The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Alzheimer's Therapeutics Targeting Amyloid Beta 1–42 Oligomers II: Sigma-2/PGRMC1 Receptors Mediate Abeta 42 Oligomer Binding and Synaptotoxicity
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Prior exploratory CSF analyses supported an impact of zervimesine on AD pathophysiology including amyloid biology, synaptic function, inflammation and lipoprotein-related biological processes.
“These exploratory analyses supported an impact of zervimesine on AD pathophysiology [1, 36, 39, 40] including amyloid biology, synaptic function [4–6], inflammation and lipoprotein-related biological processes [5, 6, 41]”
From Impact of zervimesine on the neuroinflammatory biomarker GFAP and related proteomic molecular correlates in plasma of participants from a phase 2 clinical trial in Alzheimer’s disease (2026) · cites this paper as [40]
The Results section on endogenous Aβ oligomers reports that CT01344 displaced oligomers from postmortem AD brain sections, supporting a related effect on amyloid biology. The paper does not report exploratory CSF analyses or identify an effect of zervimesine on the listed biological processes; its experiments cannot establish that broader claim. (LLM, conf=0.83)
Experimental — accuracy not yet measuredS2R modulators have been shown to ameliorate amyloid-β oligomer and α-synuclein oligomer-mediated deficits in neuronal trafficking.
“Indeed, S2R modulators have been shown to ameliorate amyloid-β oligomer and α-synuclein oligomer-mediated deficits in neuronal trafficking [2,3,4]”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [3]
The Results section says sigma-2-selective small molecules prevent and reverse amyloid-β oligomer-induced membrane-trafficking deficits in neuronal cultures. The cited paper does not address α-synuclein oligomer-mediated trafficking deficits, so it supports only the amyloid-β part of the sentence. Page numbers are not available in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measuredTMEM97 and PGRMC1 specific ligands bind their targets more prominently, and with much higher affinity, in neurons than in glial cells.
“Moreover, TMEM97 and PGRMC1 specific ligands bind their targets more prominently, and with much higher affinity, in neurons than in glial cells [6, 7, 47].”
From The Sigma-2 Receptor/TMEM97, PGRMC1, and LDL Receptor Complex Are Responsible for the Cellular Uptake of Aβ42 and Its Protein Aggregates (2020) · cites this paper as [7]
TMEM97 and PGRMC1 are expressed much higher in neurons than in glial cells.
“previous studies have shown that they are expressed much higher in neurons than in glial cells [6, 7, 47].”
From The Sigma-2 Receptor/TMEM97, PGRMC1, and LDL Receptor Complex Are Responsible for the Cellular Uptake of Aβ42 and Its Protein Aggregates (2020) · cites this paper as [7]
Preclinical studies support that S2R small molecule modulators can rescue biological processes that are impaired in neurodegenerative diseases.
“Preclinical studies support that S2R small molecule modulators can rescue biological processes that are impaired in neurodegenerative diseases [2,3,4,5].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [3]
Specific small-molecule ligands that bind to S2R displace endogenous β-amyloid oligomers from human brain samples from individuals with Alzheimer's disease, displace β-amyloid oligomer binding to primary cultured neurons, and reverse cognitive deficits in Alzheimer model mice.
“This is consistent with results showing that specific small-molecule ligands that bind to S2R displace endogenous β-amyloid oligomers from human brain samples from individuals with Alzheimer’s disease, displace β-amyloid oligomer binding to primary cultured neurons, and reverse cognitive deficits in Alzheimer model mice [2,3].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [3]
Amyloid-β oligomer binding to neuronal synapses is abrogated by knockdown of PGRMC1, PrPc, and with S2R modulators in neurons.
“Amyloid-β oligomer binding to neuronal synapses is abrogated by knockdown of PGRMC1 [3], PrPc, and with S2R modulators in neurons [2,3]”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [3]
Results from preclinical Alzheimer's models support that targeting S2R with a small-molecule approach may be a beneficial therapeutic strategy by displacing synaptotoxic amyloid-β oligomers, preventing synaptotoxicity, enabling synapses to recover, and slowing cognitive decline.
“In sum, results from studies in preclinical Alzheimer’s models support that targeting S2R with a small-molecule approach may be a beneficial therapeutic strategy by displacing synaptotoxic amyloid-β oligomers, and preventing synaptotoxicity, thereby enabling synapses to recover and slow cognitive decline [2,3].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [3]
Given the ability of S2R modulators to rescue both amyloid-β oligomer and α-synuclein oligomer deficits, there is promise that S2R may be beneficial in patients with dementia with Lewy bodies.
“Given the ability of S2R modulators to rescue both amyloid-β oligomer and α-synuclein oligomer deficits [2,3,4,64], there is promise that S2R may be beneficial in patients with dementia with Lewy bodies.”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [3]
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Citations
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Self-citationReversing EphB2 depletion rescues cognitive functions in Alzheimer model
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Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies
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Self-citationApolipoprotein E4 effects in Alzheimer’s disease are mediated by synaptotoxic oligomeric amyloid-β
Koffie, R. M., Hashimoto, T., Tai, H.-C., Kay, K. R., Serrano-Pozo, A., Joyner, D., Hou, S., Kopeikina, K. J., Frosch, M. P., Lee, V. M., et al. (2012) · Brain · doi:10.1093/brain/aws127 · Cited by 327
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Self-citationLow density of sigma1 receptors in early Alzheimer’s disease
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“In severely demented Alzheimer’s disease patients (CDR stage 3) expected to have a high degree of cell loss, the density of sigma-2 receptors remains unchanged compared to age-matched normal individuals, while the density of the unrelated sigma-1 receptor is decreased by 54%, as has been previously reported [43].”
FcγRIIb mediates amyloid-β neurotoxicity and memory impairment in Alzheimer’s disease
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Protection against Aβ-mediated rapid disruption of synaptic plasticity and memory by memantine
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SnapShot: Pathobiology of Alzheimer's Disease
Selkoe, D. J. (2013) · Cell · doi:10.1016/j.cell.2013.07.003 · Cited by 46
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Metadata
- Authors
- Izzo, N. J., Xu, J., Zeng, C., Kirk, M. J., Mozzoni, K., Silky, C., Rehak, C., Yurko, R., Look, G., Rishton, G., Safferstein, H., Cruchaga, C., Goate, A., Cahill, M. A., Arancio, O., Mach, R. H., Craven, R., Head, E., LeVine, H., Spires-Jones, T. L., & Catalano, S. M.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2014-11-12
- Volume
- 9
- Issue
- 11
- Pages
- e111899
- ISSN
- 1932-6203
- PMC
- PMC4229119
- Cited by
- 157
- References
- 16
- Language
- en
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