Cited by 67Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 351 of the 355 references it cites were found in a registry or an index.

Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets

Han, Sun-Ho, Park, Jong-Chan, Mook-Jung, Inhee·2016·Progress in Neurobiology

DOI 10.1016/j.pneurobio.2015.12.004

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Abstract

Alzheimer's disease (AD) is one of the most devastating neurodegenerative diseases in modern society because of insurmountable difficulties in early diagnosis and lack of therapeutic treatments. AD pathogenesis is tightly linked to the abnormal accumulation and aggregation of amyloid β (Aβ), seemingly the main causative factor of AD; however, intensive research on Aβ has not yet explained the complexity of AD pathogenesis. Consequently, the role of other supportive partners of Aβ have been elucidated and evaluated in the etiology of AD, and their potential molecular mechanisms have emerged as possible therapeutic targets. In this review, we compile information regarding Aβ-interacting partners in normal conditions and AD pathology, and analyze their etiological roles in diverse areas. Furthermore, we integrate this information into suggestions for probable clinical applications for AD diagnosis and therapeutics. We include Aβ-interacting partners localized to the cell surface and intracellular and extracellular compartments of different cell types ranging from the central nervous system to peripheral regions. Additionally, we expand the range of Aβ-interacting partners by including not only proteins, but also inorganic substances like metals, expecting that one of these partners may yield a critical breakthrough in the field of AD diagnostics and therapeutic drug development.

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Authors: Han, S.-H., Park, J.-C., & Mook-Jung, I.
Affiliations: Seoul National University (KR)
ORCID: Park, Jong-Chan
Venue: Progress in Neurobiology
Publisher: Elsevier BV
Published: 2016-02
Volume: 137
Pages: 17-38
ISSN: 0301-0082 (ISSN-L)
DOI: 10.1016/j.pneurobio.2015.12.004
OpenAlex: W2207689373
Cited by: 67
References: 355
Citations by year: 2026: 1 · 2025: 3 · 2024: 4 · 2023: 4 · 2022: 4 · 2021: 11 · 2020: 5 · 2019: 10 · 2018: 9 · 2017: 12 · 2016: 4
FWCI: 1.02
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Progress in Neurobiology (publishedVersion)
PubMed (publishedVersion)
Funders: NRF (2015R1A2A1A05001794, 2014M3C7A1046047, 2015M3C7A1028790, 2015R1C1A2A01053545)
MRC (2012R1A5A2A44671346)
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: Alzheimer's disease, amyloid-beta, protein-protein interaction, amyloid fibril formation, AD pathogenesis, therapeutic target
MeSH terms: Alzheimer Disease, Animals, Blood Proteins, Brain, Humans, Metals, Prions, Receptors, Cell Surface, Amyloid beta-Peptides, LDL-Receptor Related Proteins, Apolipoprotein E4

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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.

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 ›

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Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets

Abstract

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