-
1
-
-
0035066332
-
Alzheimer’s disease: genes, proteins, and therapy
-
D.J. Selkoe Alzheimer’s disease: genes, proteins, and therapy Physiol. Rev. 81 2001 741 766
-
(2001)
Physiol. Rev.
, vol.81
, pp. 741-766
-
-
Selkoe, D.J.1
-
3
-
-
0027258525
-
The carboxy terminus of the β-amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer’s disease
-
J.T. Jarrett E.P. Berger P.T. Lansbury Jr The carboxy terminus of the β-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, P.T.3
-
4
-
-
0030908095
-
Models of amyloid seeding in Alzheimer’s disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
-
J.D. Harper P.T. Lansbury Jr Models of amyloid seeding in Alzheimer’s disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 385 407
-
(1997)
Annu. Rev. Biochem.
, vol.66
, pp. 385-407
-
-
Harper, J.D.1
Lansbury, P.T.2
-
5
-
-
0026597063
-
Alzheimer’s disease: the amyloid cascade hypothesis
-
J.A. Hardy G.A. Higgins Alzheimer’s disease: the amyloid cascade hypothesis Science 256 1992 184 185
-
(1992)
Science
, vol.256
, pp. 184-185
-
-
Hardy, J.A.1
Higgins, G.A.2
-
6
-
-
0032516821
-
Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid β-peptides
-
T. Tomita S. Tokuhiro T. Hashimoto K. Aiba T.C. Saido K. Maruyama T. Iwatsubo Molecular dissection of domains in mutant presenilin 2 that mediate overproduction of amyloidogenic forms of amyloid β-peptides J. Biol. Chem. 273 1998 21153 21160
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 21153-21160
-
-
Tomita, T.1
Tokuhiro, S.2
Hashimoto, T.3
Aiba, K.4
Saido, T.C.5
Maruyama, K.6
Iwatsubo, T.7
-
7
-
-
0037470192
-
Familial Alzheimer disease-linked presenilin 1 variants enhanced production of both Aβ1–40 and Aβ1–42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of “γ-secretase”
-
T. Ikeuchi G. Dolios S.-H. Kim R. Wang S.S. Sisodia Familial Alzheimer disease-linked presenilin 1 variants enhanced production of both Aβ1–40 and Aβ1–42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of “γ-secretase” J. Biol. Chem. 278 2003 7010 7018
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 7010-7018
-
-
Ikeuchi, T.1
Dolios, G.2
Kim, S.-H.3
Wang, R.4
Sisodia, S.S.5
-
8
-
-
0031742418
-
Flemish and Dutch mutations in amyloid β precursor protein have different effects on amyloid β secretion
-
C. De Jonghe C. Zehr D. Yager C.-M. Prada S. Younkin L. Hendriks Flemish and Dutch mutations in amyloid β precursor protein have different effects on amyloid β secretion Neurobiol. Dis. 5 1998 281 286
-
(1998)
Neurobiol. Dis.
, vol.5
, pp. 281-286
-
-
De Jonghe, C.1
Zehr, C.2
Yager, D.3
Prada, C.-M.4
Younkin, S.5
Hendriks, L.6
-
9
-
-
33746572249
-
Increased BACE1 maturation contributes to the pathogenesis of Alzheimer’s disease in Down syndrome
-
X. Sun Y. Tong H. Qing C.-H. Chen W. Song Increased BACE1 maturation contributes to the pathogenesis of Alzheimer’s disease in Down syndrome FASEB J. 20 2006 1361 1368
-
(2006)
FASEB J.
, vol.20
, pp. 1361-1368
-
-
Sun, X.1
Tong, Y.2
Qing, H.3
Chen, C.-H.4
Song, W.5
-
11
-
-
1842610580
-
Down syndrome and β-amyloid deposition
-
E. Head I.T. Lott Down syndrome and β-amyloid deposition Curr. Opin. Neurol. 17 2004 95 100
-
(2004)
Curr. Opin. Neurol.
, vol.17
, pp. 95-100
-
-
Head, E.1
Lott, I.T.2
-
13
-
-
0031020909
-
Amyloid precursor protein processing and Aβ42 deposition in a transgenic mouse model of Alzheimer disease
-
K. Johnson-Wood M. Lee R. Motter K. Hu G. Gordon R. Barbour Amyloid precursor protein processing and Aβ42 deposition in a transgenic mouse model of Alzheimer disease Proc. Natl Acad. Sci. USA 94 1997 1550 1555
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 1550-1555
-
-
Johnson-Wood, K.1
Lee, M.2
Motter, R.3
Hu, K.4
Gordon, G.5
Barbour, R.6
-
14
-
-
15044339964
-
Intraneural Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s disease
-
D.C. Crowther K.J. Kinghorn E. Miranda R. Page J.A. Curry F.A. Duthie Intraneural Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s disease Neuroscience 132 2005 123 135
-
(2005)
Neuroscience
, vol.132
, pp. 123-135
-
-
Crowther, D.C.1
Kinghorn, K.J.2
Miranda, E.3
Page, R.4
Curry, J.A.5
Duthie, F.A.6
-
15
-
-
0037405291
-
Gene expression analysis in a transgenic Caenorhabditis elegans Alzheimer’s disease model
-
C. Link A. Taft V. Kapulkin K. Duke S. Kim Q. Fei Gene expression analysis in a transgenic Caenorhabditis elegans Alzheimer’s disease model Neurobiol. Aging 24 2003 397 413
-
(2003)
Neurobiol. Aging
, vol.24
, pp. 397-413
-
-
Link, C.1
Taft, A.2
Kapulkin, V.3
Duke, K.4
Kim, S.5
Fei, Q.6
-
18
-
-
33750047859
-
Regulation of steady-state β-amyloid levels in the brain by neprilysin and endothelin-converting enzyme but not angiotensin-converting enzyme
-
E.A. Eckman S.K. Adams F.J. Troendle B.A. Stodola M.A. Kahn A.H. Fauq Regulation of steady-state β-amyloid levels in the brain by neprilysin and endothelin-converting enzyme but not angiotensin-converting enzyme J. Biol. Chem. 281 2006 30471 30478
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 30471-30478
-
-
Eckman, E.A.1
Adams, S.K.2
Troendle, F.J.3
Stodola, B.A.4
Kahn, M.A.5
Fauq, A.H.6
-
19
-
-
27544432457
-
Neprilysin decreases uniformly in Alzheimer’s disease and in normal aging
-
R. Russo R. Borghi W. Markesbery M. Tabaton A. Piccini Neprilysin decreases uniformly in Alzheimer’s disease and in normal aging FEBS Lett. 579 2005 6027 6030
-
(2005)
FEBS Lett.
, vol.579
, pp. 6027-6030
-
-
Russo, R.1
Borghi, R.2
Markesbery, W.3
Tabaton, M.4
Piccini, A.5
-
22
-
-
14944378094
-
Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
-
D.M. Walsh M. Townsend M.B. Podlisny G.M. Shankar J.V. Fadeeva O.E. Agnaf Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation J. Neurosci. 25 2005 2455 2462
-
(2005)
J. Neurosci.
, vol.25
, pp. 2455-2462
-
-
Walsh, D.M.1
Townsend, M.2
Podlisny, M.B.3
Shankar, G.M.4
Fadeeva, J.V.5
Agnaf, O.E.6
-
23
-
-
0037041426
-
Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo
-
D.M. Walsh I. Klyubin J.V. Fadeeva W.K. Cullen R. Anwyl M.S. Wolfe Naturally secreted oligomers of amyloid-β protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 2002 535 539
-
(2002)
Nature
, vol.416
, pp. 535-539
-
-
Walsh, D.M.1
Klyubin, I.2
Fadeeva, J.V.3
Cullen, W.K.4
Anwyl, R.5
Wolfe, M.S.6
-
24
-
-
0036308719
-
Mutations that reduce aggregation of the Alzheimer’s Aβ42 peptide: an unbiased search for the sequence determinants of Aβ amyloidogenesis
-
C. Wurth N.K. Guimard M.H. Hecht Mutations that reduce aggregation of the Alzheimer’s Aβ42 peptide: an unbiased search for the sequence determinants of Aβ amyloidogenesis J. Mol. Biol. 319 2002 1279 1290
-
(2002)
J. Mol. Biol.
, vol.319
, pp. 1279-1290
-
-
Wurth, C.1
Guimard, N.K.2
Hecht, M.H.3
-
25
-
-
33750430630
-
Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer’s Aβ42 peptide
-
W. Kim M.H. Hecht Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer’s Aβ42 peptide Proc. Natl Acad. Sci. USA 103 2006 15824 15829
-
(2006)
Proc. Natl Acad. Sci. USA
, vol.103
, pp. 15824-15829
-
-
Kim, W.1
Hecht, M.H.2
-
26
-
-
27144447811
-
Sequence determinants of enhanced amyloidogenicity of Alzheimer Aβ42 peptide relative to Aβ40
-
W. Kim M.H. Hecht Sequence determinants of enhanced amyloidogenicity of Alzheimer Aβ42 peptide relative to Aβ40 J. Biol. Chem. 280 2005 35069 35076
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 35069-35076
-
-
Kim, W.1
Hecht, M.H.2
-
28
-
-
10644284600
-
Analysis of the secondary structure of β-amyloid (Aβ42) fibrils by systematic proline replacement
-
A. Morimoto K. Irie K. Murakami Y. Masuda H. Ohigashi M. Nagao Analysis of the secondary structure of β-amyloid (Aβ42) fibrils by systematic proline replacement J. Biol. Chem. 27 2004 52781 52788
-
(2004)
J. Biol. Chem.
, vol.27
, pp. 52781-52788
-
-
Morimoto, A.1
Irie, K.2
Murakami, K.3
Masuda, Y.4
Ohigashi, H.5
Nagao, M.6
-
29
-
-
0042467550
-
Rationalization of the effects of mutations on peptide and protein aggregation rates
-
F. Chiti M. Stefani N. Taddei G. Ramponi C.M. Dobson Rationalization of the effects of mutations on peptide and protein aggregation rates Nature 424 2003 805 808
-
(2003)
Nature
, vol.424
, pp. 805-808
-
-
Chiti, F.1
Stefani, M.2
Taddei, N.3
Ramponi, G.4
Dobson, C.M.5
-
30
-
-
0036081257
-
Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer’s β-amyloid peptide compared to E22Q Dutch mutant
-
F. Massi D. Klimov D. Thirumalai J.E. Straub Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer’s β-amyloid peptide compared to E22Q Dutch mutant Protein Sci. 11 2002 1639 1647
-
(2002)
Protein Sci.
, vol.11
, pp. 1639-1647
-
-
Massi, F.1
Klimov, D.2
Thirumalai, D.3
Straub, J.E.4
-
32
-
-
33750449952
-
A high-throughput screen for compounds that inhibit aggregation of the Alzheimer’s peptide
-
W. Kim Y. Kim J. Min D. Kim Y. Chang M. Hecht A high-throughput screen for compounds that inhibit aggregation of the Alzheimer’s peptide ACS Chem. Biol. 1 2006 461 469
-
(2006)
ACS Chem. Biol.
, vol.1
, pp. 461-469
-
-
Kim, W.1
Kim, Y.2
Min, J.3
Kim, D.4
Chang, Y.5
Hecht, M.6
-
33
-
-
0027195933
-
Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer’s disease and scrapie?
-
J.T. Jarrett P.T. Lansbury Jr Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer’s disease and scrapie? Cell 73 1993 1055 1058
-
(1993)
Cell
, vol.73
, pp. 1055-1058
-
-
Jarrett, J.T.1
Lansbury, P.T.2
-
34
-
-
0027502784
-
Thioflavin T interaction with synthetic Alzheimer’s disease β-amyloid peptides: detection of amyloid aggregation in solution
-
H. Levine III Thioflavin T interaction with synthetic Alzheimer’s disease β-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
-
35
-
-
0029920991
-
Enhanced pathologic properties of Dutch-type mutant amyloid β-protein
-
J. Davis W.E. Van Nostrand Enhanced pathologic properties of Dutch-type mutant amyloid β-protein Proc. Natl Acad. Sci. USA 93 1996 2996 3000
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 2996-3000
-
-
Davis, J.1
Van Nostrand, W.E.2
-
36
-
-
30744433878
-
Experimental constraints on quaternary structure in Alzheimer’s β-amyloid fibrils
-
A.T. Petkova W.-M. Yau R. Tycko Experimental constraints on quaternary structure in Alzheimer’s β-amyloid fibrils Biochemistry 45 2006 498 512
-
(2006)
Biochemistry
, vol.45
, pp. 498-512
-
-
Petkova, A.T.1
Yau, W.-M.2
Tycko, R.3
-
37
-
-
12244249201
-
Self-propagating, molecular-level polymorphism in Alzheimer’s β-amyloid fibrils
-
A.T. Petkova R. Leapman Z. Guo W. Yau M. Mattson R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer’s β-amyloid fibrils Science 307 2005 262 265
-
(2005)
Science
, vol.307
, pp. 262-265
-
-
Petkova, A.T.1
Leapman, R.2
Guo, Z.3
Yau, W.4
Mattson, M.5
Tycko, R.6
-
40
-
-
0034598954
-
Nature disfavors sequences of alternating polar and nonpolar amino acids: implications for amyloidogenesis
-
B.M. Broome M.H. Hecht Nature disfavors sequences of alternating polar and nonpolar amino acids: implications for amyloidogenesis J. Mol. Biol. 296 2000 961 968
-
(2000)
J. Mol. Biol.
, vol.296
, pp. 961-968
-
-
Broome, B.M.1
Hecht, M.H.2
-
45
-
-
26944437967
-
Small non-fibrillar assemblies of amyloid-β protein bearing the Arctic mutation induce rapid neuritic degeneration
-
B. Whalen D.J. Selkoe D. Hartley Small non-fibrillar assemblies of amyloid-β protein bearing the Arctic mutation induce rapid neuritic degeneration Neurobiol. Dis. 20 2005 254 266
-
(2005)
Neurobiol. Dis.
, vol.20
, pp. 254-266
-
-
Whalen, B.1
Selkoe, D.J.2
Hartley, D.3
-
46
-
-
0029869449
-
An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues
-
M. Zaccolo D. Williams D. Brown E. Gherardi An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues J. Mol. Biol. 255 1996 589 603
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 589-603
-
-
Zaccolo, M.1
Williams, D.2
Brown, D.3
Gherardi, E.4
|