ReviewThe protein journal2019
Structure and Function of Alzheimer's Amyloid βeta Proteins from Monomer to Fibrils: A Mini Review.
Review in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The Amyloid-β Pathway in Alzheimer's Disease.Molecular psychiatry · 2021Pooled it
- Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026Article
- Mechanistic insights into dimerization and cross-β sheet formation in the HIV-associated amyloidogenic peptide PAP248-286 from unbiased all-atom molecular dynamics simulations.Computational and structural biotechnology journal · 2026Article
- Conventional and Emerging Drug Targeting Sites in Alzheimer's Disease and the Role of Translational Informatics in its Diagnosis and Management.Current neuropharmacology · 2025Review
- Investigating the Effects of the POPC-POPG Lipid Bilayer Composition on PAP248-286 Binding Using CG Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- A coarse-grained molecular dynamics investigation on spontaneous binding of AβComputational and structural biotechnology journal · 2023Article
- Early stages of misfolding of PAP248-286 at two different pH values: An insight from molecular dynamics simulations.Computational and structural biotechnology journal · 2022Article
- Peptide-Based Vaccines for Neurodegenerative Diseases: Recent Endeavors and Future Perspectives.Vaccines · 2021Review
- Structural characterisation of amyloid-like fibrils formed by an amyloidogenic peptide segment of β-lactoglobulin.RSC advances · 2021Article
- Journey on Naphthoquinone and Anthraquinone Derivatives: New Insights in Alzheimer's Disease.Pharmaceuticals (Basel, Switzerland) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alzheimer's disease is the most common form of dementia, that affects millions of people worldwide. According to the widely accepted amyloid cascade hypothesis, misfolding and aggregation of Aβ peptides is the principal cause of Alzheimer's disease. In the present mini-review, we have discussed the different structures of Aβ protein from monomer to fibrils and their arrangement in different symmetries. We have highlighted the critical amino acid residue that plays a crucial role in the early stage misfolding of Aβ monomers, Aβ fibrils arrangement in different symmetries, the elongation process and Aβ protein interaction with the membrane. We have further discussed the antibodies that are currently in clinical trial phase III for Alzheimer's disease.
Indexed as
Identifiers
31325011What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.