The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
Abstract
To learn about the carboxy-terminal extent of amyloid beta-protein (A beta) composition of senile plaques (SPs) in the brain affected with Alzheimer's disease (AD), we employed two end-specific monoclonal antibodies as immunocytochemical probes: one is specific for A beta 40, the carboxyl terminus of A beta 1-40, while the other is specific for A beta 42(43). In the AD cortex, all SPs that were labeled with an authentic antibody were A beta 42(43) positive, while only one-third of which, on the average, were A beta 40 positive. There was a strong correlation between A beta 40 positivity and mature plaques. Two familial AD cortices with the mutation of beta-amyloid protein precursor 717 (beta APP717) (Val to Ile) showed a remarkable predominance of A beta 42(43)-positive, A beta 40-negative plaques. Diffuse plaques, representing the earliest stage of A beta deposition, were exclusively positive for A beta 42(43), but completely negative for A beta 40.
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In the citing paper
“These observations indicate that Aps ending at Ap42(43), which are a minor component of the Ap in human cerebrospinal fluid and plasma, are critically important in AD where they deposit selectively in plaques of all kinds.”
From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [21]
In the citing paper
“The immunocytochemical results shown here and in a recent report by Iwatsubo et al. (21) demonstrate that BC-05 intensely stains all types of senile plaques, that vessels are stained by both BC-OS and BA-27, and that BA-27 stains plaques poorly, in many cases only faintly staining occasional cored plaques (Fig. 3).”
From Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain (1995) · cites this paper as [21]
In the citing paper
“From studies of trisomy 21 brains (Iwatsubo et al., 1994), it is generally believed that, in human AD, A deposition begins with the formation of diffuse plaques.”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“there is good evidence that A1-42 is deposited early and selectively in senile plaques (Iwatsubo et al., 1994).”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“In contrast, Aβ40, the major Aβ peptide secreted by cells, appears to be the predominant species deposited in the amyloid deposits in the cerebral vasculature (congophillic angiopathy, CAA) (Gravina et al., 1995; Iwatsubo et al., 1994).”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“These data provide definitive in vivo confirmation of predictions inferred from (1) in vitro studies of Aβ aggregation, (2) effects of PS and certain APP mutations on Aβ production and deposition, and (3) analyses of Aβ peptides in the human AD brain (Gravina et al., 1995; Iwatsubo et al., 1994).”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Iwatsubo et al., 1994
In the citing paper
“Indeed, Aβ42 is the main component of amyloid plaques and is shown to be neurotoxic [30].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [30]
In the citing paper
“the slightly longer Aβ42 species that is specifically linked with FAD is also the first Aβ species deposited in cerebral plaques [82].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [82]
In the citing paper
“The subsequent development of antibodies directed at the free C-terminal ends of Aβ40 or Aβ42 [82] led to the ability to differentiate Aβ from APP labeling”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [82]
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Metadata
- Authors
- Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y.
- Affiliations
- Takeda (Japan) (JP)
- The University of Tokyo (JP)
- University of Tsukuba (JP)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1994-07
- Volume
- 13
- Issue
- 1
- Pages
- 45-53
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1991435932
- Cited by
- 1,774
- References
- 41
- Citations by year
- 2026: 30 · 2025: 41 · 2024: 53 · 2023: 49 · 2022: 49 · 2021: 55 · 2020: 68 · 2019: 49 · 2018: 41 · 2017: 49 · 2016: 52 · 2015: 45 · 2014: 68 · 2013: 69 · 2012: 66
- FWCI
- 35.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- 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, Aβ40, amyloid plaques, Alzheimer's disease, familial Alzheimer's disease, plaque maturation, diffuse plaques, immunocytochemistry
- MeSH terms
- Adult, Aged, Aged, 80 and over, Alzheimer Disease, Antibodies, Monoclonal, Brain, Cerebral Cortex, Female, Humans, Immunoenzyme Techniques, Male, Middle Aged, Mutation, Peptide Fragments, Amyloid beta-Peptides
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