메뉴 건너뛰기




Volumn 104, Issue 6, 2008, Pages 1553-1564

Curcumin binds to the α-helical intermediate and to the amyloid form of prion protein - A new mechanism for the inhibition of PrPSc accumulation

Author keywords

Amyloid; Congo red; Curcumin; Intermediate; Oligomer; Prion

Indexed keywords

AMYLOID; CONGO RED; CURCUMIN; OLIGOMER; PRION PROTEIN; PROTEIN ANTIBODY; THIOFLAVINE;

EID: 39849110292     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.05105.x     Document Type: Article
Times cited : (122)

References (64)
  • 1
    • 0037475148 scopus 로고    scopus 로고
    • In vitro detection of (S)-naproxen and ibuprofen binding to plaques in the Alzheimer's brain using the positron emission tomography molecular imaging probe 2-(1-[6-[(2-[(18)F]fluoroethyl)(methyl) amino]-2-naphthyl]ethylidene) malono nitrile
    • Agdeppa E. D., Kepe V., Petri A., Satyamurthy N., Liu J., Huang S. C., Small G. W., Cole G. M. and Barrio J. R. (2003) In vitro detection of (S)-naproxen and ibuprofen binding to plaques in the Alzheimer's brain using the positron emission tomography molecular imaging probe 2-(1-[6-[(2-[(18)F] fluoroethyl)(methyl) amino]-2-naphthyl]ethylidene)malono nitrile. Neuroscience 117, 723-730.
    • (2003) Neuroscience , vol.117 , pp. 723-730
    • Agdeppa, E.D.1    Kepe, V.2    Petri, A.3    Satyamurthy, N.4    Liu, J.5    Huang, S.C.6    Small, G.W.7    Cole, G.M.8    Barrio, J.R.9
  • 2
    • 0345328130 scopus 로고    scopus 로고
    • Photophysical studies on binding of curcumin to bovine serum albumins
    • Barik A., Priyadarsini K. I. and Mohan H. (2003) Photophysical studies on binding of curcumin to bovine serum albumins. Photochem. Photobiol. 77, 597-603.
    • (2003) Photochem. Photobiol. , vol.77 , pp. 597-603
    • Barik, A.1    Priyadarsini, K.I.2    Mohan, H.3
  • 4
    • 0041335200 scopus 로고    scopus 로고
    • Molecular-imaging probe 2-(1-[6-[(2-fluoroethyl)( methyl) amino]-2-naphthyl]ethylidene) malononitrile labels prion plaques in vitro
    • Bresjanac M., Smid L. M., Vovko T. D., Petric A., Barrio J. R. and Popovic M. (2003) Molecular-imaging probe 2-(1-[6-[(2-fluoroethyl)( methyl) amino]-2-naphthyl]ethylidene) malononitrile labels prion plaques in vitro. J. Neurosci. 23, 8029-8033.
    • (2003) J. Neurosci. , vol.23 , pp. 8029-8033
    • Bresjanac, M.1    Smid, L.M.2    Vovko, T.D.3    Petric, A.4    Barrio, J.R.5    Popovic, M.6
  • 5
    • 14844286460 scopus 로고    scopus 로고
    • Semiautomated cell-free conversion of prion protein: Applications for highthroughput screening of potential antiprion drugs
    • Breydo L., Bocharova O. V. and Baskakov I. V. (2005) Semiautomated cell-free conversion of prion protein: applications for highthroughput screening of potential antiprion drugs. Anal. Biochem. 339, 165-173.
    • (2005) Anal. Biochem. , vol.339 , pp. 165-173
    • Breydo, L.1    Bocharova, O.V.2    Baskakov, I.V.3
  • 6
    • 0031960745 scopus 로고    scopus 로고
    • A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils
    • Carter D. B. and Chou K. C. (1998) A model for structure-dependent binding of Congo red to Alzheimer beta-amyloid fibrils. Neurobiol. Aging 19, 37-40.
    • (1998) Neurobiol. Aging , vol.19 , pp. 37-40
    • Carter, D.B.1    Chou, K.C.2
  • 7
    • 6444225674 scopus 로고    scopus 로고
    • Prion diseases - Close to effective therapy?
    • Cashman N. R. and Caughey B. (2004) Prion diseases - close to effective therapy? Nat. Rev. Drug Discov. 3, 874-884.
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 874-884
    • Cashman, N.R.1    Caughey, B.2
  • 8
    • 0027280172 scopus 로고
    • Congo red inhibition of scrapie agent replication
    • Caughey B., Ernst D. and Race R. E. (1993) Congo red inhibition of scrapie agent replication. J. Virol. 67, 6270-6272.
    • (1993) J. Virol. , vol.67 , pp. 6270-6272
    • Caughey, B.1    Ernst, D.2    Race, R.E.3
  • 9
    • 0028256222 scopus 로고
    • Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and Congo red [corrected]
    • Caughey B., Brown K., Raymond G. J., Katzenstein G. E. and Thresher W. (1994) Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and Congo red [corrected]. J. Virol. 68, 2135-2141.
    • (1994) J. Virol. , vol.68 , pp. 2135-2141
    • Caughey, B.1    Brown, K.2    Raymond, G.J.3    Katzenstein, G.E.4    Thresher, W.5
  • 10
    • 0037405847 scopus 로고    scopus 로고
    • Inhibition of protease-resistant prion protein accumulation in vitro by curcumin
    • Caughey B., Raymond L. D., Raymond G. J., Maxson L., Silveira J. and Baron G. S. (2003) Inhibition of protease-resistant prion protein accumulation in vitro by curcumin. J. Virol. 77, 5499-5502.
    • (2003) J. Virol. , vol.77 , pp. 5499-5502
    • Caughey, B.1    Raymond, L.D.2    Raymond, G.J.3    Maxson, L.4    Silveira, J.5    Baron, G.S.6
  • 11
    • 0037291286 scopus 로고    scopus 로고
    • Safety and anti-inflammatory activity of curcumin: A component of turmeric (Curcuma longa)
    • Chainani-Wu N. (2003) Safety and anti-inflammatory activity of curcumin: a component of turmeric (Curcuma longa). J. Altern. Complement. Med. 9, 161-168.
    • (2003) J. Altern. Complement. Med. , vol.9 , pp. 161-168
    • Chainani-Wu, N.1
  • 13
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of thioflavin T: An induced circular dichroism/DFT study
    • Dzwolak W. and Pecul M. (2005) Chiral bias of amyloid fibrils revealed by the twisted conformation of thioflavin T: an induced circular dichroism/DFT study. FEBS Lett. 579, 6601-6603.
    • (2005) FEBS Lett. , vol.579 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 14
    • 27944485733 scopus 로고    scopus 로고
    • Structuring the puzzle of prion propagation
    • Eghiaian F. (2005) Structuring the puzzle of prion propagation. Curr. Opin. Struct. Biol. 15, 724-730.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 724-730
    • Eghiaian, F.1
  • 15
    • 0034718206 scopus 로고    scopus 로고
    • Approaches to discovery and characterization of inhibitors of amyloid beta-peptide polymerization
    • Findeis M. A. (2000) Approaches to discovery and characterization of inhibitors of amyloid beta-peptide polymerization. Biochim. Biophys. Acta 1502, 76-84.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 76-84
    • Findeis, M.A.1
  • 16
    • 33845192482 scopus 로고    scopus 로고
    • Congo red and protein aggregation in neurodegenerative diseases
    • Frid P., Anisimov S. V. and Popovic N. (2007) Congo red and protein aggregation in neurodegenerative diseases. Brain Res. Rev. 53, 135-160.
    • (2007) Brain Res. Rev. , vol.53 , pp. 135-160
    • Frid, P.1    Anisimov, S.V.2    Popovic, N.3
  • 18
    • 34547451145 scopus 로고    scopus 로고
    • Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model
    • Garcia-Alloza M., Borrelli L. A., Rozkalne A., Hyman B. T. and Bacskai B. J. (2007) Curcumin labels amyloid pathology in vivo, disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model. J. Neurochem. 102, 1095-1104.
    • (2007) J. Neurochem. , vol.102 , pp. 1095-1104
    • Garcia-Alloza, M.1    Borrelli, L.A.2    Rozkalne, A.3    Hyman, B.T.4    Bacskai, B.J.5
  • 19
    • 0022820831 scopus 로고
    • Fluorescence quenching method for determining equilibrium- constants for polycyclic aromatic-hydrocarbons binding to dissolved humic materials
    • Gauthier T. D., Shane E. C., Guerin W. F., Seitz W. R. and Grant C. L. (1986) Fluorescence quenching method for determining equilibrium- constants for polycyclic aromatic-hydrocarbons binding to dissolved humic materials. Environ. Sci. Technol. 20, 1162-1166.
    • (1986) Environ. Sci. Technol. , vol.20 , pp. 1162-1166
    • Gauthier, T.D.1    Shane, E.C.2    Guerin, W.F.3    Seitz, W.R.4    Grant, C.L.5
  • 20
    • 34250330794 scopus 로고    scopus 로고
    • Oligomerization of the human prion protein proceeds via a molten globule intermediate
    • Gerber R., Tahiri-Alaoui A., Hore P. J. and James W. (2007) Oligomerization of the human prion protein proceeds via a molten globule intermediate. J. Biol. Chem. 282, 6300-6307.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6300-6307
    • Gerber, R.1    Tahiri-Alaoui, A.2    Hore, P.J.3    James, W.4
  • 21
    • 9744229172 scopus 로고    scopus 로고
    • Curcumin, the active constituent of turmeric, inhibits amyloid peptide-induced cytochemokine gene expression and CCR5-mediated chemotaxis of THP-1 monocytes by modulating early growth response-1 transcription factor
    • Giri R. K., Rajagopal V. and Kalra V. K. (2004) Curcumin, the active constituent of turmeric, inhibits amyloid peptide-induced cytochemokine gene expression and CCR5-mediated chemotaxis of THP-1 monocytes by modulating early growth response-1 transcription factor. J. Neurochem. 91, 1199-1210.
    • (2004) J. Neurochem. , vol.91 , pp. 1199-1210
    • Giri, R.K.1    Rajagopal, V.2    Kalra, V.K.3
  • 22
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed beta-helices into trimers
    • Govaerts C., Wille H., Prusiner S. B. and Cohen F. E. (2004) Evidence for assembly of prions with left-handed beta-helices into trimers. Proc. Natl Acad. Sci. USA 101, 8342-8347.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 23
    • 34848854771 scopus 로고    scopus 로고
    • MD-2 as the target of curcumin in the inhibition of response to LPS
    • Gradisar H., Keber M. M., Pristovsek P. and Jerala R. (2007) MD-2 as the target of curcumin in the inhibition of response to LPS. J. Leukoc. Biol. 82, 968-974.
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 968-974
    • Gradisar, H.1    Keber, M.M.2    Pristovsek, P.3    Jerala, R.4
  • 25
    • 27144513779 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro
    • Hirohata M., Ono K., Naiki H. and Yamada M. (2005) Non-steroidal anti-inflammatory drugs have anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro. Neuropharmacology 49, 1088-1099.
    • (2005) Neuropharmacology , vol.49 , pp. 1088-1099
    • Hirohata, M.1    Ono, K.2    Naiki, H.3    Yamada, M.4
  • 26
    • 0028970386 scopus 로고
    • Congo red prolongs the incubation period in scrapie-infected hamsters
    • Ingrosso L., Ladogana A. and Pocchiari M. (1995) Congo red prolongs the incubation period in scrapie-infected hamsters. J. Virol. 69, 506-508.
    • (1995) J. Virol. , vol.69 , pp. 506-508
    • Ingrosso, L.1    Ladogana, A.2    Pocchiari, M.3
  • 27
    • 2942672633 scopus 로고    scopus 로고
    • Amyloid imaging probes are useful for detection of prion plaques and treatment of transmissible spongiform encephalopathies
    • Ishikawa K., Doh-ura K., Kudo Y., Nishida N., Murakami-Kubo I., Ando Y., Sawada T. and Iwaki T. (2004) Amyloid imaging probes are useful for detection of prion plaques and treatment of transmissible spongiform encephalopathies. J. Gen. Virol. 85, 1785-1790.
    • (2004) J. Gen. Virol. , vol.85 , pp. 1785-1790
    • Ishikawa, K.1    Dohura, K.2    Kudo, Y.3    Nishida, N.4    Murakami-Kubo, I.5    Ando, Y.6    Sawada, T.7    Iwaki, T.8
  • 28
    • 17344375337 scopus 로고    scopus 로고
    • Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form
    • Jansen K., Schafer O., Birkmann E., Post K., Serban H., Prusiner S. B. and Riesner D. (2001) Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form. Biol. Chem. 382, 683-691.
    • (2001) Biol. Chem. , vol.382 , pp. 683-691
    • Jansen, K.1    Schafer, O.2    Birkmann, E.3    Post, K.4    Serban, H.5    Prusiner, S.B.6    Riesner, D.7
  • 29
    • 33749533244 scopus 로고    scopus 로고
    • Inhibitory effect of curcumin on nitric oxide production from lipopolysaccharide- activated primary microglia
    • Jung K. K., Lee H. S., Cho J. Y., Shin W. C., Rhee M. H., Kim T. G., Kang J. H., Kim S. H., Hong S. and Kang S. Y. (2006) Inhibitory effect of curcumin on nitric oxide production from lipopolysaccharide- activated primary microglia. Life Sci. 79, 2022-2031.
    • (2006) Life Sci. , vol.79 , pp. 2022-2031
    • Jung, K.K.1    Lee, H.S.2    Cho, J.Y.3    Shin, W.C.4    Rhee, M.H.5    Kim, T.G.6    Kang, J.H.7    Kim, S.H.8    Hong, S.9    Kang, S.Y.10
  • 30
    • 1842783105 scopus 로고    scopus 로고
    • Curcumin suppresses lipopolysaccharide-induced cyclooxygenase-2 expression by inhibiting activator protein 1 and nuclear factor jb bindings in BV2 microglial cells
    • Kang G., Kong P. J., Yuh Y. J., Lim S. Y., Yim S. V., Chun W. and Kim S. S. (2004) Curcumin suppresses lipopolysaccharide-induced cyclooxygenase-2 expression by inhibiting activator protein 1 and nuclear factor jb bindings in BV2 microglial cells. J. Pharmacol. Sci. 94, 325-328.
    • (2004) J. Pharmacol. Sci. , vol.94 , pp. 325-328
    • Kang, G.1    Kong, P.J.2    Yuh, Y.J.3    Lim, S.Y.4    Yim, S.V.5    Chun, W.6    Kim, S.S.7
  • 31
    • 0345016388 scopus 로고    scopus 로고
    • Curcumin suppresses Janus kinase-STAT inflammatory signaling through activation of Src homology 2 domain-containing tyrosine phosphatase 2 in brain microglia
    • Kim H. Y., Park E. J., Joe E. H. and Jou I. (2003) Curcumin suppresses Janus kinase-STAT inflammatory signaling through activation of Src homology 2 domain-containing tyrosine phosphatase 2 in brain microglia. J. Immunol. 171, 6072-6079.
    • (2003) J. Immunol. , vol.171 , pp. 6072-6079
    • Kim, H.Y.1    Park, E.J.2    Joe, E.H.3    Jou, I.4
  • 32
    • 20444402292 scopus 로고    scopus 로고
    • Curcumin inhibits immunostimulatory function of dendritic cells: MAPKs and translocation of NF-kappa B as potential targets
    • Kim G. Y., Kim K. H., Lee S. H., Yoon M. S., Lee H. J., Moon D. O., Lee C. M., Ahn S. C., Park Y. C. and Park Y. M. (2005) Curcumin inhibits immunostimulatory function of dendritic cells: MAPKs and translocation of NF-kappa B as potential targets. J. Immunol. 174, 8116-8124.
    • (2005) J. Immunol. , vol.174 , pp. 8116-8124
    • Kim, G.Y.1    Kim, K.H.2    Lee, S.H.3    Yoon, M.S.4    Lee, H.J.5    Moon, D.O.6    Lee, C.M.7    Ahn, S.C.8    Park, Y.C.9    Park, Y.M.10
  • 33
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk W. E., Jacob R. F. and Mason R. P. (1999) Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol. 309, 285-305.
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 34
    • 10744232413 scopus 로고    scopus 로고
    • Imaging brain amyloid in Alzheimer's disease with Pittsburgh compound-B
    • Klunk W. E., Engler H., Nordberg A. et al. (2004) Imaging brain amyloid in Alzheimer's disease with Pittsburgh compound-B. Ann. Neurol. 55, 306-319.
    • (2004) Ann. Neurol. , vol.55 , pp. 306-319
    • Klunk, W.E.1    Engler, H.2    Nordberg, A.3
  • 35
    • 23944480892 scopus 로고    scopus 로고
    • Comparison of protease-resistant prion protein inhibitors in cell cultures infected with two strains of mouse and sheep scrapie
    • Kocisko D. A., Engel A. L., Harbuck K., Arnold K. M., Olsen E. A., Raymond L. D., Vilette D. and Caughey B. (2005) Comparison of protease-resistant prion protein inhibitors in cell cultures infected with two strains of mouse and sheep scrapie. Neurosci. Lett. 388, 106-111.
    • (2005) Neurosci. Lett. , vol.388 , pp. 106-111
    • Kocisko, D.A.1    Engel, A.L.2    Harbuck, K.3    Arnold, K.M.4    Olsen, E.A.5    Raymond, L.D.6    Vilette, D.7    Caughey, B.8
  • 36
    • 0036860355 scopus 로고    scopus 로고
    • Amyloid binding ligands as Alzheimer's disease therapies
    • Lee V. M. (2002) Amyloid binding ligands as Alzheimer's disease therapies. Neurobiol. Aging 23, 1039-1042.
    • (2002) Neurobiol. Aging , vol.23 , pp. 1039-1042
    • Lee, V.M.1
  • 37
    • 28544441271 scopus 로고    scopus 로고
    • Mechanism of A beta(1-40) fibril-induced fluorescence of (trans,trans)-1-bromo-2,5-bis(4-hydroxystyryl)benzene (K114)
    • LeVine H. III (2005a) Mechanism of A beta(1-40) fibril-induced fluorescence of (trans,trans)-1-bromo-2,5-bis(4-hydroxystyryl)benzene (K114). Biochemistry 44, 15937-15943.
    • (2005) Biochemistry , vol.44 , pp. 15937-15943
    • Levine III, H.1
  • 38
    • 21244490033 scopus 로고    scopus 로고
    • Multiple ligand binding sites on A beta(1-40) fibrils
    • LeVine H. III (2005b) Multiple ligand binding sites on A beta(1-40) fibrils. Amyloid 12, 5-14.
    • (2005) Amyloid , vol.12 , pp. 5-14
    • Levine III, H.1
  • 39
    • 0035503597 scopus 로고    scopus 로고
    • The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse
    • Lim G. P., Chu T., Yang F., Beech W., Frautschy S. A. and Cole G. M. (2001) The curry spice curcumin reduces oxidative damage and amyloid pathology in an Alzheimer transgenic mouse. J. Neurosci. 21, 8370-8377.
    • (2001) J. Neurosci. , vol.21 , pp. 8370-8377
    • Lim, G.P.1    Chu, T.2    Yang, F.3    Beech, W.4    Frautschy, S.A.5    Cole, G.M.6
  • 40
    • 33644958800 scopus 로고    scopus 로고
    • Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions
    • Luhrs T., Zahn R. and Wuthrich K. (2006) Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions. J. Mol. Biol. 357, 833-841.
    • (2006) J. Mol. Biol. , vol.357 , pp. 833-841
    • Luhrs, T.1    Zahn, R.2    Wuthrich, K.3
  • 42
    • 0033961817 scopus 로고    scopus 로고
    • Effect of Congo red on wild-type and mutated prion proteins in cultured cells
    • Milhavet O., Mange A., Casanova D. and Lehmann S. (2000) Effect of Congo red on wild-type and mutated prion proteins in cultured cells. J. Neurochem. 74, 222-230.
    • (2000) J. Neurochem. , vol.74 , pp. 222-230
    • Milhavet, O.1    Mange, A.2    Casanova, D.3    Lehmann, S.4
  • 43
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V., Bocharova O. V., Bronstein I. and Baskakov I. V. (2006a) Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 281, 13828-13836.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 44
    • 33744954409 scopus 로고    scopus 로고
    • Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay
    • Novitskaya V., Makarava N., Bellon A., Bocharova O. V., Bronstein I. B., Williamson R. A. and Baskakov I. V. (2006b) Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J. Biol. Chem. 281, 15536-15545.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15536-15545
    • Novitskaya, V.1    Makarava, N.2    Bellon, A.3    Bocharova, O.V.4    Bronstein, I.B.5    Williamson, R.A.6    Baskakov, I.V.7
  • 45
    • 1542364225 scopus 로고    scopus 로고
    • Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro
    • Ono K., Hasegawa K., Naiki H. and Yamada M. (2004) Curcumin has potent anti-amyloidogenic effects for Alzheimer's beta-amyloid fibrils in vitro. J. Neurosci. Res. 75, 742-750.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 742-750
    • Ono, K.1    Hasegawa, K.2    Naiki, H.3    Yamada, M.4
  • 47
    • 33749265462 scopus 로고    scopus 로고
    • Curcumin and dehydrozingerone derivatives: Synthesis, radiolabeling, and evaluation for beta-amyloid plaque imaging
    • Ryu E. K., Choe Y. S., Lee K. H., Choi Y. and Kim B. T. (2006) Curcumin and dehydrozingerone derivatives: synthesis, radiolabeling, and evaluation for beta-amyloid plaque imaging. J. Med. Chem. 49, 6111-6119.
    • (2006) J. Med. Chem. , vol.49 , pp. 6111-6119
    • Ryu, E.K.1    Choe, Y.S.2    Lee, K.H.3    Choi, Y.4    Kim, B.T.5
  • 48
    • 84903202261 scopus 로고    scopus 로고
    • Localization of neurofibrillary tangles and beta-amyloid plaques in the brains of living patients with Alzheimer disease
    • Shoghi-Jadid K., Small G. W., Agdeppa E. D. et al. (2002) Localization of neurofibrillary tangles and beta-amyloid plaques in the brains of living patients with Alzheimer disease. Am. J. Geriatr. Psychiatry 10, 24-35.
    • (2002) Am. J. Geriatr. Psychiatry , vol.10 , pp. 24-35
    • Shoghi-Jadid, K.1    Small, G.W.2    Agdeppa, E.D.3
  • 50
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • Stefani M. (2004) Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739, 5-25.
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 51
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • Swietnicki W., Morillas M., Chen S. G., Gambetti P. and Surewicz W. K. (2000) Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39, 424-431.
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 52
    • 0029012098 scopus 로고
    • Interpretation of binding curves obtained with high receptor concentrations: Practical aid for computer analysis
    • Swillens S. (1995) Interpretation of binding curves obtained with high receptor concentrations: practical aid for computer analysis. Mol. Pharmacol. 47, 1197-1203.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 1197-1203
    • Swillens, S.1
  • 54
    • 0026451628 scopus 로고
    • Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences
    • Turnell W. G. and Finch J. T. (1992) Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences. J. Mol. Biol. 227, 1205-1223.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1205-1223
    • Turnell, W.G.1    Finch, J.T.2
  • 58
    • 0030926135 scopus 로고    scopus 로고
    • Curcumin, a compound with antiinflammatory and anti-oxidant properties, down-regulates chemokine expression in bone marrow stromal cells
    • Xu Y. X., Pindolia K. R., Janakiraman N., Noth C. J., Chapman R. A. and Gautam S. C. (1997) Curcumin, a compound with antiinflammatory and anti-oxidant properties, down-regulates chemokine expression in bone marrow stromal cells. Exp. Hematol. 25, 413-422.
    • (1997) Exp. Hematol. , vol.25 , pp. 413-422
    • Xu, Y.X.1    Pindolia, K.R.2    Janakiraman, N.3    Noth, C.J.4    Chapman, R.A.5    Gautam, S.C.6
  • 59
    • 20044370990 scopus 로고    scopus 로고
    • Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo
    • Yang F., Lim G. P., Begum A. N. et al. (2005) Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J. Biol. Chem. 280, 5892-5901.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5892-5901
    • Yang, F.1    Lim, G.P.2    Begum, A.N.3
  • 60
    • 0030810150 scopus 로고    scopus 로고
    • Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding
    • Zahn R., von Schroetter C. and Wuthrich K. (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett. 417, 400-404.
    • (1997) FEBS Lett. , vol.417 , pp. 400-404
    • Zahn, R.1    Von Schroetter, C.2    Wuthrich, K.3
  • 61
    • 0035842881 scopus 로고    scopus 로고
    • Induced chirality upon crocetin binding to human serum albumin: Origin and nature
    • Zsila F., Bikadi Z. and Simonyi M. (2001) Induced chirality upon crocetin binding to human serum albumin: origin and nature. Tetrahedron Asymmetry 12, 3125-3137.
    • (2001) Tetrahedron Asymmetry , vol.12 , pp. 3125-3137
    • Zsila, F.1    Bikadi, Z.2    Simonyi, M.3
  • 62
    • 0037436279 scopus 로고    scopus 로고
    • Unique, pH-dependent biphasic band shape of the visible circular dichroism of curcuminserum albumin complex
    • Zsila F., Bikadi Z. and Simonyi M. (2003a) Unique, pH-dependent biphasic band shape of the visible circular dichroism of curcuminserum albumin complex. Biochem. Biophys. Res. Commun. 301, 776-782.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 776-782
    • Zsila, F.1    Bikadi, Z.2    Simonyi, M.3
  • 63
    • 0041562528 scopus 로고    scopus 로고
    • Molecular basis of the cotton effects induced by the binding of curcumin to human serum albumin
    • Zsila F., Bikadi Z. and Simonyi M. (2003b) Molecular basis of the cotton effects induced by the binding of curcumin to human serum albumin. Tetrahedron Asymmetry 14, 2433-2444.
    • (2003) Tetrahedron Asymmetry , vol.14 , pp. 2433-2444
    • Zsila, F.1    Bikadi, Z.2    Simonyi, M.3
  • 64
    • 2542451035 scopus 로고    scopus 로고
    • Induced circular dichroism spectra reveal binding of the antiinflammatory curcumin to human alpha1-acid glycoprotein
    • Zsila F., Bikadi Z. and Simonyi M. (2004) Induced circular dichroism spectra reveal binding of the antiinflammatory curcumin to human alpha1-acid glycoprotein. Bioorg. Med. Chem. 12, 3239-3245.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 3239-3245
    • Zsila, F.1    Bikadi, Z.2    Simonyi, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.