ReviewFrontiers in molecular biosciences2025
Subtle concentration changes in zinc hold the key to fibrillation of α-synuclein: an updated insight on the micronutrient's role in prevention of neurodegenerative disorders.
Review in Frontiers in molecular biosciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
2 citing papers in PubMed.
- Association of peripheral and CSF zinc levels with Parkinson's disease: A systematic review and meta-analysis.IBRO neuroscience reports · 2026Review
- Comprehensive Speciation and Computational Study of CuMolecules (Basel, Switzerland) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Misfolded proteins have been found to be at the core of an increasing number of cognitive ailments. α-synuclein, a resident chaperone of the neurosynaptic cleft has been implicated in a major share of these neurodegenerative diseases. Over the years, a daunting task for researchers has been the identification of the complex set of conditions which govern the Substantia nigra microenvironment for transformation of α-synuclein from a functional and grossly structureless chaperone to toxic cross-β fibrils. An abundance of Reactive Oxygen Species and a drop in pH of the solvent have been identified to be the key drivers of the fibrillation process which is initiated by Liquid-Liquid phase separation of α-synuclein droplets. Zinc is a significant micronutrient of the human body integral to the proper functioning of the nervous system as well as holistic cognitive development. Many recent studies have deciphered that metal ions including zinc facilitate the fibrillation of α-synuclein by shielding negative charges at the C terminus of the protein. Zinc preferentially binds to Asp121 at the C terminus and His50 at the N terminus to promote fibrillation. On the contrary, zinc has many protective roles to retard fibrillation of the protein at the same time. It downregulates ROS and assists chaperones which prevent non-native aggregation of α-synuclein. The ability of zinc to bind preferentially to α-synuclein coupled with the advent of ultrasensitive detection technologies such as the Surface Enhanced Raman Spectroscopy has led to the prospects of zinc-oxide nanoparticles as effective tools to probe the α-synuclein-based biomarker for early detection of protein aggregates in the body fluid. This review summarizes the significant mechanistic findings which has facilitated our understanding of the fibrillation of α-synuclein, the precise role and mechanism of zinc involved therein and the prospects of using zinc in designing efficient tools for diagnosis of Parkinson's Disease and other synucleinopathies.
Indexed as
Identifiers
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.