ReviewMolecules (Basel, Switzerland)2018
Peptides as Potential Therapeutics for Alzheimer's Disease.
Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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.
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Who cites it
23 citing papers in PubMed, 63 citations in OpenAlex.
- Assembling peptides for treating Alzheimer's disease: a supramolecular perspective.RSC advances · 2026Review
- Peptide-based therapeutics in the management of Alzheimer's disease (AD) and their potential to develop novel strategies.Metabolic brain disease · 2026Review
- Therapeutic Potential of HAEEPGP Peptide Against β-Amyloid Induced Neuropathology.Molecular neurobiology · 2025Article
- Structural Analysis of Amylin and Amyloid β Peptide Signaling in Alzheimer's Disease.Biomolecules · 2025Article
- Advancing Amyloid Aggregation Research: A Focus on Innovative Therapies, Molecular Modeling and Nano-Delivery Systems in Alzheimer's Disease.Current drug targets · 2025Review
- Designed Cell-Penetrating Peptide Constructs for Inhibition of Pathogenic Protein Self-Assembly.Pharmaceutics · 2024Review
- Topoisomeric Membrane-Active Peptides: A Review of the Last Two Decades.Pharmaceutics · 2023Review
- Aducanumab-Hope or Disappointment for Alzheimer's Disease.International journal of molecular sciences · 2023Review
- AmyP53, a Therapeutic Peptide Candidate for the Treatment of Alzheimer's and Parkinson's Disease: Safety, Stability, Pharmacokinetics Parameters and Nose-to Brain Delivery.International journal of molecular sciences · 2022Article
- Neuroepigenetic Mechanisms of Action of Ultrashort Peptides in Alzheimer's Disease.International journal of molecular sciences · 2022Review
- Development of Peptide Biopharmaceuticals in Russia.Pharmaceutics · 2022Review
- Pharmacokinetics and Molecular Modeling Indicate nAChRα4-Derived Peptide HAEE Goes through the Blood-Brain Barrier.Biomolecules · 2021Article
- Amyloid-β-Derived Peptidomimetics Inhibits Tau Aggregation.ACS omega · 2021Article
- Copper Dyshomeostasis in Neurodegenerative Diseases-Therapeutic Implications.International journal of molecular sciences · 2020Review
- Copper Toxicity Links to Pathogenesis of Alzheimer's Disease and Therapeutics Approaches.International journal of molecular sciences · 2020Review
- Heptameric Peptide Interferes with Amyloid-β Aggregation by Structural Reorganization of the Toxic Oligomers.ACS omega · 2020Article
- How Does the Mono-Triazole Derivative Modulate AβACS omega · 2020Article
- Amyloid beta peptide-degrading microbial enzymes and its implication in drug design.3 Biotech · 2020Review
- Oxidative Stress in Alzheimer's Disease:Oxidative medicine and cellular longevity · 2020Article
- Multitarget Therapeutic Strategies for Alzheimer's Disease: Review on Emerging Target Combinations.BioMed research international · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular synthesis, folding, trafficking and degradation of proteins are controlled and integrated by proteostasis. The frequency of protein misfolding disorders in the human population, e.g., in Alzheimer's disease (AD), is increasing due to the aging population. AD treatment options are limited to symptomatic interventions that at best slow-down disease progression. The key biochemical change in AD is the excessive accumulation of per-se non-toxic and soluble amyloid peptides (Aβ(1-37/44), in the intracellular and extracellular space, that alters proteostasis and triggers Aβ modification (e.g., by reactive oxygen species (ROS)) into toxic intermediate, misfolded soluble Aβ peptides, Aβ dimers and Aβ oligomers. The toxic intermediate Aβ products aggregate into progressively less toxic and less soluble protofibrils, fibrils and senile plaques. This review focuses on peptides that inhibit toxic Aβ oligomerization, Aβ aggregation into fibrils, or stabilize Aβ peptides in non-toxic oligomers, and discusses their potential for AD treatment.
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What 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.