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Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
Open accessAbstract
Inability to form new memories is an early clinical sign of Alzheimer’s disease (AD). There is ample evidence that the amyloid-β (Aβ) peptide plays a key role in the pathogenesis of this disorder. Soluble, bio-derived oligomers of Aβ are proposed as the key mediators of synaptic and cognitive dysfunction, but more tractable models of Aβ−mediated cognitive impairment are needed. Here we report that, in mice, acute intracerebroventricular injections of synthetic Aβ 1–42 oligomers impaired consolidation of the long-term recognition memory, whereas mature Aβ 1–42 fibrils and freshly dissolved peptide did not. The deficit induced by oligomers was reversible and was prevented by an anti-Aβ antibody. It has been suggested that the cellular prion protein (PrP C ) mediates the impairment of synaptic plasticity induced by Aβ. We confirmed that Aβ 1–42 oligomers interact with PrP C , with nanomolar affinity. However, PrP-expressing and PrP knock-out mice were equally susceptible to this impairment. These data suggest that Aβ 1–42 oligomers are responsible for cognitive impairment in AD and that PrP C is not required.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
Acute intracerebroventricular injection of synthetic Aβ1–42 oligomers impaired consolidation of long-term object-recognition memory in mice, whereas fibrils and freshly dissolved peptide did not. Although Aβ oligomers bound cellular prion protein (PrPC) with high affinity, PrP-expressing and PrP knockout mice were equally susceptible, indicating PrPC is not required for this memory impairment.
Key findings
- Synthetic Aβ1–42 oligomers (estimated 10–50 nM) impaired long-term recognition memory; mature fibrils and freshly dissolved Aβ did not.
- The oligomer-induced deficit was reversible: memory had fully recovered 10 days after injection without further Aβ, and was completely prevented by i.c.v. pretreatment with 0.25 μg/2 μL of the anti-Aβ antibody 4G8.
- Aβ oligomers bound PrPC with high affinity (Kd ≤20 nM monomer equivalent), but Prnp 0/0 mice were as susceptible as Prnp +/+ mice to oligomer-induced memory impairment; oligomers were also toxic to both Prnp +/+ and Prnp 0/0 hippocampal neurons in vitro.
- Oligomers disrupted memory encoding/consolidation but not retrieval: injection before familiarization prevented memory, whereas injection before the test phase did not.
Methods
- Male C57BL/6 mice, 7–8 weeks old, received acute i.c.v. injections of synthetic Aβ1–42 preparations and were tested in the novel-object recognition task; Prnp 0/0 and Prnp +/+ mice were compared.
- Aβ1–42 oligomers, fibrils, and initial-state peptide were characterized by atomic force microscopy and size exclusion chromatography before behavioral testing.
- Binding to PrPC was measured by surface plasmon resonance using brain homogenates and anti-PrP antibodies; primary hippocampal neuron cultures were treated with 1–3 μM oligomers for 72 h and survival measured by MTT assay. Statistical analysis used ANOVA with post hoc tests.
Limitations
- The paper states that one limitation is the use of oligomeric Aβ preparations not proven identical to those found in AD patient brains.
- Evident from the text: object recognition memory is associated more with perirhinal cortex than hippocampus, so the behavioral model may not fully align with hippocampal LTP studies.
- Evident from the text: the study used only male C57BL/6 mice and a single behavioral task, and it does not establish the mechanism linking Aβ oligomer binding to PrPC with memory impairment.
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Claims the paper makes
20 Own result · 18 Not checked yet · 11 Own interpretation · 2 No basis given · 1 Own method
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
“The deficit induced by oligomers was reversible and was prevented by an anti-Aβ antibody.”
- Also stated in: § Results · plain
“After 10 days, with no further Aβ injection, the memory deficit had fully recovered (Fig. 3A).”
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.
- Also stated in: § Results · 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
“However, PrP-expressing and PrP knock-out mice were equally susceptible to this impairment.”
- Also stated in: § Results · plain
“We found that Prnp 0/0 mice were as susceptible as Prnp +/+ mice to oligomer-induced memory impairment (Figs. 2B and 4A).”
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.
- Also stated in: § Results · 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
“Here we report that, in mice, acute intracerebroventricular injections of synthetic Aβ1–42 oligomers impaired consolidation of the long-term recognition memory, whereas mature Aβ1–42 fibrils and freshly dissolved peptide did not.”
- Also stated in: § Results · plain
“Aβ oligomer–injected mice were unable to distinguish the new object, with no significant difference in the percentage of time spent investigating the two (Fig. 2A), and a discrimination index significantly lower than vehicle-injected mice (Fig. 2B).”
plaindirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- Also stated in: § Results · 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
“We confirmed that Aβ1–42 oligomers interact with PrPC, with nanomolar affinity.”
- Also stated in: § Results · plain
“The binding was dose dependent, with a dissociation constant (K d) of ≤20 nM monomer equivalent (Fig. 7 B and D).”
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.
- Also stated in: § Results · 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
“The deficit induced by oligomers was reversible and was prevented by an anti-Aβ antibody.”
- Also stated in: § Results · plain
“An i.c.v. injection of 0.25 μg/2 μL of 4G8, 5 min before the Aβ oligomers, completely prevented the memory impairment (Fig. 3B).”
plaindirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
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- Also stated in: § Results · 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
“but found no evidence that the two events are related.”
plain- Asserted: passes — The authors put it forward as true.
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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
“An i.c.v. injection of 4G8 alone did not affect memory.”
plain- Asserted: passes — The authors put it forward as true.
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- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
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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
“On the basis of SEC, we estimated the actual oligomer concentration in this sample as 10–50 nM.”
- Also stated in: § Discussion · plain
“The effect was detectable at a nanomolar concentration of Aβ oligomers (10–50 nM).”
plain- Asserted: passes — The authors put it forward as true.
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- Also stated in: § Discussion · 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
“A single i.c.v. injection of a nanomolar concentration of synthetic Aβ1–42 oligomers impairs memory consolidation within 24 h, suggesting that oligomers rapidly interfere with the synaptic activity necessary for the stabilization of new memories.”
plaindirect- Asserted: passes — The authors put it forward as true.
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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
“Heat-denatured antibody, unable to bind Aβ, could not antagonize the effect of Aβ oligomers.”
hedged- Asserted: passes — The authors put it forward as true.
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- It may state two separate claims as one. 14
- Probably not a substantial claim. 15
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
“whereas mature Aβ1–42 fibrils and freshly dissolved peptide did not.”
- Also stated in: § Results · plain
“Neither Aβ in the initial state nor the fibrils affected memory (Fig. 2 A and B).”
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Also stated in: § Results · 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
“When Aβ initial state, oligomers or fibrils were assayed for their binding to PrPC, only Aβ oligomers bound PrPC specifically, and Aβ initial state and fibrils did not (Fig. 7 A and C).”
plaincorrelational- Asserted: passes — The authors put it forward as true.
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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
“Mice injected 2 h before familiarization were unable to remember the object previously investigated, whereas mice injected 2 h before the test phase recalled the familiar object investigated the day before (Fig. 8).”
plaindirect- Asserted: passes — The authors put it forward as true.
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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
“Preliminary data confirmed that the captured protein is actually PrPC, as no capture was detected when flowing brain homogenate from Prnp 0/0 mice (Fig. 6).”
plain- Asserted: passes — The authors put it forward as true.
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In the paper
“PrPC binds synthetic Aβ oligomers with high affinity and plays a role in the oligomer-mediated inhibition of LTP (17).”
What the sources say
- Not checked yetcites [17] Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature. 2009;457:1128–1132. doi: 10.1038/nature07761. [DOI] [PMC free article] [PubMed] [Google Scholar] source
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“All of these processes are affected by Aβ oligomers in vitro, using primary neuronal cultures (12, 15, 36, 37).”
What the sources say
- Not checked yetcites [12] Shankar GM, et al. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci. 2007;27:2866–2875. doi: 10.1523/JNEUROSCI.4970-06.2007. [DOI] [PMC free article] [PubMed] [Google Scholar] source
- Not checked yetcites [15] Lacor PN, et al. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer’s disease. J Neurosci. 2007;27:796–807. doi: 10.1523/JNEUROSCI.3501-06.2007. [DOI] [PMC free article] [PubMed] [Google Scholar] source
- Not checked yetcites [36] Hsieh H, et al. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron. 2006;52:831–843. doi: 10.1016/j.neuron.2006.10.035. [DOI] [PMC free article] [PubMed] [Google Scholar] source
- Not checked yetcites [37] Lacor PN, et al. Synaptic targeting by Alzheimer’s-related amyloid beta oligomers. J Neurosci. 2004;24:10191–10200. doi: 10.1523/JNEUROSCI.3432-04.2004. [DOI] [PMC free article] [PubMed] [Google Scholar] source
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“Several neuronal receptors have been proposed as mediating the effect of Aβ on synaptic plasticity and memory, including the α-7-nicotinic (16), glutamatergic (39–40), and insulin (14) receptors.”
What the sources say
- Not checked yetcites [16] Snyder EM, et al. Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci. 2005;8:1051–1058. doi: 10.1038/nn1503. [DOI] [PubMed] [Google Scholar] source
- Not checked yetcites [39] De Felice FG, et al. Alzheimer’s disease-type neuronal tau hyperphosphorylation induced by A beta oligomers. Neurobiol Aging. 2008;29:1334–1347. doi: 10.1016/j.neurobiolaging.2007.02.029. [DOI] [PMC free article] [PubMed] [Google Scholar] source
- Not checked yetcites [40] Irvine GB, El-Agnaf OM, Shankar GM, Walsh DM. Protein aggregation in the brain: The molecular basis for Alzheimer’s and Parkinson’s diseases. Mol Med. 2008;14:451–464. doi: 10.2119/2007-00100.Irvine. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Not checked yetcites [14] De Felice FG, et al. Protection of synapses against Alzheimer’s-linked toxins: Insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc Natl Acad Sci USA. 2009;106:1971–1976. doi: 10.1073/pnas.0809158106. [DOI] [PMC free article] [PubMed] [Google Scholar] source
hedgedconditional- Asserted: passes — The authors put it forward as true.
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- 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.
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
“These data indicate that Aβ oligomers acutely disrupt anterograde memory storage but do not interfere with its retrieval when the information has been properly stored.”
- Also stated in: § Discussion · plain
“Aβ oligomers inhibited the encoding/consolidation of information, without affecting its retrieval if properly stored.”
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Also stated in: § Discussion · plain
In the paper
“In an elegant study Lauren et al. (17) reported that PrPC mediates the Aβ oligomer-induced hippocampal synaptic plasticity impairment.”
What the sources say
- Not checked yetcites [17] Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature. 2009;457:1128–1132. doi: 10.1038/nature07761. [DOI] [PMC free article] [PubMed] [Google Scholar] source
plaindirect- Asserted: fails — The authors may not put it forward as true.
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Probably not a substantial claim. The authors may not put it forward as true. The paper’s conclusions may not depend on it.
In the paper
“Because recognition memory is dependent on the medial temporal lobe including the hippocampus (25), we examined whether oligomer-mediated memory impairment was also related to PrPC expression.”
What the sources say
- Not checked yetcites [25] Squire LR, Wixted JT, Clark RE. Recognition memory and the medial temporal lobe: A new perspective. Nat Rev Neurosci. 2007;8:872–883. doi: 10.1038/nrn2154. [DOI] [PMC free article] [PubMed] [Google Scholar]
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim.
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
“Unlike Aβ aggregates purified from biological sources, synthetic Aβ oligomers are chemically defined, and can be easily produced and biophysically characterized.”
plain- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“However, some human and primate studies have shown that hippocampal lesions result in impaired object recognition (41, 42)”
What the sources say
- Not checked yetcites [41] Reed JM, Squire LR. Impaired recognition memory in patients with lesions limited to the hippocampal formation. Behav Neurosci. 1997;111:667–675. doi: 10.1037//0735-7044.111.4.667. [DOI] [PubMed] [Google Scholar]
- Not checked yetcites [42] Zola SM, et al. Impaired recognition memory in monkeys after damage limited to the hippocampal region. J Neurosci. 2000;20:451–463. doi: 10.1523/JNEUROSCI.20-01-00451.2000. [DOI] [PMC free article] [PubMed] [Google Scholar]
hedgeddirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“These preparations, and freshly dissolved Aβ1−42 (hereafter referred to as “initial state”), were characterized by atomic force microscopy (AFM) and size exclusion chromatography (SEC) before behavioral investigation.”
plain- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim.
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
“Thus, although Aβ oligomers interact with PrPC with high affinity, they do not act together to induce memory derangement.”
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“PrPC has been involved in neurotrophic signaling (44, 45), and in the regulation of Aβ-production (46), suggesting that PrPC and Aβ may be part of a common molecular pathway governing neuronal differentiation.”
What the sources say
- Not checked yetcites [44] Kanaani J, Prusiner SB, Diacovo J, Baekkeskov S, Legname G. Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro. J Neurochem. 2005;95:1373–1386. doi: 10.1111/j.1471-4159.2005.03469.x. [DOI] [PubMed] [Google Scholar]
- Not checked yetcites [45] Santuccione A, Sytnyk V, Leshchyns’ka I, Schachner M. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J Cell Biol. 2005;169:341–354. doi: 10.1083/jcb.200409127. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Not checked yetcites [46] Parkin ET, et al. Cellular prion protein regulates beta-secretase cleavage of the Alzheimer’s amyloid precursor protein. Proc Natl Acad Sci USA. 2007;104:11062–11067. doi: 10.1073/pnas.0609621104. [DOI] [PMC free article] [PubMed] [Google Scholar]
plaincorrelational- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“However, some human and primate studies have shown that hippocampal lesions result in impaired object recognition (41, 42) and that, for the 24 h intertrial interval from familiarization to test phase used in our study, hippocampal activity is required (43).”
What the sources say
- Not checked yetcites [43] Hammond RS, Tull LE, Stackman RW. On the delay-dependent involvement of the hippocampus in object recognition memory. Neurobiol Learn Mem. 2004;82:26–34. doi: 10.1016/j.nlm.2004.03.005. [DOI] [PubMed] [Google Scholar] source
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“Memory processing requires NMDA receptor activation and intracellular signaling leading to AMPA receptor trafficking, synthesis of new proteins, and formation of dendritic spines (34, 35).”
What the sources say
- Not checked yetcites [34] Collingridge GL, Isaac JT, Wang YT. Receptor trafficking and synaptic plasticity. Nat Rev Neurosci. 2004;5:952–962. doi: 10.1038/nrn1556. [DOI] [PubMed] [Google Scholar]
- Not checked yetcites [35] Lüscher C, Nicoll RA, Malenka RC, Muller D. Synaptic plasticity and dynamic modulation of the postsynaptic membrane. Nat Neurosci. 2000;3:545–550. doi: 10.1038/75714. [DOI] [PubMed] [Google Scholar]
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“The novel-object recognition task is simple and reproducible, it measures recognition memory, which is heavily impaired in AD, and relies on spontaneous animal behavior without the need for stressor elements such as food or water deprivation, electric foot-shock, or aversive environments like water (25).”
What the sources say
- Not checked yetcites [25] Squire LR, Wixted JT, Clark RE. Recognition memory and the medial temporal lobe: A new perspective. Nat Rev Neurosci. 2007;8:872–883. doi: 10.1038/nrn2154. [DOI] [PMC free article] [PubMed] [Google Scholar]
plain- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
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
“Proof that Aβ oligomers are the active amyloid-β species was the lack of effect of either the freshly solubilized Aβ (initial state) or fibrils.”
boosteddirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
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It may state two separate claims as one.
In the paper
“The novel-object recognition task is simple and reproducible, it measures recognition memory, which is heavily impaired in AD, and relies on spontaneous animal behavior without the need for stressor elements such as food or water deprivation, electric foot-shock, or aversive environments like water (25).”
What the sources say
- Not checked yetcites [25] Squire LR, Wixted JT, Clark RE. Recognition memory and the medial temporal lobe: A new perspective. Nat Rev Neurosci. 2007;8:872–883. doi: 10.1038/nrn2154. [DOI] [PMC free article] [PubMed] [Google Scholar]
plaincorrelational- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“At variance with the native peptide, the depsi-peptide is highly soluble and it has a much lower propensity to aggregate, thus preventing the spontaneous formation of seeds in the solution (49, 50).”
What the sources say
- Not checked yetcites [49] Taniguchi A, et al. “Click peptide”: pH-triggered in situ production and aggregation of monomer Abeta1-42. ChemBioChem. 2009;10:710–715. doi: 10.1002/cbic.200800765. [DOI] [PubMed] [Google Scholar]
- Not checked yetcites [50] Taniguchi A, et al. ‘O-Acyl isopeptide method’ for peptide synthesis: Solvent effects in the synthesis of Abeta1-42 isopeptide using ‘O-acyl isodipeptide unit’. J Pept Sci. 2007;13:868–874. doi: 10.1002/psc.905. [DOI] [PubMed] [Google Scholar]
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
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
“One limitation of this study worth to be mentioned may be the use of oligomeric Aβ preparations which haven’t been proven to be identical to those found in the brain of AD patients.”
hedged- 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
“The novel-object recognition task is simple and reproducible”
plain- Asserted: passes — The authors put it forward as true.
- Checkable: fails — It may be too vague to check 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. It may be too vague to check against evidence. The paper’s conclusions may not depend on it. It may state two separate claims as one.
The paper relies on this without support.
Synthetic Aβ1–42 oligomers injected intracerebroventricularly in mice reproduce the relevant actions of endogenous Aβ oligomers in Alzheimer’s disease.
“These data suggest that Aβ1–42 oligomers are responsible for cognitive impairment in AD and that PrPC is not required.”
“Soluble, bio-derived oligomers of Aβ are proposed as the key mediators of synaptic and cognitive dysfunction, but more tractable models of Aβ−mediated cognitive impairment are needed.”
The paper relies on this without support.
There is no consensus as to which brain-derived oligomeric species mediate cognitive deficits in AD.
“since there remains no consensus as to which brain-derived oligomeric species mediate cognitive deficits in AD”
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 cited source says what the claim attributes to it.
In the citing paper
“Atomic Force Microscopy (AFM) was used to verify the actual and correct formation of the Aβ1-42 fibrils ([36]) [68,69].”
From PCSK9 affects astrocyte cholesterol metabolism and reduces neuron cholesterol supplying in vitro: potential implications in Alzheimer’s disease (2022) · cites this paper as [69]
In the citing paper
“other studies have shown that PrP-expressing and PrP-knockout mice are equally susceptible to long-term memory impairment induced by Aβ oligomers (Balducci et al., 2010; Calella et al., 2010)”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Balducci et al., 2010
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
RetractedMemory - A century of consolidation
McGaugh, J. L. (2000) · Science · doi:10.1126/science.287.5451.248 · Cited by 4,250
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Mice devoid of PrP are resistant to scrapie
Büeler, H., Aguzzi, A., Sailer, A. W., Greiner, R., Autenried, P., Aguet, M., & Weissmann, C. (1993) · Cell · doi:10.1016/0092-8674(93)90360-3 · Cited by 2,107
Mucke, 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
Natural 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
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · cited 5×
“Almeida CG, et al. (2005) Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses.”
InfluentialCellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
Cited by
Sorted by citations
Items 201–300 of 468
Advances in Proteasome Enhancement by Small Molecules
George, D. E., & Tepe, J. J. (2021) · Biomolecules · doi:10.3390/biom11121789 · Cited by 42
Cellular Prion Protein Participates in Amyloid-β Transcytosis across the Blood—Brain Barrier
Pflanzner, T., Petsch, B., André-Dohmen, B., Müller‐Schiffmann, A., Tschickardt, S., Weggen, S., Stitz, L., Korth, C., & Pietrzik, C. U. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.7 · Cited by 41
“However, these results were challenged recently (Balducci et al, 2010).”
ResultUnfolded Protein Response and Macroautophagy in Alzheimer’s, Parkinson’s and Prion Diseases
Milisav, I., Šuput, D., & Ribarič, S. (2015) · Molecules · doi:10.3390/molecules201219865 · Cited by 42
“(b) Uncoupling metabotropic glutamate receptors’ (mGluR5) dependent activation of PKC [138]; (c) Binding with PrPc to the mGluR5 and stimulating mGluR5 clustering at synapses; mGluR5 seems to act as a scaffold for the Aβ oligomer—PrPc signalling complexes [139–147]; (d) Binding with PrPc to N-methyl-D-aspartate recept…”
BackgroundNanoliposomes as a Therapeutic Tool for Alzheimer’s Disease
Ordóñez‐Gutiérrez, L., & Wandosell, F. G. (2020) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.00020 · Cited by 40
“The initial data reported that full-length, aggregated Aβ42 with Freund’s adjuvant could reduce plaque load in vivo, in an AD mouse model with no obvious toxicity (Schenk et al., 1999).”
BackgroundInfluentialInflammation and Parkinson's disease pathogenesis: Mechanisms and therapeutic insight
Forloni, G., Vitola, P. L., Cerovic, M., & Balducci, C. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.11.001 · Cited by 41
Self-citationThe Continuing Failure of Bexarotene in Alzheimer’s Disease Mice
Balducci, C., Paladini, A., Micotti, E., Tolomeo, D., Vitola, P. L., Grigoli, E., Richardson, J. C., & Forloni, G. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150029 · Cited by 37
“Smaller, soluble species, products of A aggregation, namely A oligomers, are recognized as the main species responsible for synaptic and cognitive damage as well as the best correlate of disease severity [17, 38–41].”
Self-citationOstapchenko, V. G., Beraldo, F. H., Guimarães, A. L. S., Mishra, S., Guzmán, M. S., Fan, J., Martins, V. R., Prado, V. F., & Prado, M. A. M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12296 · Cited by 38
“…been confirmed by several other laboratories (Chen et al. 2010; Kessels et al. 2010; Caetano et al. 2011), albeit the pathological significance of Ab oligomer interaction with PrPC has been the subject of some controversy (Balducci et al. 2010; Benilova and De Strooper 2010; Calella et al. 2010).”
BackgroundInfliximab ameliorates AD-associated object recognition memory impairment
Kim, D. H., Choi, S., Jho, J., Park, M., Kang, J., Park, S. J., Ryu, J. H., Jo, J., Kim, H. H., & Kim, B. C. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.06.001 · Cited by 37
Younan, N. D., Chen, K., Rose, R., Crowther, D. C., & Viles, J. H. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003319 · Cited by 41
Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization
Foley, A. R., Roseman, G. P., Chan, K., Smart, A., Finn, T. S., Yang, K., Lokey, R. S., Millhauser, G. L., & Raskatov, J. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009238117 · Cited by 38
König, A. S., Rösener, N. S., Gremer, L., Tusche, M., Flender, D., Reinartz, E., Hoyer, W., Neudecker, P., Willbold, D., & Heise, H. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100499 · Cited by 39
Stravalaci, M., Beeg, M., Salmona, M., & Gobbi, M. (2010) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2010.10.038 · Cited by 36
“In the present study, we overcome this problem by using a new ynthesis technique (called Depsipeptide-technique) which allows o obtain seed-free starting solutions of A 1–42 in its very initial tate (Balducci et al., 2010; Sohma et al., 2005; Taniguchi et al., 009).”
MethodInfluentialSelf-citationLeggio, G. M., Catania, M. V., Puzzo, D., Spatuzza, M., Pellitteri, R., Gulisano, W., Torrisi, S. A., Giurdanella, G., Piazza, C., Impellizzeri, A. A. R., et al. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.02.007 · Cited by 37
“Aβ1-42 oligomers are toxic to neurons in cultures [30-31], whereas data obtained in vivo are not unequivocal [28, 32-35].”
BackgroundWang, L.-S., Xue, T., Liu, X., Zhou, Y., Zhang, M.-D., Liao, Y., Pan, R., & Chang, Q. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01084 · Cited by 38
“Recent experiments suggest that Aβ oligomers are more toxic than fibrils (Dahlgren et al., 2002; Balducci et al., 2010; DaRocha-Souto et al., 2011) and have already been detected in Abbreviations: CSA, cajaninstilbene acid; AD, Alzheimer’s disease; Aβ, amyloid β peptide; MWM, Morris water maze;…”
BackgroundUnderstanding the neurospecificity of Prion protein signaling
Schneider, B. (2010) · Frontiers in bioscience · doi:10.2741/3682 · Cited by 36
Prion protein in Alzheimer's pathogenesis: a hot and controversial issue
Benilova, I., & Strooper, B. D. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000088 · Cited by 39
“All groups involved agree that PrP has a remarkable good affinity for Ab peptides tested in various conformations (Balducci et al, 2010; Calella et al, 2010; Lauren et al, 2009).”
BackgroundResultPrions and Neurodegenerative Diseases: A Focus on Alzheimer’s Disease
Crestini, A., Santilli, F., Martellucci, S., Carbone, E., Sorice, M., Piscopo, P., & Mattei, V. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215171 · Cited by 35
“…effect exerted by A (cid:2) Os on synaptic dysfunction, reduction of spine density, inhibition of long-term potentiation, and enhancement of long-term depression (both the last twoprocessesareconsideredmodelsofsynapticplas-ticity)areindependentontheactualpresenceof PrP c receptors [112].”
Patented biological approaches for the therapeutic modulation of the 37 kDa/67 kDa laminin receptor
Omar, A., Jovanovic, K., Dias, B. D. C., Gonsalves, D., Moodley, K., Caveney, R. J., Mbazima, V. G., & Weiss, S. F. T. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.539203 · Cited by 34
A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein
Massignan, T., Cimini, S., Stincardini, C., Cerovic, M., Vanni, I., Elezgarai, S. R., Charco, J. M., Stravalaci, M., Negro, A., Sangiovanni, V., et al. (2016) · Scientific Reports · doi:10.1038/srep23180 · Cited by 33
Self-citationSchmid, S., Jungwirth, B., Gehlert, V., Blobner, M., Schneider, G. H., Kratzer, S., Kellermann, K., & Rammes, G. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.02.007 · Cited by 34
Wilcox, K. C., Marunde, M. R., Das, A., Velasco, P. T., Kuhns, B. D., Marty, M. T., Haoming, J., Luan, C.-H., Sligar, S. G., & Klein, W. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125263 · Cited by 37
Review: PrP 106‐126 – 25 years after
Forloni, G., Chiesa, R., Bugiani, O., Salmona, M., & Tagliavini, F. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12538 · Cited by 34
Self-citationThe development of ADAM10 endocytosis inhibitors for the treatment of Alzheimer’s disease
Musardo, S., Therin, S., Pelucchi, S., D’Andrea, L., Stringhi, R., Ribeiro, A., Manca, A., Balducci, C., Pagano, J., Sala, C., et al. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.03.024 · Cited by 36
Self-citationA novel ARC gene polymorphism is associated with reduced risk of Alzheimer’s disease
Landgren, S., von Otter, M., Palmér, M. S., Zetterström, C. E., Nilsson, S., Skoog, I. G., Gustafson, D., Minthon, L., Wallin, A., Andreasen, N., et al. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0823-x · Cited by 34
“…Ab peptides have been shown to induce cell death (Lambert et al. 1998) and block synaptic plasticity (Lambert et al. 1998; Townsend et al. 2006; Shankar et al. 2008), as well as prevent learning in rodents (Cleary et al. 2005; Lesne et al. 2006; Poling et al. 2008; Balducci et al. 2010).”
BackgroundMiyamoto, T., Kim, D., Knox, J. A., Johnson, E., & Mucke, L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.666529 · Cited by 33
Alzheimer’s disease: From basic science to precision medicine approach
Forloni, G. (2020) · BMJ Neurology Open · doi:10.1136/bmjno-2020-000079 · Cited by 33
Self-citationSynaptic Disruption by Soluble Oligomers in Patients with Alzheimer’s and Parkinson’s Disease
Gutierrez, B. A., & Limón, A. (2022) · Biomedicines · doi:10.3390/biomedicines10071743 · Cited by 32
Neuroprotective and Neurotoxic Signaling by the Prion Protein
Resenberger, U. K., Winklhofer, K. F., & Tatzelt, J. (2011) · Topics in current chemistry · doi:10.1007/128_2011_160 · Cited by 38
Five Questions on Prion Diseases
Aguzzi, A., & Zhu, C. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002651 · Cited by 32
A graphene oxide-based fluorescent platform for selective detection of amyloid-β oligomers
Liu, L., Xia, N., Zhang, J., Mao, W., Wu, Y., & Ge, X. (2015) · Analytical Methods · doi:10.1039/c5ay02018b · Cited by 33
Interaction between Prion Protein and Aβ Amyloid Fibrils Revisited
Nieznański, K., Surewicz, K. A., Chen, S., Nieznańska, H., & Surewicz, W. K. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500019c · Cited by 33
Natural Amyloid-Beta Oligomers Acutely Impair the Formation of a Contextual Fear Memory in Mice
Kittelberger, K. A., Piazza, F., Tesco, G., & Reijmers, L. G. J. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029940 · Cited by 35
“. There is an ongoing effort to determine which of these binding sites are essential for the cognitive effects of Abeta oligomers”
BackgroundLee, T.-Y., Chang, C.-C., Lu, W., et al. (2017) · Scientific Reports · doi:10.1038/srep40002 · Cited by 32
Alier, K. A., Ma, L., Yang, J., Westaway, D. A., & Jhamandas, J. H. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4367-11.2011 · Cited by 30
“…have disputed an obligatory role for PrP C in A -induced impairment of synaptic structure and function, and in AD-related behavioral endpoints (Balducci et al., 2010; Calella et al., 2010; Kessels et al., 2010; Cissé et al., 2011) yet have confirmed physical interactions between A and PrP…”
BackgroundAmyloid Beta-Protein and Neural Network Dysfunction
Peña‐Ortega, F. (2013) · Journal of Neurodegenerative Diseases · doi:10.1155/2013/657470 · Cited by 31
“This type of research may yield not only basic knowledge of neural network dysfunction associated with AD, but also novel options to treat this modern epidemic.”
BackgroundProtein-Protein Interactions and Aggregation Inhibitors in Alzheimer’s Disease
Ganeshpurkar, A., Swetha, R., Kumar, D., Gangaram, G. P., Singh, R., Gutti, G., Jana, S., Kumar, D., Kumar, A., & Singh, S. K. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190304153353 · Cited by 30
Dinamarca, M. C., Luca, M. D., Godoy, J. A., & Inestrosa, N. C. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.08.107 · Cited by 32
Aβ pathology downregulates brain mGluR5 density in a mouse model of Alzheimer
Lee, M., Lee, H., Park, I. S., Park, J. A., Kwon, Y., Ryu, Y. H., Kim, C. H., Kang, J. H., Hyun, I. Y., Lee, K. C., et al. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.02.003 · Cited by 30
“They also suggest that Abo in responsible for cognitive impairment in AD, but that PrPC is not involved in Abo toxicity (Balducci et al., 2010).”
Chen, R.-J., Chang, W.-W., Lin, Y., Cheng, P., & Chen, Y. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn400085q · Cited by 30
Insoluble cellular prion protein and its association with prion and Alzheimer diseases
Zou, W., Zhou, X., Yuan, J., & Xiao, X. (2011) · Prion · doi:10.4161/pri.5.3.16894 · Cited by 28
Domains of STIP1 responsible for regulating PrPC-dependent amyloid-β oligomer toxicity
Maciejewski, A., Ostapchenko, V. G., Beraldo, F. H., Prado, V. F., Prado, M. A. M., & Choy, W. (2016) · Biochemical Journal · doi:10.1042/bcj20160087 · Cited by 31
Monomeric amyloid-β reduced amyloid-β oligomer-induced synapse damage in neuronal cultures
Bate, C., & Williams, A. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.12.007 · Cited by 30
Breaking the Code of Amyloid- β Oligomers
Lesné, S. (2013) · International Journal of Cell Biology · doi:10.1155/2013/950783 · Cited by 29
Tomaselli, S., La Vitola, P., Pagano, K., Brandi, E., Santamaria, G., Galante, D., D’Arrigo, C., Moni, L., Lambruschini, C., Banfi, L., et al. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00241 · Cited by 29
Self-citationAlzheimer's Disease and Prion Protein
Zhou, J. (2013) · Intractable & Rare Diseases Research · doi:10.5582/irdr.2013.v2.2.35 · Cited by 31
Prion protein and its role in signal transduction
Didonna, A. (2013) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-013-0085-0 · Cited by 29
Cellular Prion Protein Mediates Toxic Signaling of Amyloid Beta
Resenberger, U. K., Winklhofer, K. F., & Tatzelt, J. (2011) · Neurodegenerative Diseases · doi:10.1159/000332596 · Cited by 28
Cronier, S., Carimalo, J., Schaeffer, B., Jaumain, E., Béringue, V., Miquel, M., Laude, H., & Peyrin, J. (2012) · The FASEB Journal · doi:10.1096/fj.11-201772 · Cited by 28
Role of cellular prion protein in interneuronal amyloid transmission
del Rı́o, J. A., Ferrer, I., & Gavı́n, R. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.03.001 · Cited by 30
A d-enantiomeric peptide interferes with heteroassociation of amyloid-β oligomers and prion protein
Rösener, N. S., Gremer, L., Reinartz, E., König, A., Brener, O., Heise, H., Hoyer, W., Neudecker, P., & Willbold, D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003116 · Cited by 26
“Aβ(1-42)oligo by sucrose DGC and subsequent RP-HPLC analytics (Fig.”
BackgroundMethodInfluentialAccumulation of cellular prion protein within β‐amyloid oligomer plaques in aged human brains
Takahashi, R. H., Yokotsuka, M., Tobiume, M., Sato, Y., Hasegawa, H., Nagao, T., & Gouras, G. K. (2021) · Brain Pathology · doi:10.1111/bpa.12941 · Cited by 27
“Aβ oligomers are associated with early neuritic degeneration, especially in synaptic compartments (6,7), leading to cognitive impairment (8).”
BackgroundMartínez-Valbuena, I., Valenti‐Azcarate, R., Amat, I., Marcilla, I., Martí‐Andrés, G., Caballero, M. C., Riverol, M., Tuñon, M.-T., Fraser, P. E., & Luquín, M. R. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01171-0 · Cited by 30
Prion protein oligomer and its neurotoxicity
Huang, P., Lian, F., Wen, Y., Guo, C., & Lin, D. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt037 · Cited by 29
Humanin Specifically Interacts with Amyloid-β Oligomers and Counteracts Their in vivo Toxicity
Romeo, M., Stravalaci, M., Beeg, M., Rossi, A., Fiordaliso, F., Corbelli, A., Salmona, M., Gobbi, M., Cagnotto, A., & Diomede, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160951 · Cited by 28
Self-citationPrion Protein PRNP: A New Player in Innate Immunity? The Aβ Connection
Lathe, R., & Darlix, J. (2017) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-170037 · Cited by 28
Ilitchev, A. I., Giammona, M. J., Olivas, C., Claud, S. L., Cantrell, K. L., Wu, C. F., Buratto, S. K., & Bowers, M. T. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b05925 · Cited by 29
Both ghrelin deletion and unacylated ghrelin overexpression preserve muscles in aging mice
Agosti, E., Feudis, M. D., Angelino, E., Belli, R., Teixeira, M. A., Zaggia, I., Tamiso, E., Raiteri, T., Scircoli, A., Ronzoni, F., et al. (2020) · Aging · doi:10.18632/aging.103802 · Cited by 27
Legname, G., & Scialò, C. (2020) · Prion · doi:10.1080/19336896.2020.1854034 · Cited by 29
β-amyloid oligomers and prion protein
Forloni, G., & Balducci, C. (2011) · Prion · doi:10.4161/pri.5.1.14367 · Cited by 26
Self-citationEpelbaum, S., Youssef, I., Lacor, P. N., Chaurand, P., Duplus, E., Brugg, B., Duyckaerts, C. J., & Delatour, B. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.005 · Cited by 30
Darricau, M., Dou, C., Kinet, R., Zhu, T., Zhou, L., Li, X., Bedel, A., Claverol, S., Tokarski, C., Katsinelos, T., et al. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.13604 · Cited by 30
The Quest for Cellular Prion Protein Functions in the Aged and Neurodegenerating Brain
Gavı́n, R., Lidón, L., Ferrer, I., & del Rı́o, J. A. (2020) · Cells · doi:10.3390/cells9030591 · Cited by 25
Prospects of Saffron and its Derivatives in Alzheimer’s Disease
Zandi, N., Pazoki, B., Roudsari, N. M., Lashgari, N., Jamshidi, V., Momtaz, S., Abdolghaffari, A. H., & Akhondzadeh, S. (2021) · Archives of Iranian Medicine · doi:10.34172/aim.2021.35 · Cited by 25
Impact of the Cellular Prion Protein on Amyloid-β and 3PO-Tau Processing
Schmitz, M., Wulf, K., Signore, S. C., Schulz‐Schaeffer, W., Kermer, P., Bähr, M., Wouters, F. S., Zafar, S., & Zerr, I. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130566 · Cited by 25
Cytotoxic Curli Intermediates Form during Salmonella Biofilm Development
Nicastro, L. K., Tursi, S. A., Le, L. S., Miller, A. L., Efimov, A., Buttaro, B. A., Tam, V. C., & Tükel, Ç. (2019) · Journal of Bacteriology · doi:10.1128/jb.00095-19 · Cited by 26
Rial, D., Piermartiri, T., Duarte, F. S., Tasca, C. I., Walz, R., & Prediger, R. D. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.04.034 · Cited by 25
“In recent years, a growing body of research has emphasized that PrP may function as a receptor for Ab oligomers (Lauren et al., 2009; Balducci et al., 2010; Calella et al., 2011).”
BackgroundResult(2011) · Nature Neuroscience · doi:10.1038/nn0411-399 · Cited by 25
Kroker, K. S., Moreth, J., Kußmaul, L., Rast, G. F., & Rosenbrock, H. (2013) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.04.006 · Cited by 24
Choi, J. G., Moon, M., Kim, H. G., Mook‐Jung, I., Chung, S.-Y., Kang, T. H., Kim, S. Y., Lee, E. H., & Oh, M. S. (2011) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2011.06.004 · Cited by 24
“Previous studies suggested that AbO impairs LTP and memory formation as well as interferes with recognition memory in the novel-object recognition test (Balducci et al., 2010; Cleary et al., 2005).”
Brain amyloid β protein and memory disruption in Alzheimer’s disease
Xia, W. (2010) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s7460 · Cited by 24
Lin, K., Lu, W., Wang, S. H., et al. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1140-7 · Cited by 24
“[14], with minor modifications, by using the ProteOn XPR36 Protein Interaction Array system (Bio-Rad).”
BackgroundMethodThe cellular prion protein beyond prion diseases
Manni, G., Lewis, V., Senesi, M., Spagnolli, G., Fallarino, F., Collins, S. J., Mouillet‐Richard, S., & Biasini, E. (2020) · Swiss Medical Weekly · doi:10.4414/smw.2020.20222 · Cited by 25
Self-citationEffect of C-phycocyanin on HDAC3 and miRNA-335 in Alzheimer’s disease
Li, Z., Gan, L., Yan, S., Yan, Y., & Huang, W. (2020) · Translational Neuroscience · doi:10.1515/tnsci-2020-0101 · Cited by 23
RetractedDifferential RNA methylation analysis for MeRIP-seq data under general experimental design
Guo, Z., Shafik, A. M., Jin, P., & Wu, H. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac601 · Cited by 22
Globular and Protofibrillar Aβ Aggregates Impair Neurotransmission by Different Mechanisms
Moreth, J., Kroker, K. S., Schwanzar, D., Schnack, C., Arnim, C. A. F. V., Hengerer, B., Rosenbrock, H., & Kußmaul, L. (2013) · Biochemistry · doi:10.1021/bi3016444 · Cited by 24
Prion protein and prion disease at a glance
Zhu, C., & Aguzzi, A. (2021) · Journal of Cell Science · doi:10.1242/jcs.245605 · Cited by 27
Mario, A. D., Peggion, C., Massimino, M. L., Norante, R. P., Zulian, A., Bertoli, A., & Sorgato, M. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184640 · Cited by 22
Madhu, P., & Mukhopadhyay, S. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00646 · Cited by 20
Bobkova, N. V., Medvinskaya, N. I., Kamynina, A. V., Aleksandrova, I. Y., Nesterova, I. V., Samokhin, A. N., Koroev, D. O., Филатова, М. П., Nekrasov, P. V., Abramov, A. Y., et al. (2013) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2013.10.019 · Cited by 21
“On the other hand, it was reported that memory impairment induced by acute injection of Ab oligomers derived from synthetic peptides does not require PrP, despite the binding of the oligomers to PrP was confirmed (Balducci et al., 2010).”
InfluentialPossible role for Ca2+ in the pathophysiology of the prion protein?
Peggion, C., Bertoli, A., & Sorgato, M. C. (2011) · BioFactors · doi:10.1002/biof.161 · Cited by 21
The cell-permeable Aβ1-6A2VTAT(D) peptide reverts synaptopathy induced by Aβ1-42wt
Cimini, S., Sclip, A., Mancini, S., Colombo, L., Messa, M., Cagnotto, A., Fede, G. D., Tagliavini, F., Salmona, M., & Borsello, T. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.12.013 · Cited by 22
Self-citationDual role of cellular prion protein in normal host and Alzheimer’s disease
Onodera, T. (2017) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.93.010 · Cited by 22
Han, X., Ma, Y., Liu, X., Wang, L., Qi, S., Zhang, Q., & Du, Y. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0803-1 · Cited by 20
The multiple functions of PrPC in physiological, cancer, and neurodegenerative contexts
Grimaldi, I., Leser, F. S., Janeiro, J. M., da Rosa, B. G., Campanelli, A. C., Romão, L. F., & Lima, F. R. S. (2022) · Journal of Molecular Medicine · doi:10.1007/s00109-022-02245-9 · Cited by 21
The Hidden Role of Non-Canonical Amyloid β Isoforms in Alzheimer’s Disease
Busch, L., Eggert, S., Endres, K., & Bufe, B. (2022) · Cells · doi:10.3390/cells11213421 · Cited by 20
Sohma, Y., Hirayama, Y., Taniguchi, A., et al. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.01.021 · Cited by 20
Unaltered prion protein expression in Alzheimer disease patients
Saijo, E., Scheff, S. W., & Telling, G. C. (2011) · Prion · doi:10.4161/pri.5.2.16355 · Cited by 19
N-homocysteinylation of ovine prion protein induces amyloid-like transformation
Stroylova, Y. Y., Chobert, J., Muronetz, V. I., Jakubowski, H., & Haertlé, T. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.06.008 · Cited by 20
Hijacking PrPc-dependent signal transduction: when prions impair Aβ clearance
Hernandez-Rapp, J., Martin‐Lannerée, S., Hirsch, T. Z., Launay, J., & Mouillet‐Richard, S. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00025 · Cited by 24
“While the involvement of PrPc in Aβ-induced neurotoxicity was initially subject to controversy (Balducci et al., 2010; Calella et al., 2010; Kessels et al., 2010; Cisse et al., 2011), possibly as a result of distinct experimental paradigms, notably in the preparation of Aβ mixtures (Nicoll et al.,…”
ResultWilliams, T. L., Choi, J.-K., Surewicz, K. A., & Surewicz, W. K. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00229 · Cited by 20
“amyloid beta-protein (1-40) and (1-42): an”
A Rational Structured Epitope Defines a Distinct Subclass of Toxic Amyloid-beta Oligomers
Silverman, J. M., Gibbs, E., Peng, X., Martens, K. M., Balducci, C., Wang, J., Yousefi, M., Cowan, C. M., Lamour, G., Louadi, S., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00469 · Cited by 21
Self-citationImpact of Genetic Variation in SORCS1 on Memory Retention
Reitz, C., Lee, J. H., Rogers, R. S., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024588 · Cited by 19
“Memory is the cognitive domain predominantly affected by AD, and is associated with changes in Ab levels [32,33,34].”
BackgroundNovel Anti-Neuroinflammatory Properties of a Thiosemicarbazone–Pyridylhydrazone Copper(II) Complex
Choo, X. Y., McInnes, L. E., Grubman, A., Wasielewska, J. M., Belaya, I., Burrows, E. L., Quek, H., Cañas-Martín, J., Loppi, S. H., Sorvari, A., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810722 · Cited by 19
Kanojia, N., Thapa, K., Kaur, G., Sharma, A., Puri, V., & Verma, N. (2022) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2022.104074 · Cited by 19
Cellular prion protein modulates β-amyloid deposition in aged APP/PS1 transgenic mice
Ordóñez‐Gutiérrez, L., Torres, J. M., Gavı́n, R., Antón, M., Arroba, A. I., Espinosa, J. C., Vergara, C., del Rı́o, J. A., & Wandosell, F. G. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.019 · Cited by 19
“, 2010), although subsequent in vivo experiments reported Ab-induced memory impairment in the absence of PrPc (Balducci et al., 2010).”
BackgroundInfluentialStocki, P., Sawicki, M., Mays, C. E., Hong, S. J., Chapman, D. C., Westaway, D. A., & Williams, D. B. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-10-0729 · Cited by 21
Identification of prion protein-derived peptides of potential use in Alzheimer's disease therapy
Nieznańska, H., Bandyszewska, M., Surewicz, K. A., Zajkowski, T., Surewicz, W. K., & Nieznański, K. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.03.023 · Cited by 19
Mantile, F., Trovato, M., Santoni, A., Barba, P., Ottonello, S., Berardinis, P. D., & Prisco, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101474 · Cited by 19
“Immuno-dot blot analysis of (1–11)E2 antisera reactivity against different Ab species Distinct Ab species were generated from the water-soluble depsipeptide derivative of Ab42 (Ab42-depsi; RP10017-1, GenScript) as described previously [15,16].”
MethodModulation of prion polymerization and toxicity by rationally designed peptidomimetics
Srivastava, A., Sharma, S., Sadanandan, S., Gupta, S., Singh, J., Gupta, S., Haridas, V., & Kundu, B. (2016) · Biochemical Journal · doi:10.1042/bcj20160737 · Cited by 19
“oligomers of different morphological features have been reported (81-83).”
BackgroundThe neuroprotective effects of Chinese bayberry leaves proanthocyanidins
Li, L., Zhang, Y., Sun, B., Zhang, H., Tao, W., Tian, J., Ye, X., & Chen, S. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.08.031 · Cited by 19
Metadata
- Authors
- Balducci, C., Beeg, M., Stravalaci, M., Bastone, A., Sclip, A., Biasini, E., Tapella, L., Colombo, L., Manzoni, C., Borsello, T., Chiesa, R., Gobbi, M., Salmona, M., & Forloni, G.
- Affiliations
- Mario Negri Institute for Pharmacological Research (IT)
- Dulbecco Telethon Institute (IT)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-01-19
- Volume
- 107
- Issue
- 5
- Pages
- 2295-2300
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2836680
- OpenAlex
- W2002280328
- Semantic Scholar
- 63625a2fc958c65a2cb276db617f403efa9be515
- Cited by
- 466
- References
- 57
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 14 · 2023: 19 · 2022: 20 · 2021: 24 · 2020: 31 · 2019: 25 · 2018: 32 · 2017: 40 · 2016: 31 · 2015: 35 · 2014: 27 · 2013: 47 · 2012: 36
- FWCI
- 33.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Iris (University of Trento) (submittedVersion)
- 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
- amyloid-beta oligomers, amyloid-beta 42, Alzheimer's disease, long-term memory, memory consolidation, recognition memory, cellular prion protein, anti-amyloid antibodies, cognitive impairment, intracerebroventricular administration, amyloid fibrils
- MeSH terms
- Prion Proteins, Alzheimer Disease, Animals, Cognition Disorders, Humans, Injections, Intraventricular, Male, Memory, Mice, Inbred C57BL, Neuronal Plasticity, Peptide Fragments, Prions, Protein Binding, Amyloid beta-Peptides, Mice, Knockout, PrPC Proteins, Surface Plasmon Resonance, Mice
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