-
1
-
-
7044220336
-
Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches
-
J. Tsai, J. Grutzendler, K. Duff, and W.-B. Gan Fibrillar amyloid deposition leads to local synaptic abnormalities and breakage of neuronal branches Nat. Neurol. 7 2004 1181 1183
-
(2004)
Nat. Neurol.
, vol.7
, pp. 1181-1183
-
-
Tsai, J.1
Grutzendler, J.2
Duff, K.3
Gan, W.-B.4
-
2
-
-
0029902166
-
Evidence for neuronal oxidative damage in Alzheimer's disease
-
P.F. Good, P. Werner, A. Hsu, C. Olanow, and D.P. Perl Evidence for neuronal oxidative damage in Alzheimer's disease Am. J. Pathol. 149 1996 21 27
-
(1996)
Am. J. Pathol.
, vol.149
, pp. 21-27
-
-
Good, P.F.1
Werner, P.2
Hsu, A.3
Olanow, C.4
Perl, D.P.5
-
3
-
-
0346106076
-
Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence
-
J. Dong, C.S. Atwood, V.E. Anderson, S.L. Siedlak, M.A. Smith, G. Perry, and P.R. Carey Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence Biochemistry 42 2003 2768 2773
-
(2003)
Biochemistry
, vol.42
, pp. 2768-2773
-
-
Dong, J.1
Atwood, C.S.2
Anderson, V.E.3
Siedlak, S.L.4
Smith, M.A.5
Perry, G.6
Carey, P.R.7
-
4
-
-
0030885482
-
Iron accumulation in Alzheimer's disease is a source of redox-generated free radicals
-
M.A. Smith, P.L.R. Harris, L.M. Sayre, and G. Perry Iron accumulation in Alzheimer's disease is a source of redox-generated free radicals Proc. Natl. Acad. Sci. USA 94 1997 9866 9868
-
(1997)
Proc. Natl. Acad. Sci. USA
, vol.94
, pp. 9866-9868
-
-
Smith, M.A.1
Harris, P.L.R.2
Sayre, L.M.3
Perry, G.4
-
5
-
-
0032011905
-
A method based on ICP-MS for the analysis of Alzheimer's amyloid plaques
-
D. Beauchemin, and R. Kisilevsky A method based on ICP-MS for the analysis of Alzheimer's amyloid plaques Anal. Chem. 70 1998 1026 1029
-
(1998)
Anal. Chem.
, vol.70
, pp. 1026-1029
-
-
Beauchemin, D.1
Kisilevsky, R.2
-
6
-
-
0033964859
-
In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: A central role for bound transition metals
-
L.M. Sayre, G. Perry, P.L.R. Harris, Y. Liu, K.A. Schubert, and M.A. Smith In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals J. Neurochem. 74 2000 270 279
-
(2000)
J. Neurochem.
, vol.74
, pp. 270-279
-
-
Sayre, L.M.1
Perry, G.2
Harris, P.L.R.3
Liu, Y.4
Schubert, K.A.5
Smith, M.A.6
-
7
-
-
18344414746
-
The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction
-
X. Huang, C.S. Atwood, M.A. Hartshorn, G. Multhaup, L.E. Goldstein, R.C. Scarpa, M.P. Cuajungco, D.N. Gray, J. Lim, R.D. Moir, R.E. Tanzi, and A.I. Bush The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction Biochemistry 38 1999 7609 7616
-
(1999)
Biochemistry
, vol.38
, pp. 7609-7616
-
-
Huang, X.1
Atwood, C.S.2
Hartshorn, M.A.3
Multhaup, G.4
Goldstein, L.E.5
Scarpa, R.C.6
Cuajungco, M.P.7
Gray, D.N.8
Lim, J.9
Moir, R.D.10
Tanzi, R.E.11
Bush, A.I.12
-
8
-
-
0035865905
-
Redox-active iron mediates amyloid-β toxicity
-
C.A. Rottkamp, A.K. Raina, X. Zhu, E. Gaier, A.I. Bush, C.S. Atwood, M. Chevion, G. Perry, and M.A. Smith Redox-active iron mediates amyloid-β toxicity Free Radic. Biol. Med. 30 2001 447 450
-
(2001)
Free Radic. Biol. Med.
, vol.30
, pp. 447-450
-
-
Rottkamp, C.A.1
Raina, A.K.2
Zhu, X.3
Gaier, E.4
Bush, A.I.5
Atwood, C.S.6
Chevion, M.7
Perry, G.8
Smith, M.A.9
-
9
-
-
0034973708
-
The relationship between the aggregational state of the amyloid-β peptides and free radical generation by the peptides
-
A. Monji, H. Utsumi, T. Ueda, T. Imoto, I. Yoshida, S. Hashioka, K.-I. Tashiro, and N. Tashiro The relationship between the aggregational state of the amyloid-β peptides and free radical generation by the peptides J. Neurochem. 77 2001 1425 1432
-
(2001)
J. Neurochem.
, vol.77
, pp. 1425-1432
-
-
Monji, A.1
Utsumi, H.2
Ueda, T.3
Imoto, T.4
Yoshida, I.5
Hashioka, S.6
Tashiro, K.-I.7
Tashiro, N.8
-
11
-
-
0031912255
-
Mechanisms underlying the aluminum-induced potentiation of the pro-oxidant properties of transition metals
-
S.C. Bondy, S.X. Guo-Ross, and J. Pien Mechanisms underlying the aluminum-induced potentiation of the pro-oxidant properties of transition metals Neurotoxicology 19 1998 65 72
-
(1998)
Neurotoxicology
, vol.19
, pp. 65-72
-
-
Bondy, S.C.1
Guo-Ross, S.X.2
Pien, J.3
-
12
-
-
0032514165
-
Promotion of transition metal-induced reactive oxygen species formation by β-amyloid
-
S.C. Bondy, S.X. Guo-Ross, and A.T. Truong Promotion of transition metal-induced reactive oxygen species formation by β-amyloid Brain Res. 799 1998 91 96
-
(1998)
Brain Res.
, vol.799
, pp. 91-96
-
-
Bondy, S.C.1
Guo-Ross, S.X.2
Truong, A.T.3
-
13
-
-
0033612959
-
The stabilisation of ferrous iron by a toxic β-amyloid fragment and by an aluminum salt
-
E.Y. Yang, S.X. Guo-Ross, and S.C. Bondy The stabilisation of ferrous iron by a toxic β-amyloid fragment and by an aluminum salt Brain Res. 839 1999 221 226
-
(1999)
Brain Res.
, vol.839
, pp. 221-226
-
-
Yang, E.Y.1
Guo-Ross, S.X.2
Bondy, S.C.3
-
14
-
-
0027363215
-
Simultaneous determination of Fe(III) and Fe(II) in water solutions and tissue homogenates using desferal and 1,10-phenanthroline
-
D.Y. Yegorov, A.V. Kozlov, O.A. Azizova, and Y.A. Vladimorov Simultaneous determination of Fe(III) and Fe(II) in water solutions and tissue homogenates using desferal and 1,10-phenanthroline Free Radic. Biol. Med. 15 1993 565 574
-
(1993)
Free Radic. Biol. Med.
, vol.15
, pp. 565-574
-
-
Yegorov, D.Y.1
Kozlov, A.V.2
Azizova, O.A.3
Vladimorov, Y.A.4
-
15
-
-
0027502784
-
Thioflavine-T interaction with synthetic Alzheimer's-disease beta amyloid peptides-Detection of amyloid aggregation in solution
-
H. Levine Thioflavine-T interaction with synthetic Alzheimer's-disease beta amyloid peptides-Detection of amyloid aggregation in solution Protein Sci. 2 1993 404 410
-
(1993)
Protein Sci.
, vol.2
, pp. 404-410
-
-
Levine, H.1
-
16
-
-
0035320171
-
Promotion of formation of amyloid fibrils by aluminum adenosine triphosphate (AlATP)
-
C. Exley, and O.V. Korchazhkina Promotion of formation of amyloid fibrils by aluminum adenosine triphosphate (AlATP) J. Inorg. Biochem. 84 2001 215 224
-
(2001)
J. Inorg. Biochem.
, vol.84
, pp. 215-224
-
-
Exley, C.1
Korchazhkina, O.V.2
-
17
-
-
0041817542
-
The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations
-
P. Sengupta, K. Garai, B. Sahoo, Y. Shi, D. Callaway, and S. Maiti The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations Biochemistry 42 2003 10506 10513
-
(2003)
Biochemistry
, vol.42
, pp. 10506-10513
-
-
Sengupta, P.1
Garai, K.2
Sahoo, B.3
Shi, Y.4
Callaway, D.5
Maiti, S.6
-
18
-
-
0036468326
-
Kinetic model for Fe(II) oxidation in seawater in the absence and presence of natural organic matter
-
A.L. Rose, and T.D. Waite Kinetic model for Fe(II) oxidation in seawater in the absence and presence of natural organic matter Environ. Sci. Technol. 36 2002 433 444
-
(2002)
Environ. Sci. Technol.
, vol.36
, pp. 433-444
-
-
Rose, A.L.1
Waite, T.D.2
-
19
-
-
0348047453
-
A study on the reaction of copper complex of dioxotetraamine with superoxide ion by spectrophotometry and pulse radiolysis
-
Q.-H. Luo, J.-J. Zhang, X.-L. Hu, X.-Q. Jiang, M.-C. Shen, and F.-M. Li A study on the reaction of copper complex of dioxotetraamine with superoxide ion by spectrophotometry and pulse radiolysis Inorg. Chim. Acta 357 2004 66 74
-
(2004)
Inorg. Chim. Acta
, vol.357
, pp. 66-74
-
-
Luo, Q.-H.1
Zhang, J.-J.2
Hu, X.-L.3
Jiang, X.-Q.4
Shen, M.-C.5
Li, F.-M.6
-
20
-
-
1642481207
-
The pro-oxidant activity of aluminium
-
C. Exley The pro-oxidant activity of aluminium Free Radic. Biol. Med. 36 2004 380 387
-
(2004)
Free Radic. Biol. Med.
, vol.36
, pp. 380-387
-
-
Exley, C.1
-
21
-
-
0035914631
-
Coordination of semiquinone and superoxide radical anions to zinc ion in SOD model complexes that act as the key step in disproportionation of the radical anions
-
H. Ohtsu, and S. Fukuzumi Coordination of semiquinone and superoxide radical anions to zinc ion in SOD model complexes that act as the key step in disproportionation of the radical anions Chem. - Eur. J. 7 2001 4947 4953
-
(2001)
Chem. - Eur. J.
, vol.7
, pp. 4947-4953
-
-
Ohtsu, H.1
Fukuzumi, S.2
-
22
-
-
0033517053
-
Binding of Zn(II), Cu(II) and Fe(II) ions to Alzheimer's Aβ peptide studied by fluorescence
-
W. Garzon-Rodriguez, A.K. Yatsimirsky, and C.G. Glabe Binding of Zn(II), Cu(II) and Fe(II) ions to Alzheimer's Aβ peptide studied by fluorescence Bioorg. Med. Chem. Lett. 9 1999 2243 2248
-
(1999)
Bioorg. Med. Chem. Lett.
, vol.9
, pp. 2243-2248
-
-
Garzon-Rodriguez, W.1
Yatsimirsky, A.K.2
Glabe, C.G.3
-
23
-
-
0033515564
-
Amyloid β peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalysed oxidation of hydroxylamines to nitroxides
-
S.I. Dikalov, M.P. Vitek, K.R. Maples, and R.P. Mason Amyloid β peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalysed oxidation of hydroxylamines to nitroxides J. Biol. Chem. 274 1999 9392 9399
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 9392-9399
-
-
Dikalov, S.I.1
Vitek, M.P.2
Maples, K.R.3
Mason, R.P.4
-
24
-
-
0035874024
-
New evidence that the Alzheimer's β-amyloid peptide does not spontaneously form free radicals: An ESR study using a series of spin traps
-
S. Turnbull, B.J. Tabner, O.M.A. El-Agnaf, L.J. Twyman, and D. Allsop New evidence that the Alzheimer's β-amyloid peptide does not spontaneously form free radicals: an ESR study using a series of spin traps Free Radic. Biol. Med. 30 2001 1154 1162
-
(2001)
Free Radic. Biol. Med.
, vol.30
, pp. 1154-1162
-
-
Turnbull, S.1
Tabner, B.J.2
El-Agnaf, O.M.A.3
Twyman, L.J.4
Allsop, D.5
-
25
-
-
0034733705
-
Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc
-
M.P. Cuajungco, L.E. Goldstein, A. Nunomura, M.A. Smith, J.T. Lim, C.S. Atwood, X. Huang, Y.W. Farrag, G. Perry, and A.I. Bush Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc J. Biol. Chem. 275 2000 19439 19442
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 19439-19442
-
-
Cuajungco, M.P.1
Goldstein, L.E.2
Nunomura, A.3
Smith, M.A.4
Lim, J.T.5
Atwood, C.S.6
Huang, X.7
Farrag, Y.W.8
Perry, G.9
Bush, A.I.10
-
26
-
-
12844266117
-
The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity
-
D.A. Butterfield, and D. Boyd-Kimball The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1-42)-induced oxidative stress and neurotoxicity Biochim. Biophys. Acta 1703 2005 149 156
-
(2005)
Biochim. Biophys. Acta
, vol.1703
, pp. 149-156
-
-
Butterfield, D.A.1
Boyd-Kimball, D.2
-
27
-
-
0033794593
-
Reversible inactivation of superoxide-sensitive aconitase in Aβ1-42-treated neuronal cell lines
-
V.D. Longo, K.L. Viola, W.L. Klein, and C.E. Finch Reversible inactivation of superoxide-sensitive aconitase in Aβ1-42-treated neuronal cell lines J. Neurochem. 75 2000 1977 1985
-
(2000)
J. Neurochem.
, vol.75
, pp. 1977-1985
-
-
Longo, V.D.1
Viola, K.L.2
Klein, W.L.3
Finch, C.E.4
-
28
-
-
10944272619
-
Fibrillar amyloid-β peptides kill human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase
-
A. Jana, and K. Pahan Fibrillar amyloid-β peptides kill human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase J. Biol. Chem. 279 2004 51451 51459
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 51451-51459
-
-
Jana, A.1
Pahan, K.2
-
29
-
-
15944400016
-
Human amyloid peptides Aβ1-40 and Aβ1-42 exhibit NADH oxidase activity with copper-induced oscillations and a period length of 24 min
-
C. Markert, D.M. Morré, and D.J. Morré Human amyloid peptides Aβ1-40 and Aβ1-42 exhibit NADH oxidase activity with copper-induced oscillations and a period length of 24 min BioFactors 20 2004 221 235
-
(2004)
BioFactors
, vol.20
, pp. 221-235
-
-
Markert, C.1
Morré, D.M.2
Morré, D.J.3
-
30
-
-
14044258771
-
NADPH oxidase-derived reactive oxygen species mediate the cerebrovascular dysfunction induced by the amyloid β peptide
-
L. Park, J. Anrather, P. Zhou, K. Frys, R. Pitstick, S. Younkin, G.A. Carlson, and C. Iadecola NADPH oxidase-derived reactive oxygen species mediate the cerebrovascular dysfunction induced by the amyloid β peptide J. Neurosci. 16 2005 1769 1777
-
(2005)
J. Neurosci.
, vol.16
, pp. 1769-1777
-
-
Park, L.1
Anrather, J.2
Zhou, P.3
Frys, K.4
Pitstick, R.5
Younkin, S.6
Carlson, G.A.7
Iadecola, C.8
|