-
1
-
-
84931005949
-
Aβ43 is neurotoxic and primes aggregation of Aβ40 in vivo
-
Burnouf S, Gorsky MK, Dols J, Gronke S, Partridge L (2015) Aβ43 is neurotoxic and primes aggregation of Aβ40 in vivo. Acta Neuropathol 130: 35-47
-
(2015)
Acta Neuropathol
, vol.130
, pp. 35-47
-
-
Burnouf, S.1
Gorsky, M.K.2
Dols, J.3
Gronke, S.4
Partridge, L.5
-
2
-
-
0030657665
-
Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation
-
Capell A, Saffrich R, Olivo JC, Meyn L, Walter J, Grunberg J, Mathews P, Nixon R, Dotti C, Haass C (1997) Cellular expression and proteolytic processing of presenilin proteins is developmentally regulated during neuronal differentiation. J Neurochem 69: 2432-2440
-
(1997)
J Neurochem
, vol.69
, pp. 2432-2440
-
-
Capell, A.1
Saffrich, R.2
Olivo, J.C.3
Meyn, L.4
Walter, J.5
Grunberg, J.6
Mathews, P.7
Nixon, R.8
Dotti, C.9
Haass, C.10
-
3
-
-
84861194622
-
The mechanism of γ-secretase dysfunction in familial Alzheimer disease
-
Chavez-Gutierrez L, Bammens L, Benilova I, Vandersteen A, Benurwar M, Borgers M, Lismont S, Zhou L, Van Cleynenbreugel S, Esselmann H et al (2012) The mechanism of γ-secretase dysfunction in familial Alzheimer disease. EMBO J 31: 2261-2274
-
(2012)
EMBO J
, vol.31
, pp. 2261-2274
-
-
Chavez-Gutierrez, L.1
Bammens, L.2
Benilova, I.3
Vandersteen, A.4
Benurwar, M.5
Borgers, M.6
Lismont, S.7
Zhou, L.8
Van Cleynenbreugel, S.9
Esselmann, H.10
-
4
-
-
0026745610
-
Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
-
Citron M, Oltersdorf T, Haass C, McConlogue L, Hung AY, Seubert P, Vigo-Pelfrey C, Lieberburg I, Selkoe DJ (1992) Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production. Nature 360: 672-674
-
(1992)
Nature
, vol.360
, pp. 672-674
-
-
Citron, M.1
Oltersdorf, T.2
Haass, C.3
McConlogue, L.4
Hung, A.Y.5
Seubert, P.6
Vigo-Pelfrey, C.7
Lieberburg, I.8
Selkoe, D.J.9
-
5
-
-
0038664363
-
Reconstitution of γ-secretase activity
-
Edbauer D, Winkler E, Regula JT, Pesold B, Steiner H, Haass C (2003) Reconstitution of γ-secretase activity. Nat Cell Biol 5: 486-488
-
(2003)
Nat Cell Biol
, vol.5
, pp. 486-488
-
-
Edbauer, D.1
Winkler, E.2
Regula, J.T.3
Pesold, B.4
Steiner, H.5
Haass, C.6
-
6
-
-
8644276394
-
A presenilin 1 R278I mutation presenting with language impairment
-
Godbolt AK, Beck JA, Collinge J, Garrard P, Warren JD, Fox NC, Rossor MN (2004) A presenilin 1 R278I mutation presenting with language impairment. Neurology 63: 1702-1704
-
(2004)
Neurology
, vol.63
, pp. 1702-1704
-
-
Godbolt, A.K.1
Beck, J.A.2
Collinge, J.3
Garrard, P.4
Warren, J.D.5
Fox, N.C.6
Rossor, M.N.7
-
7
-
-
33847662852
-
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
-
Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat Rev Mol Cell Biol 8: 101-112
-
(2007)
Nat Rev Mol Cell Biol
, vol.8
, pp. 101-112
-
-
Haass, C.1
Selkoe, D.J.2
-
8
-
-
77954602182
-
A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of γ-secretase activity
-
Heilig EA, Xia W, Shen J, Kelleher RJ 3rd (2010) A presenilin-1 mutation identified in familial Alzheimer disease with cotton wool plaques causes a nearly complete loss of γ-secretase activity. J Biol Chem 285: 22350-22359
-
(2010)
J Biol Chem
, vol.285
, pp. 22350-22359
-
-
Heilig, E.A.1
Xia, W.2
Shen, J.3
Kelleher 3rd, R.J.4
-
9
-
-
84880442012
-
Trans-dominant negative effects of pathogenic PSEN1 mutations on γ-secretase activity and Aβ production
-
Heilig EA, Gutti U, Tai T, Shen J, Kelleher RJ 3rd (2013) Trans-dominant negative effects of pathogenic PSEN1 mutations on γ-secretase activity and Aβ production. J Neurosci 33: 11606-11617
-
(2013)
J Neurosci
, vol.33
, pp. 11606-11617
-
-
Heilig, E.A.1
Gutti, U.2
Tai, T.3
Shen, J.4
Kelleher 3rd, R.J.5
-
10
-
-
0028973637
-
Amyloid β-protein ending at Thr43 is a minor component of some diffuse plaques in the Alzheimer's disease brain, but is not found in cerebrovascular amyloid
-
Iizuka T, Shoji M, Harigaya Y, Kawarabayashi T, Watanabe M, Kanai M, Hirai S (1995) Amyloid β-protein ending at Thr43 is a minor component of some diffuse plaques in the Alzheimer's disease brain, but is not found in cerebrovascular amyloid. Brain Res 702: 275-278
-
(1995)
Brain Res
, vol.702
, pp. 275-278
-
-
Iizuka, T.1
Shoji, M.2
Harigaya, Y.3
Kawarabayashi, T.4
Watanabe, M.5
Kanai, M.6
Hirai, S.7
-
11
-
-
0030611097
-
Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F (PDAPP) transgenic mouse
-
Irizarry MC, Soriano F, McNamara M, Page KJ, Schenk D, Games D, Hyman BT (1997) Aβ deposition is associated with neuropil changes, but not with overt neuronal loss in the human amyloid precursor protein V717F (PDAPP) transgenic mouse. J Neurosci 17: 7053-7059
-
(1997)
J Neurosci
, vol.17
, pp. 7053-7059
-
-
Irizarry, M.C.1
Soriano, F.2
McNamara, M.3
Page, K.J.4
Schenk, D.5
Games, D.6
Hyman, B.T.7
-
12
-
-
84864471159
-
A mutation in APP protects against Alzheimer's disease and age-related cognitive decline
-
Jonsson T, Atwal JK, Steinberg S, Snaedal J, Jonsson PV, Bjornsson S, Stefansson H, Sulem P, Gudbjartsson D, Maloney J et al (2012) A mutation in APP protects against Alzheimer's disease and age-related cognitive decline. Nature 488: 96-99
-
(2012)
Nature
, vol.488
, pp. 96-99
-
-
Jonsson, T.1
Atwal, J.K.2
Steinberg, S.3
Snaedal, J.4
Jonsson, P.V.5
Bjornsson, S.6
Stefansson, H.7
Sulem, P.8
Gudbjartsson, D.9
Maloney, J.10
-
13
-
-
84875266748
-
Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase
-
Kretner B, Fukumori A, Kuhn PH, Perez-Revuelta BI, Lichtenthaler SF, Haass C, Steiner H (2013) Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase. J Neurochem 125: 144-156
-
(2013)
J Neurochem
, vol.125
, pp. 144-156
-
-
Kretner, B.1
Fukumori, A.2
Kuhn, P.H.3
Perez-Revuelta, B.I.4
Lichtenthaler, S.F.5
Haass, C.6
Steiner, H.7
-
14
-
-
77956392552
-
ADAM10 is the physiologically relevant, constitutive α-secretase of the amyloid precursor protein in primary neurons
-
Kuhn PH, Wang H, Dislich B, Colombo A, Zeitschel U, Ellwart JW, Kremmer E, Rossner S, Lichtenthaler SF (2010) ADAM10 is the physiologically relevant, constitutive α-secretase of the amyloid precursor protein in primary neurons. EMBO J 29: 3020-3032
-
(2010)
EMBO J
, vol.29
, pp. 3020-3032
-
-
Kuhn, P.H.1
Wang, H.2
Dislich, B.3
Colombo, A.4
Zeitschel, U.5
Ellwart, J.W.6
Kremmer, E.7
Rossner, S.8
Lichtenthaler, S.F.9
-
15
-
-
77957785420
-
Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio
-
Kuperstein I, Broersen K, Benilova I, Rozenski J, Jonckheere W, Debulpaep M, Vandersteen A, Segers-Nolten I, Van Der Werf K, Subramaniam V et al (2010) Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio. EMBO J 29: 3408-3420
-
(2010)
EMBO J
, vol.29
, pp. 3408-3420
-
-
Kuperstein, I.1
Broersen, K.2
Benilova, I.3
Rozenski, J.4
Jonckheere, W.5
Debulpaep, M.6
Vandersteen, A.7
Segers-Nolten, I.8
Van Der Werf, K.9
Subramaniam, V.10
-
16
-
-
79955663580
-
Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing
-
Lichtenthaler SF, Haass C, Steiner H (2011) Regulated intramembrane proteolysis-lessons from amyloid precursor protein processing. J Neurochem 117: 779-796
-
(2011)
J Neurochem
, vol.117
, pp. 779-796
-
-
Lichtenthaler, S.F.1
Haass, C.2
Steiner, H.3
-
17
-
-
84927713045
-
Carnosic acid attenuates apoptosis induced by amyloid-β 1-42 or 1-43 in SH-SY5Y human neuroblastoma cells
-
Meng P, Yoshida H, Tanji K, Matsumiya T, Xing F, Hayakari R, Wang L, Tsuruga K, Tanaka H, Mimura J et al (2015) Carnosic acid attenuates apoptosis induced by amyloid-β 1-42 or 1-43 in SH-SY5Y human neuroblastoma cells. Neurosci Res 94: 1-9
-
(2015)
Neurosci Res
, vol.94
, pp. 1-9
-
-
Meng, P.1
Yoshida, H.2
Tanji, K.3
Matsumiya, T.4
Xing, F.5
Hayakari, R.6
Wang, L.7
Tsuruga, K.8
Tanaka, H.9
Mimura, J.10
-
18
-
-
18444391830
-
Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production
-
Moehlmann T, Winkler E, Xia X, Edbauer D, Murrell J, Capell A, Kaether C, Zheng H, Ghetti B, Haass C et al (2002) Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production. Proc Natl Acad Sci USA 99: 8025-8030
-
(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 8025-8030
-
-
Moehlmann, T.1
Winkler, E.2
Xia, X.3
Edbauer, D.4
Murrell, J.5
Capell, A.6
Kaether, C.7
Zheng, H.8
Ghetti, B.9
Haass, C.10
-
19
-
-
21444450394
-
Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid β-peptides
-
Nakaya Y, Yamane T, Shiraishi H, Wang HQ, Matsubara E, Sato T, Dolios G, Wang R, De Strooper B, Shoji M et al (2005) Random mutagenesis of presenilin-1 identifies novel mutants exclusively generating long amyloid β-peptides. J Biol Chem 280: 19070-19077
-
(2005)
J Biol Chem
, vol.280
, pp. 19070-19077
-
-
Nakaya, Y.1
Yamane, T.2
Shiraishi, H.3
Wang, H.Q.4
Matsubara, E.5
Sato, T.6
Dolios, G.7
Wang, R.8
De Strooper, B.9
Shoji, M.10
-
20
-
-
38149013121
-
Generation of Aβ38 and Aβ42 is independently and differentially affected by FAD-associated presenilin 1 mutations and γ-secretase modulation
-
Page RM, Baumann K, Tomioka M, Perez-Revuelta BI, Fukumori A, Jacobsen H, Flohr A, Luebbers T, Ozmen L, Steiner H et al (2008) Generation of Aβ38 and Aβ42 is independently and differentially affected by FAD-associated presenilin 1 mutations and γ-secretase modulation. J Biol Chem 283: 677-683
-
(2008)
J Biol Chem
, vol.283
, pp. 677-683
-
-
Page, R.M.1
Baumann, K.2
Tomioka, M.3
Perez-Revuelta, B.I.4
Fukumori, A.5
Jacobsen, H.6
Flohr, A.7
Luebbers, T.8
Ozmen, L.9
Steiner, H.10
-
21
-
-
0034747316
-
Correlation between Aβx-40-, Aβx-42-, and Aβx-43-containing amyloid plaques and cognitive decline
-
Parvathy S, Davies P, Haroutunian V, Purohit DP, Davis KL, Mohs RC, Park H, Moran TM, Chan JY, Buxbaum JD (2001) Correlation between Aβx-40-, Aβx-42-, and Aβx-43-containing amyloid plaques and cognitive decline. Arch Neurol 58: 2025-2032
-
(2001)
Arch Neurol
, vol.58
, pp. 2025-2032
-
-
Parvathy, S.1
Davies, P.2
Haroutunian, V.3
Purohit, D.P.4
Davis, K.L.5
Mohs, R.C.6
Park, H.7
Moran, T.M.8
Chan, J.Y.9
Buxbaum, J.D.10
-
22
-
-
79960819248
-
Potent amyloidogenicity and pathogenicity of Aβ43
-
Saito T, Suemoto T, Brouwers N, Sleegers K, Funamoto S, Mihira N, Matsuba Y, Yamada K, Nilsson P, Takano J et al (2011) Potent amyloidogenicity and pathogenicity of Aβ43. Nat Neurosci 14: 1023-1032
-
(2011)
Nat Neurosci
, vol.14
, pp. 1023-1032
-
-
Saito, T.1
Suemoto, T.2
Brouwers, N.3
Sleegers, K.4
Funamoto, S.5
Mihira, N.6
Matsuba, Y.7
Yamada, K.8
Nilsson, P.9
Takano, J.10
-
23
-
-
84895544711
-
The pathogenic Aβ43 is enriched in familial and sporadic Alzheimer disease
-
Sandebring A, Welander H, Winblad B, Graff C, Tjernberg LO (2013) The pathogenic Aβ43 is enriched in familial and sporadic Alzheimer disease. PLoS One 8: e55847
-
(2013)
PLoS One
, vol.8
, pp. e55847
-
-
Sandebring, A.1
Welander, H.2
Winblad, B.3
Graff, C.4
Tjernberg, L.O.5
-
24
-
-
0034774969
-
Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch
-
Sastre M, Steiner H, Fuchs K, Capell A, Multhaup G, Condron MM, Teplow DB, Haass C (2001) Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep 2: 835-841
-
(2001)
EMBO Rep
, vol.2
, pp. 835-841
-
-
Sastre, M.1
Steiner, H.2
Fuchs, K.3
Capell, A.4
Multhaup, G.5
Condron, M.M.6
Teplow, D.B.7
Haass, C.8
-
25
-
-
11144354609
-
Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration
-
Saura CA, Choi SY, Beglopoulos V, Malkani S, Zhang D, Shankaranarayana Rao BS, Chattarji S, Kelleher RJ 3rd, Kandel ER, Duff K et al (2004) Loss of presenilin function causes impairments of memory and synaptic plasticity followed by age-dependent neurodegeneration. Neuron 42: 23-36
-
(2004)
Neuron
, vol.42
, pp. 23-36
-
-
Saura, C.A.1
Choi, S.Y.2
Beglopoulos, V.3
Malkani, S.4
Zhang, D.5
Shankaranarayana Rao, B.S.6
Chattarji, S.7
Kelleher 3rd, R.J.8
Kandel, E.R.9
Duff, K.10
-
26
-
-
16044373524
-
Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
-
Scheuner D, Eckman C, Jensen M, Song X, Citron M, Suzuki N, Bird TD, Hardy J, Hutton M, Kukull W et al (1996) Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat Med 2: 864-870
-
(1996)
Nat Med
, vol.2
, pp. 864-870
-
-
Scheuner, D.1
Eckman, C.2
Jensen, M.3
Song, X.4
Citron, M.5
Suzuki, N.6
Bird, T.D.7
Hardy, J.8
Hutton, M.9
Kukull, W.10
-
27
-
-
33846282302
-
The presenilin hypothesis of Alzheimer's disease: evidence for a loss-of-function pathogenic mechanism
-
Shen J, Kelleher RJ 3rd (2007) The presenilin hypothesis of Alzheimer's disease: evidence for a loss-of-function pathogenic mechanism. Proc Natl Acad Sci USA 104: 403-409
-
(2007)
Proc Natl Acad Sci USA
, vol.104
, pp. 403-409
-
-
Shen, J.1
Kelleher 3rd, R.J.2
-
28
-
-
34250328818
-
Pathological activity of familial Alzheimer's disease-associated mutant presenilin can be executed by six different γ-secretase complexes
-
Shirotani K, Tomioka M, Kremmer E, Haass C, Steiner H (2007) Pathological activity of familial Alzheimer's disease-associated mutant presenilin can be executed by six different γ-secretase complexes. Neurobiol Dis 27: 102-107
-
(2007)
Neurobiol Dis
, vol.27
, pp. 102-107
-
-
Shirotani, K.1
Tomioka, M.2
Kremmer, E.3
Haass, C.4
Steiner, H.5
-
29
-
-
0033583047
-
The biological and pathological function of the presenilin-1 incrementexon 9 mutation is independent of its defect to undergo proteolytic processing
-
Steiner H, Romig H, Grim MG, Philipp U, Pesold B, Citron M, Baumeister R, Haass C (1999) The biological and pathological function of the presenilin-1 incrementexon 9 mutation is independent of its defect to undergo proteolytic processing. J Biol Chem 274: 7615-7618
-
(1999)
J Biol Chem
, vol.274
, pp. 7615-7618
-
-
Steiner, H.1
Romig, H.2
Grim, M.G.3
Philipp, U.4
Pesold, B.5
Citron, M.6
Baumeister, R.7
Haass, C.8
-
30
-
-
0033778262
-
Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases
-
Steiner H, Kostka M, Romig H, Basset G, Pesold B, Hardy J, Capell A, Meyn L, Grim MG, Baumeister R et al (2000) Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases. Nat Cell Biol 2: 848-851
-
(2000)
Nat Cell Biol
, vol.2
, pp. 848-851
-
-
Steiner, H.1
Kostka, M.2
Romig, H.3
Basset, G.4
Pesold, B.5
Hardy, J.6
Capell, A.7
Meyn, L.8
Grim, M.G.9
Baumeister, R.10
-
31
-
-
78449287185
-
γ-Secretase gene mutations in familial acne inversa
-
Wang B, Yang W, Wen W, Sun J, Su B, Liu B, Ma D, Lv D, Wen Y, Qu T et al (2010) γ-Secretase gene mutations in familial acne inversa. Science 330: 1065
-
(2010)
Science
, vol.330
, pp. 1065
-
-
Wang, B.1
Yang, W.2
Wen, W.3
Sun, J.4
Su, B.5
Liu, B.6
Ma, D.7
Lv, D.8
Wen, Y.9
Qu, T.10
-
32
-
-
84858720343
-
Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's disease
-
Weggen S, Beher D (2012) Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's disease. Alzheimers Res Ther 4: 9
-
(2012)
Alzheimers Res Ther
, vol.4
, pp. 9
-
-
Weggen, S.1
Beher, D.2
-
33
-
-
67649488309
-
Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains
-
Welander H, Franberg J, Graff C, Sundstrom E, Winblad B, Tjernberg LO (2009) Aβ43 is more frequent than Aβ40 in amyloid plaque cores from Alzheimer disease brains. J Neurochem 110: 697-706
-
(2009)
J Neurochem
, vol.110
, pp. 697-706
-
-
Welander, H.1
Franberg, J.2
Graff, C.3
Sundstrom, E.4
Winblad, B.5
Tjernberg, L.O.6
-
34
-
-
0030951595
-
Improved electrophoretic separation and immunoblotting of β-amyloid (Aβ) peptides 1-40, 1-42, and 1-43
-
Wiltfang J, Smirnov A, Schnierstein B, Kelemen G, Matthies U, Klafki HW, Staufenbiel M, Huther G, Ruther E, Kornhuber J (1997) Improved electrophoretic separation and immunoblotting of β-amyloid (Aβ) peptides 1-40, 1-42, and 1-43. Electrophoresis 18: 527-532
-
(1997)
Electrophoresis
, vol.18
, pp. 527-532
-
-
Wiltfang, J.1
Smirnov, A.2
Schnierstein, B.3
Kelemen, G.4
Matthies, U.5
Klafki, H.W.6
Staufenbiel, M.7
Huther, G.8
Ruther, E.9
Kornhuber, J.10
-
35
-
-
84924262484
-
Presenilin-1 knockin mice reveal loss-of-function mechanism for familial Alzheimer's disease
-
Xia D, Watanabe H, Wu B, Lee SH, Li Y, Tsvetkov E, Bolshakov VY, Shen J, Kelleher RJ 3rd (2015) Presenilin-1 knockin mice reveal loss-of-function mechanism for familial Alzheimer's disease. Neuron 85: 967-981
-
(2015)
Neuron
, vol.85
, pp. 967-981
-
-
Xia, D.1
Watanabe, H.2
Wu, B.3
Lee, S.H.4
Li, Y.5
Tsvetkov, E.6
Bolshakov, V.Y.7
Shen, J.8
Kelleher 3rd, R.J.9
-
36
-
-
33645559774
-
The GxGD motif of presenilin contributes to catalytic function and substrate identification of γ-secretase
-
Yamasaki A, Eimer S, Okochi M, Smialowska A, Kaether C, Baumeister R, Haass C, Steiner H (2006) The GxGD motif of presenilin contributes to catalytic function and substrate identification of γ-secretase. J Neurosci 26: 3821-3828
-
(2006)
J Neurosci
, vol.26
, pp. 3821-3828
-
-
Yamasaki, A.1
Eimer, S.2
Okochi, M.3
Smialowska, A.4
Kaether, C.5
Baumeister, R.6
Haass, C.7
Steiner, H.8
-
37
-
-
84878244551
-
Aβ43 is the earliest-depositing Aβ species in APP transgenic mouse brain and is converted to Aβ41 by two active domains of ACE
-
Zou K, Liu J, Watanabe A, Hiraga S, Liu S, Tanabe C, Maeda T, Terayama Y, Takahashi S, Michikawa M et al (2013) Aβ43 is the earliest-depositing Aβ species in APP transgenic mouse brain and is converted to Aβ41 by two active domains of ACE. Am J Pathol 182: 2322-2331
-
(2013)
Am J Pathol
, vol.182
, pp. 2322-2331
-
-
Zou, K.1
Liu, J.2
Watanabe, A.3
Hiraga, S.4
Liu, S.5
Tanabe, C.6
Maeda, T.7
Terayama, Y.8
Takahashi, S.9
Michikawa, M.10
|