메뉴 건너뛰기




Volumn 335, Issue 2, 2005, Pages 501-504

Aβ-polyacrolein aggregates: Novel mechanism of plastic formation in senile plaques

Author keywords

Acrolein; Alzheimer's disease; Amyloid ; Light microscopy; Polyacrolein

Indexed keywords

AMYLOID BETA PROTEIN; ACROLEIN; AMYLOID; BIOPOLYMER; PEPTIDE; PEPTIDE FRAGMENT; PLASTIC; POLYACROLEIN; POLYMER;

EID: 23744513820     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.07.111     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 0036753272 scopus 로고    scopus 로고
    • Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death
    • D.A. Butterfield, A. Castegna, C.M. Lauderback, and J. Drake Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer's disease brain contribute to neuronal death Neurobiol. Aging 23 2002 655 664
    • (2002) Neurobiol. Aging , vol.23 , pp. 655-664
    • Butterfield, D.A.1    Castegna, A.2    Lauderback, C.M.3    Drake, J.4
  • 2
    • 0035112495 scopus 로고    scopus 로고
    • Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures
    • M.A. Lovell, C. Xie, and W.R. Markesbery Acrolein is increased in Alzheimer's disease brain and is toxic to primary hippocampal cultures Neurobiol. Aging 22 2001 187 194
    • (2001) Neurobiol. Aging , vol.22 , pp. 187-194
    • Lovell, M.A.1    Xie, C.2    Markesbery, W.R.3
  • 3
    • 0032905632 scopus 로고    scopus 로고
    • Protein-bound acrolein: A novel marker of oxidative stress in Alzheimer's disease
    • N.Y. Calingasan, K. Uchida, and G.E. Gibson Protein-bound acrolein: a novel marker of oxidative stress in Alzheimer's disease J. Neurochem. 72 1999 751 756
    • (1999) J. Neurochem. , vol.72 , pp. 751-756
    • Calingasan, N.Y.1    Uchida, K.2    Gibson, G.E.3
  • 4
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, and H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radic. Biol. Med. 11 1991 81 128
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 5
    • 0034659147 scopus 로고    scopus 로고
    • Role of reactive aldehyde in cardiovascular diseases
    • K. Uchida Role of reactive aldehyde in cardiovascular diseases Free Radic. Biol. Med. 28 2000 1685 1696
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1685-1696
    • Uchida, K.1
  • 7
    • 2942678692 scopus 로고    scopus 로고
    • Albumin-bound polyacrolein: Implications for Alzheimer's disease
    • N.W. Seidler, and G.S. Yeargans Albumin-bound polyacrolein: implications for Alzheimer's disease Biochem. Biophys. Res. Commun. 320 2004 213 217
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 213-217
    • Seidler, N.W.1    Yeargans, G.S.2
  • 8
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • J.T. Jarrett, E.P. Berger, and P.T. Lansbury Jr. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease Biochemistry 32 1993 4693 4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 10
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation
    • A.J. Modler, K. Gast, G. Lutsch, and G. Damaschun Assembly of amyloid protofibrils via critical oligomers-a novel pathway of amyloid formation J. Mol. Biol. 325 2003 135 148
    • (2003) J. Mol. Biol. , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 11
    • 0037076539 scopus 로고    scopus 로고
    • Growth of beta-amyloid (1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
    • M.R. Nichols, M.A. Moss, D.K. Reed, W.L. Lin, R. Mukhopadhyay, J.H. Hoh, and T.L. Rosenberry Growth of beta-amyloid (1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy Biochemistry 41 2002 6115 6127
    • (2002) Biochemistry , vol.41 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 12
    • 0032796425 scopus 로고    scopus 로고
    • Amyloid-beta-sheet formation at the air-water interface
    • C. Schladitz, E.P. Vieira, H. Hermel, and H. Mohwald Amyloid-beta-sheet formation at the air-water interface Biophys. J. 77 1999 3305 3310
    • (1999) Biophys. J. , vol.77 , pp. 3305-3310
    • Schladitz, C.1    Vieira, E.P.2    Hermel, H.3    Mohwald, H.4
  • 13
    • 4544353492 scopus 로고    scopus 로고
    • Adsorption of amyloid beta (1-40) peptide to phosphatidylethanolamine monolayers
    • E. Maltseva, and G. Brezesinski Adsorption of amyloid beta (1-40) peptide to phosphatidylethanolamine monolayers Chem. phys. chem. 5 2004 1185 1190
    • (2004) Chem. Phys. Chem. , vol.5 , pp. 1185-1190
    • Maltseva, E.1    Brezesinski, G.2
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 15
    • 22844445793 scopus 로고    scopus 로고
    • Imaging amyloid beta peptide oligomeric particles in solution
    • J. Dong, R.P. Apkarian, and D.G. Lynn Imaging amyloid beta peptide oligomeric particles in solution Bioorg. Med. Chem. 2005 [Epub ahead of print]
    • (2005) Bioorg. Med. Chem.
    • Dong, J.1    Apkarian, R.P.2    Lynn, D.G.3
  • 16
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta
    • S.J. Wood, B. Maleeff, T. Hart, and R. Wetzel Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta J. Mol. Biol. 256 1996 870 877
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4
  • 17
    • 0028872558 scopus 로고
    • Apolipoprotein e is a kinetic but not a thermodynamic inhibitor of amyloid formation: Implications for the pathogenesis and treatment of Alzheimer disease
    • K.C. Evans, E.P. Berger, C.G. Cho, K.H. Weisgraber, and P.T. Lansbury Jr. Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease Proc. Natl. Acad. Sci. USA 92 1995 763 767
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.P.2    Cho, C.G.3    Weisgraber, K.H.4    Lansbury Jr., P.T.5
  • 18
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of a beta 1-40: Implications for the search for a beta fibril formation inhibitors
    • C.S. Goldsbury, S. Wirtz, S.A. Muller, S. Sunderji, P. Wicki, U. Aebi, and P. Frey Studies on the in vitro assembly of a beta 1-40: implications for the search for a beta fibril formation inhibitors J. Struct. Biol. 130 2000 217 231
    • (2000) J. Struct. Biol. , vol.130 , pp. 217-231
    • Goldsbury, C.S.1    Wirtz, S.2    Muller, S.A.3    Sunderji, S.4    Wicki, P.5    Aebi, U.6    Frey, P.7
  • 19
    • 5444228433 scopus 로고    scopus 로고
    • Amyloid-like formation by self-assembly of peptidolipids in two dimensions
    • C. Li, J. Orbulescu, G. Sui, and R.M. Leblanc Amyloid-like formation by self-assembly of peptidolipids in two dimensions Langmuir 20 2004 8641 8645
    • (2004) Langmuir , vol.20 , pp. 8641-8645
    • Li, C.1    Orbulescu, J.2    Sui, G.3    Leblanc, R.M.4
  • 20
    • 0021891354 scopus 로고
    • Polyacrolein microspheres: Preparation and characteristics
    • M. Chang, G. Richards, and A. Rembaum Polyacrolein microspheres: preparation and characteristics Methods Enzymol. 112 1985 150 164
    • (1985) Methods Enzymol. , vol.112 , pp. 150-164
    • Chang, M.1    Richards, G.2    Rembaum, A.3
  • 21
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's a beta peptides and the mechanism of amyloid aggregation
    • B. Soreghan, J. Kosmoski, and C. Glabe Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation J. Biol. Chem. 269 1994 28551 28554
    • (1994) J. Biol. Chem. , vol.269 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 23
    • 0025936368 scopus 로고
    • In vitro covalent modification of serum albumin by acrolein
    • J.C. Gan, A. Oandasan, and G.A. Ansari In vitro covalent modification of serum albumin by acrolein Chemosphere 23 1991 939 947
    • (1991) Chemosphere , vol.23 , pp. 939-947
    • Gan, J.C.1    Oandasan, A.2    Ansari, G.A.3
  • 24
    • 0033621398 scopus 로고    scopus 로고
    • Aberrant protein deposition and neurological disease
    • M.D. Kaytor, and S.T. Warren Aberrant protein deposition and neurological disease J. Biol. Chem. 274 1999 37507 37510
    • (1999) J. Biol. Chem. , vol.274 , pp. 37507-37510
    • Kaytor, M.D.1    Warren, S.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.