메뉴 건너뛰기




Volumn 47, Issue 47, 2008, Pages 12254-12256

Human plasma contains cross-reactive Aβ conformer-specific IgG antibodies

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; CHROMATOGRAPHIC ANALYSIS; MONOMERS; OLIGOMERS; PLASMA (HUMAN); PLASMAS; POLYMERS;

EID: 56749153276     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801767k     Document Type: Article
Times cited : (47)

References (23)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 34248190279 scopus 로고    scopus 로고
    • Aβ oligomers: A decade of discovery
    • Walsh, D. M., and Selkoe, D. J. (2007) Aβ oligomers: A decade of discovery. J. Neurochem. 101, 1172-1184.
    • (2007) J. Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 3
    • 20444459853 scopus 로고    scopus 로고
    • Autoantibodies to redox-modified oligomeric Aβ are attenuated in the plasma of Alzheimer's disease patients
    • Moir, R. D., Tseitlin, K. A., Soscia, S., Hyman, B. T., Irizarry, M. C., and Tanzi, R. E. (2005) Autoantibodies to redox-modified oligomeric Aβ are attenuated in the plasma of Alzheimer's disease patients. J. Biol. Chem. 280, 17458-17463.
    • (2005) J. Biol. Chem , vol.280 , pp. 17458-17463
    • Moir, R.D.1    Tseitlin, K.A.2    Soscia, S.3    Hyman, B.T.4    Irizarry, M.C.5    Tanzi, R.E.6
  • 5
    • 33646865770 scopus 로고    scopus 로고
    • Diagnostic and therapeutic potential of amyloid-reactive IgG antibodies contained in human sera
    • O'Nuallain, B., Hrncic, R., Wall, J. S., Weiss, D. T., and Solomon, A. (2006) Diagnostic and therapeutic potential of amyloid-reactive IgG antibodies contained in human sera. J. Immunol. 176, 7071-7078.
    • (2006) J. Immunol , vol.176 , pp. 7071-7078
    • O'Nuallain, B.1    Hrncic, R.2    Wall, J.S.3    Weiss, D.T.4    Solomon, A.5
  • 6
    • 33746419618 scopus 로고    scopus 로고
    • Intravenous immunoglobulin enhances the clearance of fibrillar amyloid-β peptide
    • Istrin, G., Bosis, E., and Solomon, B. (2006) Intravenous immunoglobulin enhances the clearance of fibrillar amyloid-β peptide. J. Neurosci. Res. 84, 434-444.
    • (2006) J. Neurosci. Res , vol.84 , pp. 434-444
    • Istrin, G.1    Bosis, E.2    Solomon, B.3
  • 7
    • 0036085702 scopus 로고    scopus 로고
    • Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals
    • Weksler, M. E., Relkin, N., Turkenich, R., LaRusse, S., Zhou, L., and Szabo, P. (2002) Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals. Exp. Gerontol. 37, 943-948.
    • (2002) Exp. Gerontol , vol.37 , pp. 943-948
    • Weksler, M.E.1    Relkin, N.2    Turkenich, R.3    LaRusse, S.4    Zhou, L.5    Szabo, P.6
  • 12
    • 0023678692 scopus 로고
    • Immunoassays with time-resolved fluorescence spectroscopy: Principles and applications
    • Diamandis, E. P. (1988) Immunoassays with time-resolved fluorescence spectroscopy: Principles and applications. Clin. Biochem. 21, 139-150.
    • (1988) Clin. Biochem , vol.21 , pp. 139-150
    • Diamandis, E.P.1
  • 13
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4
    • Wood, S. J., Wetzel, R., Martin, J. D., and Hurle, M. R. (1995) Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry 34, 724-730.
    • (1995) Biochemistry , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4
  • 16
    • 20444488480 scopus 로고    scopus 로고
    • Conformational changes of the amyloid β-peptide (1-40) adsorbed on solid surfaces
    • Giacomelli, C. E., and Norde, W. (2005) Conformational changes of the amyloid β-peptide (1-40) adsorbed on solid surfaces. Macromol. Biosci. 5, 401-407.
    • (2005) Macromol. Biosci , vol.5 , pp. 401-407
    • Giacomelli, C.E.1    Norde, W.2
  • 18
    • 8844257296 scopus 로고    scopus 로고
    • Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
    • Dumoulin, M., and Dobson, C. M. (2004) Probing the origins, diagnosis and treatment of amyloid diseases using antibodies. Biochimie 86, 589-600.
    • (2004) Biochimie , vol.86 , pp. 589-600
    • Dumoulin, M.1    Dobson, C.M.2
  • 19
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • Glabe, C. G. (2004) Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem. Sci. 29, 542-547.
    • (2004) Trends Biochem. Sci , vol.29 , pp. 542-547
    • Glabe, C.G.1
  • 20
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson, J. S., and Richardson, D. C. (2002) Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. U.S.A. 99, 2754-2759.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 21
    • 0242695726 scopus 로고    scopus 로고
    • Senile amyloidoses-diseases of increasing importance
    • Enqvist, S., Peng, S., Persson, A., and Westermark, P. (2003) Senile amyloidoses-diseases of increasing importance. Acta Histochem. 105, 377-378.
    • (2003) Acta Histochem , vol.105 , pp. 377-378
    • Enqvist, S.1    Peng, S.2    Persson, A.3    Westermark, P.4
  • 22
    • 34047234694 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing
    • Pearce, F. G., Mackintosh, S. H., and Gerrard, J. A. (2007) Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing. J. Agric. Food Chem. 55, 318-322.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 318-322
    • Pearce, F.G.1    Mackintosh, S.H.2    Gerrard, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.