The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index; 1 of the 9 sources its claims cite were checked for support.
Aβ40 Inhibits Amyloid Deposition In Vivo
Open accessAbstract
Numerous studies have established a pivotal role for Aβ42 in Alzheimer's disease (AD) pathogenesis. In contrast, although Aβ40 is the predominant form of amyloid β (Aβ) produced and accumulates to a variable degree in the human AD brain, its role in AD pathogenesis has not been established. It has generally been assumed that an increase in Aβ40 would accelerate amyloid plaque formation in vivo. We have crossed BRI-Aβ40 mice that selectively express high levels of Aβ40 with both Tg2576 (APPswe, K670N+M671L) mice and BRI-Aβ42A mice expressing Aβ42 selectively and analyzed parenchymal and cerebrovascular Aβ deposition in the bitransgenic mice compared with their singly transgenic littermates. In the bitransgenic mice, the increased steady-state levels of Aβ40 decreased Aβ deposition by 60–90%. These results demonstrate that Aβ42 and Aβ40 have opposing effects on amyloid deposition: Aβ42 promotes amyloid deposition but Aβ40 inhibits it. In addition, increasing Aβ40 levels protected BRI-Aβ40/Tg2576 mice from the premature-death phenotype observed in Tg2576 mice. The protective properties of Aβ40 with respect to amyloid deposition suggest that strategies that preferentially target Aβ40 may actually worsen the disease course and that selective increases in Aβ40 levels may actually reduce the risk for development of AD.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
Increasing Aβ40 levels in transgenic mouse models reduced parenchymal and vascular amyloid deposition, contrary to the assumption that Aβ40 promotes plaque formation. Aβ40 directly inhibited Aβ42 aggregation in vitro and also reduced premature death in BRI-Aβ40/Tg2576 mice.
Key findings
- In BRI-Aβ40/Tg2576 mice, increased steady-state Aβ40 levels decreased Aβ deposition by 60–90%; RIPA-insoluble, formic acid-extractable Aβ40 and Aβ42 levels were reduced by 60–80% in forebrain and hindbrain, and CAA severity score and affected leptomeningeal vessels decreased by ~60 and ~30% at 15 and 20 months, respectively.
- In BRI-Aβ40/BRI-Aβ42A mice at 8 months, Aβ plaque burden, ThioS-positive cored plaques in cerebellum, and formic acid-extractable Aβ42 were significantly decreased by ~75%, despite soluble brain Aβ (Aβ40 plus Aβ42) being increased ~10-fold compared with BRI-Aβ42A littermates.
- Premature death was modulated by Aβ: BRI-Aβ40/BRI-Aβ42A mice approached 100% death by 16 months, BRI-Aβ42A/Tg2576 mice had ~50% premature death versus ~30% in Tg2576 littermates, while BRI-Aβ40/Tg2576 mice had ~10% death at 7 months.
- In vitro, adding Aβ40 to Aβ42 reduced formation of high-molecular-weight Aβ42 aggregates, leaving most Aβ42 as low-molecular-weight species.
Methods
- Hemizygous BRI-Aβ40 mice were crossed with Tg2576 (APPswe) mice and with BRI-Aβ42A or BRI-Aβ42B mice; littermates were compared across aging series (8–20 months), with n = 5–7 mice per genotype at each age group.
- Parenchymal amyloid burden and ThioS-positive cored plaques were quantified by immunohistochemistry; CAA was scored in leptomeningeal vessels; Aβ levels were measured by sandwich ELISA; APP/C99 levels by Western blot; survival by Kaplan-Meier analysis; and Aβ aggregation by nondenaturing gel assay with synthetic Aβ40/Aβ42 peptides.
- Statistical analyses used ANOVA with Holm-Sidak post hoc tests, t tests, nonparametric tests where needed, and multiple linear regression with no intercept to test additive Aβ levels.
Limitations
- The paper states that extensive premature death in BRI-Aβ40/BRI-Aβ42A mice limited rigorous pathological analyses to an 8-month time point.
- The paper states that it is difficult to completely exclude other transgene-related and genetic background effects, and that premature death rate/extent is influenced by total Aβ levels, Aβ40:Aβ42 ratio, and genetic background.
- The paper states that additional studies are needed to understand factors promoting Aβ40 accumulation within vessels and to investigate effects of increased Aβ40 on oligomer formation and behavioral abnormalities; evident from the text, the work is in mouse models and in vitro assays, with no human AD cohort or cognitive/behavioral therapeutic testing reported.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
34 Own result · 5 No full text of the sources · 4 Own interpretation · 2 Not checked yet · 1 Supported · 1 No basis given
Every source the paper cites for this claim was checked and supports it.
In the paper
“accumulates to a variable degree in the human AD brain”
- Also stated in: § Introduction · plain
“A40 does accumulate in the AD brain, but the extent of A40 accumulation relative to A42 is highly variable and is usually attributed to accumulation of A40 in cerebral vessels (Gravina et al., 1995).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Abstract
What the sources say
- Supportedcites Gravina et al., 1995 source
The paper’s opening summary reports that 18 of 27 AD brains contained increasing amounts of Aβ ending at Aβ40. It also says that widely varying amounts were deposited in the remaining AD brains, primarily in blood vessel walls. (LLM, conf=0.94)
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- Also stated in: § Introduction · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“There was a significant decrease in both the A plaque burden and number of ThioS-positive plaques in BRI-A40/Tg2576 mice compared with Tg2576 littermates ( p Ͻ 0.05).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Extensive premature death observed in BRI-A40/BRI-A42A mice limited rigorous pathological analyses to an 8 month time point (see Fig.7A).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“There was a significant decrease in both the A plaque burden and number of ThioS-positive plaques in BRI-A40/Tg2576 mice compared with Tg2576 littermates ( p Ͻ 0.05).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“BRI-A42A/Tg2576 mice had a significantly increased premature death rate compared with Tg2576 littermates ( p Ͻ 0.05).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plaincorrelational- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“A, RIPA-insoluble, FA-extractable A40 and A42 levels in the forebrain of BRI-A40/Tg2576 were significantly reduced compared with Tg2576 littermates at all ages (A40 levels at p ϭ 0.01, p Ͻ 0.001, and p Ͻ 0.001 at 11, 15, and 20 months, respectively, and A42 levels at p Ͻ 0.001 at all age).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plaincorrelational- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“There was no difference in survival rates for Tg2576 progeny from breeding with either BRI-A40 mice or BRI-A42A mice ( p ϭ 0.884), thus Tg2576 data were pooled.”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“At this age, A plaque burden, the number of ThioS-positive cored plaques in the cerebellum, and FA-fraction A42 levels were significantly decreased by ϳ75% in BRI-A40/BRI-A42A mice (Fig.4), although steady-state soluble brain A (A40 plus A42) levels were increased by ϳ10-fold in bitransgenic mice compared with BRI-A42A littermates (Fig.5D).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“At this age, A plaque burden, the number of ThioS-positive cored plaques in the cerebellum, and FA-fraction A42 levels were significantly decreased by ϳ75% in BRI-A40/BRI-A42A mice (Fig.4), although steady-state soluble brain A (A40 plus A42) levels were increased by ϳ10-fold in bitransgenic mice compared with BRI-A42A littermates (Fig.5D).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“A, RIPA-insoluble, FA-extractable A40 and A42 levels in the forebrain of BRI-A40/Tg2576 were significantly reduced compared with Tg2576 littermates at all ages (A40 levels at p ϭ 0.01, p Ͻ 0.001, and p Ͻ 0.001 at 11, 15, and 20 months, respectively, and A42 levels at p Ͻ 0.001 at all age).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plaincorrelational- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- It may state two separate claims as one. 7
- Probably not a substantial claim. 6
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Bitransgenic BRI-A40/BRI-A42A had an accelerated mortality, whereas non-Tg, single transgenic BRI-A40, and BRI-A42A mice did not show any premature death ( p Ͻ 0.01).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Although BRI-A40/Tg2576 only had 10% premature death at 7 months of age, Tg2576 mice had ϳ30% early death ( p Ͻ 0.01).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Decreased FA-A40 levels were also detected but did not reach statistical significance ( p ϭ 0.101 by rank sum test).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“After a 2 h incubation, the A42-only preparation (A40:A42 ratio; 0:1) formed very high molecular weight (HMW) aggregates (indicated by”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“When A40 was mixed with A42 (A40:A42 ratio; 0.5:1 and 1:1), A40 inhibited the formation of HMW A42 aggregates, and the vast majority of A42 remained as LMW species (indicated by 4 at the bottom of the blot).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“In vivo, A42 is the predominant form of A that accumulates in the AD brain and is essential for seeding A deposition (Younkin, 1998;Fryer and Holtzman, 2005).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Introduction
What the sources say
- Not checked — no full text of the sourcecites Younkin, 1998 source
- Not matchedcites Fryer and Holtzman, 2005
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. It may state two separate claims as one.
In the paper
“-Synuclein inhibits ␣-synuclein aggregation in mice, and mouse tau may retard human tau aggregation (Rochet et al., 2000;Hashimoto et al., 2001;Andorfer et al., 2003).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
What the sources say
- Not checked — no full text of the sourcecites Hashimoto et al., 2001 source
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
In the paper
“although A40 is the predominant form of amyloid  (A) produced”
- Also stated in: § Introduction · plain
“Sequential amyloid  precursor protein (APP) processing by -secretase and ␥-secretase produces a major A species, A1-40, and a number of minor species, including A1-42 (Steiner and Haass, 2000).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Abstract
What the sources say
- Not checked — no full text of the sourcecites Steiner and Haass, 2000 source
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
- Also stated in: § Introduction · plain
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The inhibition of amyloid deposition by A40 may have critical implications for AD therapy.”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
hedgedconditional- Asserted: passes — The authors put it forward as true.
- Checkable: fails — It may be too vague to check against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. It may be too vague to check against evidence.
- Rests on an assumption: Findings in transgenic mouse models of amyloid deposition are relevant to human Alzheimer's disease therapy.
None of the sources cited for this claim have been checked yet.
In the paper
“BRI-A42A mice initially develop amyloid deposition in the cerebellum at ϳ3 months of age, whereas forebrain pathology was consistently observed only after ϳ12 months of age(McGowan et al., 2005).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
What the sources say
- Not checked yetcites McGowan et al., 2005 source
Checked before — its earlier verdict is held back until a new check runs.
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Not checked yet
In the paper
“-Synuclein inhibits ␣-synuclein aggregation in mice, and mouse tau may retard human tau aggregation (Rochet et al., 2000;Hashimoto et al., 2001;Andorfer et al., 2003).”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Discussion
What the sources say
- Not checked — no full text of the sourcecites Andorfer et al., 2003 source
hedgedconditional- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“its role in AD pathogenesis has not been established”
§ Neurobiology of Disease A40 Inhibits Amyloid Deposition In Vivo > Abstract
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim.
The paper relies on this without support.
Findings in transgenic mouse models of amyloid deposition are relevant to human Alzheimer's disease therapy.
“The inhibition of amyloid deposition by A40 may have critical implications for AD therapy.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“By crossing BRI2-A1-40 or BRI-A1-42 transgenic mice with Tg2576 mice, we previously demonstrated that A1-40 and A42 have opposing effects on amyloid deposition (McGowan et al., 2005;Kim et al., 2007).”
From BRI2 (ITM2b) Inhibits A Deposition In Vivo (2008) · cites this paper as Kim et al., 2007
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Aβ40 is present in larger amounts in the brain, yet Aβ42 is more neurotoxic and has a higher tendency to aggregate.8–11”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [9]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Almost all previous studies investigating the effect of bifunctional compounds on the neurotoxicity of metal-Aβ species have focused on the less neurotoxic and possibly even anti-amyloidogenic Aβ40 peptide.9,97,98”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [9]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Aβ species, including the most abundant Aβ40 and more toxic Aβ42, are produced by two sequential proteolytic cleavages of amyloid precursor protein (APP) by β- and γ-secretases (Kim et al., 2007; McGowan et al., 2005).”
From Apolipoprotein E in Synaptic Plasticity and Alzheimer’s Disease: Potential Cellular and Molecular Mechanisms (2014) · cites this paper as Kim et al., 2007
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Several methods were used, including a native gel assay previously used to demonstrate that A1-40 inhibits A1-42 aggregation (Kim et al., 2007).”
From BRI2 (ITM2b) Inhibits A Deposition In Vivo (2008) · cites this paper as Kim et al., 2007
The cited source says what the claim attributes to it.
In the citing paper
“The reduction in A deposition observed in the mice expressing the rAAV1 BRI2-A1-40 transgene was consistent with our previous transgenic mice studies (Kim et al., 2007), whereas the reduction of A deposition observed in the mice expressing BRI2 was unexpected.”
From BRI2 (ITM2b) Inhibits A Deposition In Vivo (2008) · cites this paper as Kim et al., 2007
The cited source says what the claim attributes to it.
In the citing paper
“The studies with BRI2-A1-40 confirmed previous studies obtained using conventional transgenic mice expressing BRI2-A1-40 (McGowan et al., 2005;Kim et al., 2007).”
From BRI2 (ITM2b) Inhibits A Deposition In Vivo (2008) · cites this paper as Kim et al., 2007
The cited source says what the claim attributes to it.
In the citing paper
“Such high concentrations may artificially cause Aβ40 to aggregate without an Aβ42 seeding nucleus, despite the fact that Aβ40 has an anti-amyloidogenic effect in vivo (Kim et al., 2007).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Kim et al., 2007
The cited source says what the claim attributes to it.
In the citing paper
“Several recent studies suggest that Aβ40 and Aβ42 may have opposing effects on Aβ aggregation in vivo (Kim et al., 2007; McGowan et al., 2005).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Kim et al., 2007
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Self-check results appear here once an independent check has confirmed them.
Cited works that were retracted
Works this paper cites that were later retracted, from the retraction notices publishers deposit. Major when the notice came out before this paper was published.
A note, not an issue: for example, a cited work that was retracted only after this paper was published, which its authors could not have known.
In the paper
“…2003; Lombardo et al., 2003; Tsai et al., 2004), an increasing body of evidence suggests that soluble oligomeric and protofibrillar A species, such as A *56, may cause the synaptic dysfunction and memory deficits in mice (Klein et al., 2004; Cleary et al., 2005; Glabe, 2006; Lesne et al., 2006).”
Cited work 10.1038/nature04533 · retracted 2024-06-24 · notice 10.1038/s41586-024-07691-8 · this paper published 2007-01-17
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“…2003; Lombardo et al., 2003; Tsai et al., 2004), an increasing body of evidence suggests that soluble oligomeric and protofibrillar A species, such as A *56, may cause the synaptic dysfunction and memory deficits in mice (Klein et al., 2004; Cleary et al., 2005; Glabe, 2006; Lesne et al., 2006).”
BackgroundRetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210 · cited 3×
“…BRI-A 40/Tg2576 mice We crossed hemizygous BRI-A 40 mice that produce only A 40 with hemizygous APPswe (Tg2576) mice overexpressing a normal profile of human A peptides (Hsiao et al., 1996), generating offspring with nontransgenic (non-Tg), BRI-A 40, Tg2576, and BRI-A 40/Tg2576 genotypes.”
BackgroundMethodInfluentialMucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856 · cited 1×
“Finally, results from transgenic mice expressing wild-type and various mutant forms of APP also suggest that increased A 40 levels might reduce amyloid deposition (Mucke et al., 2000).”
BackgroundNatural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722 · cited 2×
“, 2004), an increasing body of evidence suggests that soluble oligomeric and protofibrillar A species, such as A *56, may cause the synaptic dysfunction and memory deficits in mice (Klein et al., 2004; Cleary et al., 2005; Glabe, 2006; Lesne et al., 2006).”
BackgroundCaughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650 · cited 3×
“In vitro, A 42 aggregates into amyloid much more rapidly than A 40 (Caughey and Lansbury, 2003).”
BackgroundA subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
Weggen, S., Eriksen, J. L., Das, P., Sagi, S. A., Wang, R., Pietrzik, C. U., Findlay, K. A., Smith, T. E., Murphy, M. P., Bulter, T., et al. (2001) · Nature · doi:10.1038/35102591 · Cited by 1,388 · cited 1×
“Our data support the strategy that selectively targeting A 42 by allosterically modulating -secretase may be preferential to nonselective inhibition of -secretase activity (Weggen et al., 2001; Eriksen et al., 2003; Lleo et al., 2004).”
MethodSelf-citationKawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 2×
“3 (anti-A 35-42 Ab) as the capture Ab for A 42, and Ab9 –HRP as the detection Ab for A 42, as described previously (Kawarabayashi et al., 2001) (n 5–7 mice per genotype at each age group).”
MethodInfluentialLeissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 725
Cited by
Sorted by citations
Items 201–300 of 361
G9a Inhibition Promotes Neuroprotection through GMFB Regulation in Alzheimer’s Disease
Bellver‐Sanchís, A., Geng, Q., Navarro, G., Ávila-López, P. A., Companys‐Alemany, J., Marsal-García, L., Larramona‐Arcas, R., Miró, L., Pérez‐Bosque, A., Ortuño‐Sahagún, D., et al. (2024) · Aging and Disease · doi:10.14336/ad.2023.0424-2 · Cited by 26
Vicente, M. C., Addo-Osafo, K., & Vossel, K. A. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1277613 · Cited by 25
Aβ-Degrading Proteases: Therapeutic Potential in Alzheimer Disease
Leissring, M. A. (2016) · CNS Drugs · doi:10.1007/s40263-016-0364-1 · Cited by 26
Maesako, M., Uemura, K., Kubota, M., Hiyoshi, K., Andō, K., Kuzuya, A., Kihara, T., Asada, M., Akiyama, H., & Kinoshita, A. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2010.12.017 · Cited by 24
Asih, P. R., Chatterjee, P., Verdile, G., Gupta, V. B., Trengove, R. D., & Martins, R. N. (2014) · Neurodegenerative Disease Management · doi:10.2217/nmt.14.29 · Cited by 24
Jung, J. I., Ran, Y., Cruz, P. E., Rosario, A. M., Ladd, T. B., Kukar, T. L., Koo, E. H., Felsenstein, K. M., & Golde, T. E. (2014) · Biochemistry · doi:10.1021/bi401521t · Cited by 22
Self-citationBate, C., & Williams, A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100528 · Cited by 23
N‐cadherin‐based adhesion enhances Aβ release and decreases Aβ42/40 ratio
Uemura, K., Lill, C. M., Banks, M., Asada, M., Aoyagi, N., Andō, K., Kubota, M., Kihara, T., Nishimoto, T., Sugimoto, H., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05760.x · Cited by 22
Ahlawat, A., Walia, V., & Garg, M. (2025) · Acta Neurologica Belgica · doi:10.1007/s13760-024-02706-7 · Cited by 26
Genetic Animal Models of Cerebral Vasculopathies
Lee, J. H., Bacskai, B. J., & Ayata, C. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394596-9.00002-0 · Cited by 21
Inhibition of Amyloid β-Induced Lipid Membrane Permeation and Amyloid β Aggregation by K162
Mrđenović, D., Zarzycki, P., Majewska, M., Pieta, I. S., Nowakowski, R., Kutner, W., Lipkowski, J., & Pięta, P. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00754 · Cited by 22
Zinc utilization by microglia in Alzheimer’s disease
Shippy, D. C., Oliai, S. F., & Ulland, T. K. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107306 · Cited by 25
Jin, Y., Li, F., Li, Z., Ikezu, T. C., O’Leary, J., Selvaraj, M., Zhu, Y., Martens, Y. A., Koga, S., Santhakumar, H., et al. (2024) · Science Advances · doi:10.1126/sciadv.adk3700 · Cited by 26
Self-citationLi, X., Yang, Z., Chen, Y., Zhang, S., Wei, G., & Zhang, L. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c01078 · Cited by 22
Ran, Y., Cruz, P. E., Ladd, T. B., Fauq, A. H., Jung, J. I., Matthews, J., Felsenstein, K. M., & Golde, T. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.512921 · Cited by 21
Self-citationAbdul‐Hay, S. O., Luo, J., Asghodom, R. T., & Thatcher, G. R. J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06353.x · Cited by 21
Levites, Y., O’Nuallain, B., Puligedda, R. D., Ondrejčák, T., Adekar, S. P., Chen, C. S., Cruz, P. E., Rosario, A. M., Macy, S. D., Mably, A. J., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5109-14.2015 · Cited by 21
Self-citationAgca, C., Klakotskaia, D., Schachtman, T. R., Chan, A. W. S., Lah, J. J., & Ağca, Y. (2016) · BMC Neuroscience · doi:10.1186/s12868-016-0281-8 · Cited by 21
Zhao, H., Huang, X., & Tong, Z. (2021) · ChemMedChem · doi:10.1002/cmdc.202100428 · Cited by 21
Cholestenoic acid, an endogenous cholesterol metabolite, is a potent γ-secretase modulator
Jung, J. I., Price, A. R., Ladd, T. B., Ran, Y., Park, H.-J., Ceballos‐Diaz, C., Smithson, L. A., Hochhaus, G., Tang, Y., Akula, R., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0021-z · Cited by 21
Self-citationAbdelhameed, N. G., Ahmed, Y. H., Yasin, N. A. E., Mahmoud, M. Y., & El-Sakhawy, M. A.-M. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00406 · Cited by 20
Kleinschmidt, M., Schoenfeld, R., Göttlich, C., Bittner, D., Metzner, J. E., Leplow, B., & Demuth, H. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-143189 · Cited by 21
Aβ42 Peptide Promotes Proliferation and Gliogenesis in Human Neural Stem Cells
Bernabeu-Zornoza, A., Coronel, R., Palmer, C., Calero, M., Martı́nez-Serrano, A., Cano, E., Zambrano, A., & Liste, I. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1355-7 · Cited by 22
MicroRNA-138 Overexpression Alters Aβ42 Levels and Behavior in Wildtype Mice
Boscher, E., Goupil, C., Petry, S., Keraudren, R., Loiselle, A., Planel, E., & Hébert, S. S. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.591138 · Cited by 21
Tong, G., Izquierdo, P., & Raashid, R. A. (2017) · The Open Neurology Journal · doi:10.2174/1874205x01711010027 · Cited by 18
Recent Mechanisms of Neurodegeneration and Photobiomodulation in the Context of Alzheimer’s Disease
Su, M., Nizamutdinov, D., Liu, H., & Huang, J. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119272 · Cited by 26
Sortilin inhibits amyloid pathology by regulating non-specific degradation of APP
Ruan, C., Liu, J., Yang, M., Saadipour, K., Zeng, Y.-Q., Liao, H., Wang, Y., Bobrovskaya, L., & Zhou, X. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.10.018 · Cited by 17
Wang, H., Yu, Y., Chen, W., Cui, Y., Luo, T., Jian, M., Jiang, X., & Qin, S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-130812 · Cited by 18
Abdul‐Hay, S. O., Edirisinghe, P. D., & Thatcher, G. R. J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06355.x · Cited by 17
Multiple effects of β-amyloid on single excitatory synaptic connections in the PFC
Wang, Y., Zhou, T. H., Zhi, Z., Barakat, A., Hlatky, L., & Querfurth, H. W. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00129 · Cited by 20
Drzezga, A. E. (2008) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-007-0697-6 · Cited by 17
Terrill, S. E., Colvin, B. A., Davenport, R. E., & Nichols, M. R. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.03.017 · Cited by 18
Jin, Z., Lu, Y., Tang, H., & Cui, H. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70472 · Cited by 24
Adebambo, K. F., & Ojoh, O. (2024) · International Journal of Alzheimer s Disease · doi:10.1155/2024/2988685 · Cited by 20
Wanngren, J., Lara, P., Öjemalm, K., Maioli, S., Moradi, N., Chen, L., Tjernberg, L. O., Lundkvist, J., Nilsson, I., & Karlström, H. (2014) · FEBS Open Bio · doi:10.1016/j.fob.2014.04.006 · Cited by 16
O-GlcNAcylation of Amyloid-β Protein Precursor by Insulin Signaling Reduces Amyloid-β Production
Kwon, O.-H., Cho, Y. Y., Kim, T., & Chung, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190060 · Cited by 16
Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly
Seither, K. M., McMahon, H. A., Singh, N., Wang, H. H., Cushman-Nick, M., Montalvo, G. L., DeGrado, W. F., & Shorter, J. (2014) · Biochemical Journal · doi:10.1042/bj20131609 · Cited by 15
Davunetide improves spatial learning and memory in Alzheimer's disease-associated rats
Zhang, J., Wei, S.-Y., Yuan, L., Kong, L., Zhang, S., Wang, Z., Wu, M., & Qi, J. (2017) · Physiology & Behavior · doi:10.1016/j.physbeh.2017.02.038 · Cited by 15
E22Q-Mutant Aβ Peptide (AβDutch) Increases Vascular but Reduces Parenchymal Aβ Deposition
Herzig, M. C., Eisele, Y. S., Staufenbiel, M., & Jucker, M. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080790 · Cited by 15
Differential effects of angiotensin II receptor blockers on Aβ generation
Liu, J., Liu, S., Tanabe, C., Maeda, T., Zou, K., & Komano, H. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.03.030 · Cited by 16
Scannevin, R. H., Chollate, S., Brennan, M. S., Snodgrass-Belt, P., Peng, H., Xu, L. S., Jung, M., Bussière, T., Arastu, M. F., Talreja, T., et al. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.12.006 · Cited by 15
An anti-CRF antibody suppresses the HPA axis and reverses stress-induced phenotypes
Futch, H. S., McFarland, K. N., Moore, B. D., Kuhn, M. Z., Giasson, B. I., Ladd, T. B., Scott, K. A., Shapiro, M. R., Nosacka, R. L., Goodwin, M. S., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20190430 · Cited by 16
Self-citationAhyayauch, H., Masserini, M., Goñi, F. M., & Alonso, A. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.112 · Cited by 15
Mutant presenilin-1 deregulated peripheral immunity exacerbates Alzheimer-like pathology
Zhu, Y., Obregon, D. F., Hou, H., Giunta, B. N., Ehrhart, J. C., Fernandez, F., Mori, T., Nikolic, W. V., Zhao, Y., Morgan, D., et al. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00962.x · Cited by 14
Efficient four‐drug cocktail therapy targeting amyloid‐β peptide for Alzheimer's disease
Asai, M., Iwata, N., Tomita, T., Iwatsubo, T., Ishiura, S., Saido, T. C., & Maruyama, K. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22503 · Cited by 15
Downey, M. A., Giammona, M. J., Lang, C. A., Buratto, S. K., Singh, A. K., & Bowers, M. T. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-1975-1 · Cited by 15
Dutta, M. S., & Basu, S. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1711192 · Cited by 15
Qiu, Q., Jia, L., Wang, Q., Zhao, L., Jin, H., Li, T., Quan, M., Xu, L., Li, B., Li, Y., et al. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.05.018 · Cited by 13
Chan, H. H., Koh, R. Y., Lim, C. L., & Leong, C. O. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191023102422 · Cited by 15
Griñán‐Ferré, C., Jarné‐Ferrer, J., Bellver‐Sanchís, A., Codony, S., Puigoriol‐Illamola, D., Sanfeliu, C., Oh, Y., Lee, S., Vázquez, S., & Pallàs, M. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14511 · Cited by 14
Zhou, A. L., Swaminathan, S. K., Salian, V. S., Wang, L., Curran, G. L., Min, H.-K. P., Lowe, V. J., & Kandimalla, K. K. (2024) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c00784 · Cited by 12
Nasello, M., Schirò, G., Crapanzano, F., & Balistreri, C. R. (2017) · Rejuvenation Research · doi:10.1089/rej.2017.1946 · Cited by 12
Age-Dependent Changes in the Plasma and Brain Pharmacokinetics of Amyloid-β Peptides and Insulin
Zhou, A. L., Sharda, N., Sarma, V., Ahlschwede, K. M., Curran, G. L., Tang, X., Poduslo, J. F., Kalari, K. R., Lowe, V. J., & Kandimalla, K. K. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215128 · Cited by 12
Dutta, M., & Mattaparthi, V. S. K. (2017) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2017.1296783 · Cited by 11
Allosteric Modulators of Potential Targets Related to Alzheimer's Disease: a Review
Silva, G. M., Barcelos, M. P., Poiani, J. G. C., Hage-Melim, L. I. D. S., & da Silva, C. H. T. D. P. (2019) · ChemMedChem · doi:10.1002/cmdc.201900299 · Cited by 12
Ma, W., Chen, A.-F., Xie, X., & Huang, Y. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108342 · Cited by 12
Simões, J. L. B., Sobierai, L. D., Leal, I. F., dos Santos, M. V. R., Coiado, J. V., & Bagatini, M. D. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.12.007 · Cited by 11
Wild type but not mutant APP is involved in protective adaptive responses against oxidants
Cenini, G., Maccarinelli, G., Lanni, C., Bonini, S. A., Ferrari‐Toninelli, G., Govoni, S. M., Racchi, M., Butterfield, D. A., Memo, M., & Uberti, D. L. (2010) · Amino Acids · doi:10.1007/s00726-009-0438-1 · Cited by 11
Upregulation of endocytic protein expression in the Alzheimer’s disease male human brain
Alsaqati, M., Thomas, R. S., & Kidd, E. J. (2023) · Aging Brain · doi:10.1016/j.nbas.2023.100084 · Cited by 10
SAR investigations on a novel class of gamma-secretase modulators based on a unique scaffold
Austin, W., Hubbs, J. L., Fuller, N. O., Creaser, S. P., McKee, T. D., Loureiro, R. M. B., Findeis, M. A., Tate, B. A., Ives, J. L., & Bronk, B. S. (2013) · MedChemComm · doi:10.1039/c3md20357c · Cited by 10
Neurogenesis Is Increased in Human Neural Stem Cells by Aβ40 Peptide
Bernabeu-Zornoza, A., Coronel, R., Palmer, C., Martín, A., López-Alonso, V., & Liste, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105820 · Cited by 11
Nordberg, A. K., Kadir, A., Andreasen, N., Almkvist, O., Wall, A. E., Blennow, K., Långström, B., & Zetterberg, H. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-132474 · Cited by 10
Tsamou, M., Pistollato, F., & Roggen, E. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201418 · Cited by 9
Tagami, S., Okochi, M., Yanagida, K., Kodama, T. S., Arai, T., Kuwano, R., Ikeuchi, T., & Takeda, M. (2013) · Neurodegenerative Diseases · doi:10.1159/000355258 · Cited by 9
Iron treatment inhibits Aβ42 deposition in vivo and reduces Aβ42/Aβ40 ratio
Shen, X., Liu, J., Fujita, Y., Liu, S., Maeda, T., Kikuchi, K., Obara, T., Takebe, A., Sayama, R., Takahashi, T., et al. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.01.119 · Cited by 9
Switched Aβ43 generation in familial Alzheimer’s disease with presenilin 1 mutation
Kakuda, N., Takami, M., Okochi, M., Kasuga, K., Ihara, Y., & Ikeuchi, T. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01684-1 · Cited by 9
A Human Embryonic Stem Cell Model of Aβ-Dependent Chronic Progressive Neurodegeneration
Ubina, T., Magallanes, M., Srivastava, S., Warden, C., Yee, J., & Salvaterra, P. M. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01007 · Cited by 9
Targeting Purinergic Signaling and Cell Therapy in Cardiovascular and Neurodegenerative Diseases
Andrejew, R., Glaser, T., Oliveira‐Giacomelli, Á., Ribeiro, D. E., de Godoy, M. A., Granato, A. E. C., & Ulrich, H. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-31206-0_14 · Cited by 10
Development of an accelerated cellular model for early changes in Alzheimer’s disease
Xue, H., Gate, S., Gentry, E., Losert, W., & Cao, K. (2023) · Scientific Reports · doi:10.1038/s41598-023-45826-5 · Cited by 8
Qiang, W., Kengwerere, M. K., Zhao, W., Scott, F. J., Wutoh-Hughes, X., Wang, T., & Mentink‐Vigier, F. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00523 · Cited by 9
Trambauer, J., Sarmiento, R. M. R., Garringer, H. J., Salbaum, K. A., Pedro, L. D., Crusius, D., Vidal, R., Ghetti, B. F., Paquet, D., Baumann, K., et al. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01680-3 · Cited by 9
The role of prion strain diversity in the development of successful therapeutic treatments
Holec, S. A. M., Block, A. J., & Bartz, J. C. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.07.001 · Cited by 8
The Influence of SARS-CoV-2 Infection on the Development of Selected Neurological Diseases
Kryńska, K., Kuliś, K., Mazurek, W., Gudowska-Sawczuk, M., Zajkowska, M., & Mroczko, B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168715 · Cited by 9
Duchateau, L., Küҫükali, F., Roeck, A. D., Wittens, M. M. J., Temmerman, J., Weets, I., Timmers, M., Engelborghs, S., Bjerke, M., & Sleegers, K. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01338-y · Cited by 8
Are γ-secretase inhibitors detrimental for Alzheimer's disease patients?
Ross, J., & Imbimbo, B. P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101548 · Cited by 8
Angiotensin converting enzyme and Alzheimer’s disease
Kugaevskaya, E. V. (2012) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s199075081201009x · Cited by 8
Angiotensin converting enzyme and Alzheimer's disease
Kugaevskaya, E. V. (2013) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20135901005 · Cited by 8
Kollarik, S., Bimbiryte, D., Sethi, A., Dias, I., Moreira, C. G., & Noaín, D. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1519225 · Cited by 8
The stability and dynamics of the Aβ40/Aβ42 interlaced mixed fibrils
Jana, A. K., Güven, O., & Yaşar, F. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2280765 · Cited by 7
Amyloid β Hypothesis in the Development of Therapeutic Agents for Alzheimer’s Disease
Adeniji, A. O., Adams, P. W., & Mody, V. V. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802810-0.00007-6 · Cited by 7
Miotto, E. C., Brucki, S. M. D., Cerqueira, C. T., Bazán, P. R., Silva, G. A. A., Martin, M. D. G. M., Squarzoni, P., Faria, D. D. P., Coutinho, A. M., Buchpiguel, C. A., et al. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220100 · Cited by 7
Maeda, T., Shimamori, K., Kurita, H., Tokuraku, K., & Kuragano, M. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.113958 · Cited by 7
Iwata, N., Tsubuki, S., Sekiguchi, M., Watanabe-Iwata, K., Matsuba, Y., Kamano, N., Fujioka, R., Takamura, R., Watamura, N., Kakiya, N., et al. (2024) · Life Science Alliance · doi:10.26508/lsa.202402650 · Cited by 8
Gains and losses on the road to understanding Alzheimer’s disease
Konietzko, U. (2015) · Swiss Medical Weekly · doi:10.4414/smw.2015.14233 · Cited by 6
Oughli, H. A., Siddarth, P., Lum, M., Tang, L., Ito, B. S., Abikenari, M. A., Cappelleti, M., Khalsa, D. S., Nguyen, S. A., & Lavretsky, H. (2025) · The Canadian Journal of Psychiatry · doi:10.1177/07067437251343291 · Cited by 5
Jung, C., Uhm, K., Horike, H., Kim, M., Misumi, S., Ishida, A., Ueda, Y., Choi, E., Kim, Y., Michikawa, M., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-141692 · Cited by 5
Apolipoprotein E4 inhibits γ‐secretase activity via binding to the γ‐secretase complex
Sun, Y., Islam, S., Gao, Y., Nakamura, T., Zou, K., & Michikawa, M. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15750 · Cited by 5
Sahara, N., & Lewis, J. M. (2010) · Future Neurology · doi:10.2217/fnl.10.10 · Cited by 5
Classification, pathology, and basic aspects
Pantoni, L., & Gorelick, P. B. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781139382694.002 · Cited by 5
Liu, Z., Meng, X., Lu, R., Meng, X., Li, S., Wang, Y., Liu, X., Liu, J., & Liu, J. (2025) · Aging Cell · doi:10.1111/acel.70311 · Cited by 4
Insights into the Mixture of Aβ24 and Aβ42 Peptides from Atomistic Simulations
Nguyen, P. H., & Derreumaux, P. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c07321 · Cited by 4
The Impact of Apolipoprotein E Allelic Variants on Alzheimer’s Disease
Serrano, E., Sanz, P. G., & Barrantes, F. J. (2021) · Springer eBooks · doi:10.1007/978-3-030-61721-9_29 · Cited by 4
Broeck, B. V., Vanhoutte, G., Cuijt, I., Pereson, S., Joris, G., Timmermans, J., der Linden, A. V., Broeckhoven, C. V., & Kumar‐Singh, S. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.09.073 · Cited by 4
The roles of GxxxG motif and gamma-secretase components in APP processing
Kim, J. (2009) · Interdisciplinary Bio Central · doi:10.4051/ibc.2009.4.0015 · Cited by 3
Self-citationPresenilin 1 deficiency impairs Aβ42-to-Aβ40- and angiotensin-converting activities of ACE
Gao, Y., Sun, Y., Islam, S., Nakamura, T., Tomita, T., Zou, K., & Michikawa, M. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1098034 · Cited by 4
Pal, S., & Melnik, R. (2025) · Quantitative Biology · doi:10.1002/qub2.70001 · Cited by 5
Morisaku, T., & Yui, H. (2017) · Analytical Sciences · doi:10.2116/analsci.33.79 · Cited by 3
Molecular Determinants of Protein Pathogenicity at the Single‐Aggregate Level
Urbanek, A. N., Garland, E. F., Prescott, E. E., King, M. C., Olerinyova, A., Wareing, H. E., Georgieva, N., Bradshaw, E. L., Tzokov, S. B., Knight, A., et al. (2025) · Advanced Science · doi:10.1002/advs.202410229 · Cited by 3
Henry, L., Bhattacharya, S., Bergaglio, T., Pinotsi, D., & Nirmalraj, P. N. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00692 · Cited by 2
Zhou, Y., Sun, Y., Guo, H., Liang, Y.-Z., Zhu, S., Sha, Y., Wan, Z., Xu, J., Jiang, J.-R., Li, Q., et al. (2024) · Food Science and Human Wellness · doi:10.26599/fshw.2024.9250164 · Cited by 2
Metadata
- Authors
- Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D. W., Golde, T., & McGowan, E.
- Affiliations
- Mayo Clinic (US)
- Mayo Clinic in Florida (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2007-01-17
- Volume
- 27
- Issue
- 3
- Pages
- 627-633
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6672801
- OpenAlex
- W2016811754
- Semantic Scholar
- cdc788c9481c38fa796d91320b21decd840d7619
- Cited by
- 359
- References
- 52
- Citations by year
- 2026: 4 · 2025: 12 · 2024: 17 · 2023: 20 · 2022: 16 · 2021: 19 · 2020: 14 · 2019: 21 · 2018: 11 · 2017: 14 · 2016: 21 · 2015: 16 · 2014: 21 · 2013: 27 · 2012: 16
- FWCI
- 17.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- Mayo Foundation for Medical Education and Research
- National Institute on Aging (R01AG022595)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Aβ40, amyloid-beta 42, Alzheimer's disease, amyloid deposition, amyloid plaques, Tg2576 mice, bitransgenic mice, cerebrovascular amyloid
- MeSH terms
- Amyloid, Animals, Humans, Mice, Inbred C57BL, Mice, Transgenic, Peptide Fragments, Amyloid beta-Peptides, Mice, Plaque, Amyloid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
A language model drew the claims from the paper on 2026-10-17, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-10-17 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
Cited sources are checked with a language model’s help (gpt-6-sol).
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
