    scopus 로고
    • Neuropathologic changes in Alzheimer's disease
    • Wenk, G. L. (2003) Neuropathologic changes in Alzheimer's disease. J. Clin. Psychiatry 64, 7-10
    • (2003) J. Clin. Psychiatry , vol.64 , pp. 7-10
    • Wenk, G.L.1
  • 11
    • 0036548070 scopus 로고    scopus 로고
    • γ-Secretase, Notch, Aβ and Alzheimer's disease: Where do the presenilins fit in?
    • Sisodia, S. S., and George-Hyslop, P. H. (2002) γ-Secretase, Notch, Aβ and Alzheimer's disease: where do the presenilins fit in? Nat. Rev. Neurosci. 3, 281-290
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 281-290
    • Sisodia, S.S.1    George-Hyslop, P.H.2
  • 12
    • 0842307665 scopus 로고    scopus 로고
    • Amyloidosis of Alzheimer's Aβ peptides: Solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies
    • Antzutkin, O. N. (2004) Amyloidosis of Alzheimer's Aβ peptides: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies. Magn. Reson. Chem. 42, 231-246
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 231-246
    • Antzutkin, O.N.1
  • 16
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of Aβ 1-40: Implications for the search for Aβ fibril formation inhibitors
    • Goldsbury, C. S., Wirtz, S., Müller, S. A., Sunderji, S., Wicki, P., Aebi, U., and Frey, P. (2000) Studies on the in vitro assembly of Aβ 1-40: implications for the search for Aβ fibril formation inhibitors. J. Struct. Biol. 130, 217-231
    • (2000) J. Struct. Biol. , vol.130 , pp. 217-231
    • Goldsbury, C.S.1    Wirtz, S.2    Müller, S.A.3    Sunderji, S.4    Wicki, P.5    Aebi, U.6    Frey, P.7
  • 17
  • 18
    • 34547162589 scopus 로고    scopus 로고
    • Solid-state NMR as a method to reveal structure and membrane-interaction of amyloidogenic proteins and peptides
    • Naito, A., and Kawamura, I. (2007) Solid-state NMR as a method to reveal structure and membrane-interaction of amyloidogenic proteins and peptides. Biochim. Biophys. Acta 1768, 1900-1912
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1900-1912
    • Naito, A.1    Kawamura, I.2
  • 22
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotypes, and treatments
    • Selkoe, D. J. (1997) Alzheimer's disease: genotypes, phenotypes, and treatments. Science 275, 630-631
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 24
    • 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
  • 26
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • Ferreira, S. T., Vieira, M. N., and De Felice, F. G. (2007) Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases. IUBMB Life 59, 332-345
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 28
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • Serpell, L. C. (2000) Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 1502, 16-30
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 29
    • 0029823181 scopus 로고    scopus 로고
    • Brain extracellular matrix
    • Ruoslahti, E. (1996) Brain extracellular matrix. Glycobiology 6, 489-492
    • (1996) Glycobiology , vol.6 , pp. 489-492
    • Ruoslahti, E.1
  • 30
    • 0042703654 scopus 로고    scopus 로고
    • Amyloidogenesis: Historical and modern observations point to heparan sulfate proteoglycans as a major culprit
    • Ancsin, J. B. (2003) Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit. Amyloid 10, 67-79
    • (2003) Amyloid , vol.10 , pp. 67-79
    • Ancsin, J.B.1
  • 32
    • 0024273721 scopus 로고
    • The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease
    • Snow, A. D., Mar, H., Nochlin, D., Kimata, K., Kato, M., Suzuki, S., Hassell, J., and Wight, T. N. (1988) The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease. Am. J. Pathol. 133, 456-463
    • (1988) Am. J. Pathol. , vol.133 , pp. 456-463
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kimata, K.4    Kato, M.5    Suzuki, S.6    Hassell, J.7    Wight, T.N.8
  • 33
    • 0026548436 scopus 로고
    • Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease
    • Snow, A. D., Mar, H., Nochlin, D., Kresse, H., and Wight, T. N. (1992) Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease. J. Histochem. Cytochem. 40, 105-113
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 105-113
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3    Kresse, H.4    Wight, T.N.5
  • 34
    • 0029881267 scopus 로고    scopus 로고
    • Identification and immunolocalization of a new class of proteoglycan (keratan sulfate) to the neuritic plaques of Alzheimer's disease
    • Snow, A. D., Nochlin, D., Sekiguchi, R., and Carlson, S. S. (1996) Identification and immunolocalization of a new class of proteoglycan (keratan sulfate) to the neuritic plaques of Alzheimer's disease. Exp. Neurol. 138, 305-317
    • (1996) Exp. Neurol. , vol.138 , pp. 305-317
    • Snow, A.D.1    Nochlin, D.2    Sekiguchi, R.3    Carlson, S.S.4
  • 35
    • 0026468915 scopus 로고
    • Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease
    • Su, J. H., Cummings, B. J., and Cotman, C. W. (1992) Localization of heparan sulfate glycosaminoglycan and proteoglycan core protein in aged brain and Alzheimer's disease. Neuroscience 51, 801-813
    • (1992) Neuroscience , vol.51 , pp. 801-813
    • Su, J.H.1    Cummings, B.J.2    Cotman, C.W.3
  • 36
    • 0027209456 scopus 로고
    • Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease
    • DeWitt, D. A., Silver, J., Canning, D. R., and Perry, G. (1993) Chondroitin sulfate proteoglycans are associated with the lesions of Alzheimer's disease. Exp. Neurol. 121, 149-152
    • (1993) Exp. Neurol. , vol.121 , pp. 149-152
    • DeWitt, D.A.1    Silver, J.2    Canning, D.R.3    Perry, G.4
  • 37
    • 0028978227 scopus 로고
    • Proteoglycan-mediated inhibition of aβ proteolysis. A potential cause of senile plaque accumulation
    • Gupta-Bansal, R., Frederickson, R. C., and Brunden, K. R. (1995) Proteoglycan-mediated inhibition of Aβ proteolysis. A potential cause of senile plaque accumulation. J. Biol. Chem. 270, 18666-18671
    • (1995) J. Biol. Chem. , vol.270 , pp. 18666-18671
    • Gupta-Bansal, R.1    Frederickson, R.C.2    Brunden, K.R.3
  • 38
    • 0031895939 scopus 로고    scopus 로고
    • Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation
    • Castillo, G. M., Cummings, J. A., Yang, W., Judge, M. E., Sheardown, M. J., Rimvall, K., Hansen, J. B., and Snow, A. D. (1998) Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. Diabetes 47, 612-620
    • (1998) Diabetes , vol.47 , pp. 612-620
    • Castillo, G.M.1    Cummings, J.A.2    Yang, W.3    Judge, M.E.4    Sheardown, M.J.5    Rimvall, K.6    Hansen, J.B.7    Snow, A.D.8
  • 40
    • 0033548474 scopus 로고    scopus 로고
    • The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis
    • Ancsin, J. B., and Kisilevsky, R. (1999) The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis. J. Biol. Chem. 274, 7172-7181
    • (1999) J. Biol. Chem. , vol.274 , pp. 7172-7181
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 41
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro
    • Cohlberg, J. A., Li, J., Uversky, V. N., and Fink, A. L. (2002) Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro. Biochemistry 41, 1502-1511
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 42
    • 3042760011 scopus 로고    scopus 로고
    • Prion protein conversion in vitro
    • Supattapone, S. (2004) Prion protein conversion in vitro. J. Mol. Med. 82, 348-356
    • (2004) J. Mol. Med. , vol.82 , pp. 348-356
    • Supattapone, S.1
  • 44
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., and Crowther, R. A. (1996) Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 383, 550-553
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 45
    • 0033572813 scopus 로고    scopus 로고
    • Interactions of Alzheimer amyloid-β peptides with glycosaminoglycans. Effects on fibril nucleation and growth
    • McLaurin, J., Franklin, T., Zhang, X., Deng, J., and Fraser, P. E. (1999) Interactions of Alzheimer amyloid-β peptides with glycosaminoglycans. Effects on fibril nucleation and growth. Eur. J. Biochem. 266, 1101-1110
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1101-1110
    • McLaurin, J.1    Franklin, T.2    Zhang, X.3    Deng, J.4    Fraser, P.E.5
  • 46
    • 0033026552 scopus 로고    scopus 로고
    • The sulfate moieties of glycosaminoglycans are critical for the enhancement of β-amyloid protein fibril formation
    • Castillo, G. M., Lukito, W., Wight, T. N., and Snow, A. D. (1999) The sulfate moieties of glycosaminoglycans are critical for the enhancement of β-amyloid protein fibril formation. J. Neurochem. 72, 1681-1687
    • (1999) J. Neurochem. , vol.72 , pp. 1681-1687
    • Castillo, G.M.1    Lukito, W.2    Wight, T.N.3    Snow, A.D.4
  • 47
    • 0028792576 scopus 로고
    • Heparan sulfate and chondroitin sulfate glycosaminoglycan attenuate β-amyloid(25-35) induced neurodegeneration in cultured hippocampal neurons
    • Woods, A. G., Cribbs, D. H., Whittemore, E. R., and Cotman, C. W. (1995) Heparan sulfate and chondroitin sulfate glycosaminoglycan attenuate β-amyloid(25-35) induced neurodegeneration in cultured hippocampal neurons. Brain. Res. 697, 53-62
    • (1995) Brain. Res. , vol.697 , pp. 53-62
    • Woods, A.G.1    Cribbs, D.H.2    Whittemore, E.R.3    Cotman, C.W.4
  • 49
    • 0028870182 scopus 로고
    • Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β-amyloid in rat PC12 cells
    • Pollack, S. J., Sadler, I. I., Hawtin, S. R., Tailor, V. J., and Shearman, M. S. (1995) Sulfated glycosaminoglycans and dyes attenuate the neurotoxic effects of β-amyloid in rat PC12 cells. Neurosci. Lett. 184, 113-116
    • (1995) Neurosci. Lett. , vol.184 , pp. 113-116
    • Pollack, S.J.1    Sadler, I.I.2    Hawtin, S.R.3    Tailor, V.J.4    Shearman, M.S.5
  • 51
    • 0343939111 scopus 로고    scopus 로고
    • Cortical areas abundant in extracellular matrix chondroitin sulphate proteoglycans are less affected by cytoskeletal changes in Alzheimer's disease
    • Brückner, G., Hausen, D., Härtig, W., Drlicek, M., Arendt, T., and Brauer, K. (1999) Cortical areas abundant in extracellular matrix chondroitin sulphate proteoglycans are less affected by cytoskeletal changes in Alzheimer's disease. Neuroscience 92, 791-805
    • (1999) Neuroscience , vol.92 , pp. 791-805
    • Brückner, G.1    Hausen, D.2    Härtig, W.3    Drlicek, M.4    Arendt, T.5    Brauer, K.6
  • 52
    • 0035997236 scopus 로고    scopus 로고
    • Glycosaminoglycans and β-amyloid, prion and tau peptides in neurodegenerative diseases
    • Díaz-Nido, J., Wandosell, F., and Avila, J. (2002) Glycosaminoglycans and β-amyloid, prion and tau peptides in neurodegenerative diseases. Peptides 23, 1323-1332
    • (2002) Peptides , vol.23 , pp. 1323-1332
    • Díaz-Nido, J.1    Wandosell, F.2    Avila, J.3
  • 53
    • 0033755865 scopus 로고    scopus 로고
    • Effect of amino-acid substitutions on Alzheimer's amyloid-β peptide-glycosaminoglycan interactions
    • McLaurin, J., and Fraser, P. E. (2000) Effect of amino-acid substitutions on Alzheimer's amyloid-β peptide-glycosaminoglycan interactions. Eur. J. Biochem. 267, 6353-6361
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6353-6361
    • McLaurin, J.1    Fraser, P.E.2
  • 54
    • 11144221004 scopus 로고    scopus 로고
    • Amyloid accomplices and enforcers
    • Alexandrescu, A. T. (2005) Amyloid accomplices and enforcers. Protein. Sci. 14, 1-12
    • (2005) Protein. Sci. , vol.14 , pp. 1-12
    • Alexandrescu, A.T.1
  • 56
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman, D. A., Case, D. A., Caldwell, J. W., Ross, W. S., Cheatham, T. E., Debolt, S., Ferguson, D., Seibel, G., and Kollman, P. (1995) AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun. 91, 1-41
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham, T.E.5    Debolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 58
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., Mantsch, H. H., and Chapman, D. (1993) Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry 32, 389-394
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 59
    • 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
  • 60
    • 0035794123 scopus 로고    scopus 로고
    • Amyloid-β interactions with chondroitin sulfate-derived monosaccharides and disaccharides. Implications for drug development
    • Fraser, P. E., Darabie, A. A., and McLaurin, J. A. (2001) Amyloid-β interactions with chondroitin sulfate-derived monosaccharides and disaccharides. Implications for drug development. J. Biol. Chem. 276, 6412-6419
    • (2001) J. Biol. Chem. , vol.276 , pp. 6412-6419
    • Fraser, P.E.1    Darabie, A.A.2    McLaurin, J.A.3
  • 61
    • 0034130950 scopus 로고    scopus 로고
    • Conformational behavior of hyaluronan in relation to its physical properties as probed by molecular modeling
    • Haxaire, K., Braccini, I., Milas, M., Rinaudo, M., and Pérez, S. (2000) Conformational behavior of hyaluronan in relation to its physical properties as probed by molecular modeling. Glycobiology 10, 587-594
    • (2000) Glycobiology , vol.10 , pp. 587-594
    • Haxaire, K.1    Braccini, I.2    Milas, M.3    Rinaudo, M.4    Pérez, S.5
  • 62
    • 0034110252 scopus 로고    scopus 로고
    • Glycosaminoglycan conformation: Do aqueous molecular dynamics simulations agree with x-ray fiber diffraction?
    • Almond, A., and Sheehan, J. K. (2000) Glycosaminoglycan conformation: do aqueous molecular dynamics simulations agree with x-ray fiber diffraction? Glycobiology 10, 329-338
    • (2000) Glycobiology , vol.10 , pp. 329-338
    • Almond, A.1    Sheehan, J.K.2
  • 63
    • 0038713317 scopus 로고    scopus 로고
    • Conformational behavior of chondroitin and chondroitin sulfate in relation to their physical properties as inferred by molecular modeling
    • Rodríguez-Carvajal, M. A., Imberty, A., and Pérez, S. (2003) Conformational behavior of chondroitin and chondroitin sulfate in relation to their physical properties as inferred by molecular modeling. Biopolymers 69, 15-28
    • (2003) Biopolymers , vol.69 , pp. 15-28
    • Rodríguez-Carvajal, M.A.1    Imberty, A.2    Pérez, S.3
  • 64
    • 0027164634 scopus 로고
    • N.m.r. and molecular-modelling studies of the solution conformation of heparin
    • Mulloy, B., Forster, M. J., Jones, C., and Davies, D. B. (1993) N.m.r. and molecular-modelling studies of the solution conformation of heparin. Biochem. J. 293, 849-858
    • (1993) Biochem. J. , vol.293 , pp. 849-858
    • Mulloy, B.1    Forster, M.J.2    Jones, C.3    Davies, D.B.4
  • 65
    • 39949084677 scopus 로고    scopus 로고
    • Intriguing nucleic-acid-binding features of mammalian prion protein
    • Silva, J. L., Lima, L. M., Foguel, D., and Cordeiro, Y. (2008) Intriguing nucleic-acid-binding features of mammalian prion protein. Trends Biochem. Sci. 33, 132-140
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 132-140
    • Silva, J.L.1    Lima, L.M.2    Foguel, D.3    Cordeiro, Y.4
  • 67
    • 0022547855 scopus 로고
    • X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation
    • Kirschner, D. A., Abraham, C., and Selkoe, D. J. (1986) X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation. Proc. Natl. Acad. Sci. U. S. A. 83, 503-507
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 503-507
    • Kirschner, D.A.1    Abraham, C.2    Selkoe, D.J.3
  • 69
    • 0028741551 scopus 로고
    • Molecular and crystal structure of the anhydrous form of chitosan
    • Yui, T., Imada, K., Okuyama, K., Obata, Y., Suzuki, K., and Ogawa, K. (1994) Molecular and crystal structure of the anhydrous form of chitosan. Macromolecules 27, 7601-7605
    • (1994) Macromolecules , vol.27 , pp. 7601-7605
    • Yui, T.1    Imada, K.2    Okuyama, K.3    Obata, Y.4    Suzuki, K.5    Ogawa, K.6
  • 70
    • 2342648312 scopus 로고    scopus 로고
    • The AGE of the matrix: Chemistry, consequence and cure
    • DeGroot, J. (2004) The AGE of the matrix: chemistry, consequence and cure. Curr. Opin. Pharmacol. 4, 301-305
    • (2004) Curr. Opin. Pharmacol. , vol.4 , pp. 301-305
    • DeGroot, J.1
  • 71
    • 70449732132 scopus 로고    scopus 로고
    • Immunohistochemical analysis of human brain suggests pathological synergism of Alzheimer's disease and diabetes mellitus
    • Valente, T., Gella, A., Fernàndez-Busquets, X., Unzeta, M., and Durany, N. (2010) Immunohistochemical analysis of human brain suggests pathological synergism of Alzheimer's disease and diabetes mellitus. Neurobiol. Dis. 37, 67-76
    • (2010) Neurobiol. Dis. , vol.37 , pp. 67-76
    • Valente, T.1    Gella, A.2    Fernàndez-Busquets, X.3    Unzeta, M.4    Durany, N.5
  • 72
    • 7444236944 scopus 로고    scopus 로고
    • Protein trafficking in Plasmodium falciparum-infected red blood cells
    • Cooke, B. M., Lingelbach, K., Bannister, L. H., and Tilley, L. (2004) Protein trafficking in Plasmodium falciparum-infected red blood cells. Trends Parasitol. 20, 581-589
    • (2004) Trends Parasitol. , vol.20 , pp. 581-589
    • Cooke, B.M.1    Lingelbach, K.2    Bannister, L.H.3    Tilley, L.4
  • 74
    • 34548644754 scopus 로고    scopus 로고
    • Merozoite surface protein 2 of Plasmodium falciparum: Expression, structure, dynamics, and fibril formation of the conserved N-terminal domain
    • Low, A., Chandrashekaran, I. R., Adda, C. G., Yao, S., Sabo, J. K., Zhang, X., Soetopo, A., Anders, R. F., and Norton, R. S. (2007) Merozoite surface protein 2 of Plasmodium falciparum: expression, structure, dynamics, and fibril formation of the conserved N-terminal domain. Biopolymers 87, 12-22
    • (2007) Biopolymers , vol.87 , pp. 12-22
    • Low, A.1    Chandrashekaran, I.R.2    Adda, C.G.3    Yao, S.4    Sabo, J.K.5    Zhang, X.6    Soetopo, A.7    Anders, R.F.8    Norton, R.S.9
  • 75
    • 37349023138 scopus 로고    scopus 로고
    • A partially structured region of a largely unstructured protein, Plasmodium falciparum merozoite surface protein 2 (MSP2), forms amyloid-like fibrils
    • Yang, X., Adda, C. G., Keizer, D. W., Murphy, V. J., Rizkalla, M. M., Perugini, M. A., Jackson, D. C., Anders, R. F., and Norton, R. S. (2007) A partially structured region of a largely unstructured protein, Plasmodium falciparum merozoite surface protein 2 (MSP2), forms amyloid-like fibrils. J. Pept. Sci. 13, 839-848
    • (2007) J. Pept. Sci. , vol.13 , pp. 839-848
    • Yang, X.1    Adda, C.G.2    Keizer, D.W.3    Murphy, V.J.4    Rizkalla, M.M.5    Perugini, M.A.6    Jackson, D.C.7    Anders, R.F.8    Norton, R.S.9
  • 76
    • 0034210687 scopus 로고    scopus 로고
    • The Duffy-binding-like domain 1 of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a heparan sulfate ligand that requires 12 mers for binding
    • Barragan, A., Fernandez, V., Chen, Q., von Euler, A., Wahlgren, M., and Spillmann, D. (2000) The Duffy-binding-like domain 1 of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a heparan sulfate ligand that requires 12 mers for binding. Blood 95, 3594-3599
    • (2000) Blood , vol.95 , pp. 3594-3599
    • Barragan, A.1    Fernandez, V.2    Chen, Q.3    Von Euler, A.4    Wahlgren, M.5    Spillmann, D.6
  • 77
    • 21544432431 scopus 로고    scopus 로고
    • Inhibition of chondroitin-4-sulfate-specific adhesion of Plasmodium falciparum-infected erythrocytes by sulfated polysaccharides
    • Andrews, K. T., Klatt, N., Adams, Y., Mischnick, P., and Schwartz- Albiez, R. (2005) Inhibition of chondroitin-4-sulfate-specific adhesion of Plasmodium falciparum-infected erythrocytes by sulfated polysaccharides. Infect. Immun. 73, 4288-4294
    • (2005) Infect. Immun. , vol.73 , pp. 4288-4294
    • Andrews, K.T.1    Klatt, N.2    Adams, Y.3    Mischnick, P.4    Schwartz-Albiez, R.5
  • 78
    • 51349147433 scopus 로고    scopus 로고
    • Structure of the DBL3x domain of pregnancy-associated malaria protein VAR2CSA complexed with chondroitin sulfate A
    • Singh, K., Gittis, A. G., Nguyen, P., Gowda, D. C., Miller, L. H., and Garboczi, D. N. (2008) Structure of the DBL3x domain of pregnancy-associated malaria protein VAR2CSA complexed with chondroitin sulfate A. Nat. Struct. Mol. Biol. 15, 932-938
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 932-938
    • Singh, K.1    Gittis, A.G.2    Nguyen, P.3    Gowda, D.C.4    Miller, L.H.5    Garboczi, D.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.