ArticleInternational journal of cell biology2013
Disulfide bonding in neurodegenerative misfolding diseases.
Article in International journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 51 citations in OpenAlex.
- Predicted high affinity binding of prion PRPC protein to Human Leukocyte Antigen (HLA).Journal of immunological sciences · 2026Article
- Construction of artificial organellesChemical science · 2025Review
- Hydroxyurea induces an oxidative stress response that triggers ER expansion and cytoplasmic protein aggregation.PLoS biology · 2025Article
- Investigating the role of disulfidoptosis in spinal cord injury and development of a novel diagnostic model.Acta orthopaedica et traumatologica turcica · 2025Article
- Protein Oxidative Modifications in Neurodegenerative Diseases: From Advances in Detection and Modelling to Their Use as Disease Biomarkers.Antioxidants (Basel, Switzerland) · 2024Review
- Role of Nanoparticle-Conjugates and Nanotheranostics in Abrogating Oxidative Stress and Ameliorating Neuroinflammation.Antioxidants (Basel, Switzerland) · 2023Review
- Self-assembly of achiral building blocks into chiral cyclophanes using non-directional interactions.Chemical science · 2023Article
- A Single-Molecule Strategy to Capture Non-native Intramolecular and Intermolecular Protein Disulfide Bridges.Nano letters · 2022Article
- Review
- Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling.International journal of molecular sciences · 2021Article
- Accelerating Reaction Rates of Biomolecules by Using Shear Stress in Artificial Capillary Systems.Journal of the American Chemical Society · 2021Article
- Feasibility of Sijunzi Tang (Chinese medicine) to enhance protein disulfide isomerase activities for reactivating malate dehydrogenase deactivated by polycyclic aromatic hydrocarbons.Environmental science and pollution research international · 2021Article
- The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding.The protein journal · 2021Review
- Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments.Molecules (Basel, Switzerland) · 2021Review
- The Extracellular Domains of GluN Subunits Play an Essential Role in Processing NMDA Receptors in the ER.Frontiers in neuroscience · 2021Review
- Mechanism of human γD-crystallin protein aggregation in UV-C light.Molecular vision · 2021Article
- Revisiting the Formation of a Native Disulfide Bond: Consequences for Protein Regeneration and Beyond.Molecules (Basel, Switzerland) · 2020Review
- Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Profiling Cysteine Reactivity and Oxidation in the Endoplasmic Reticulum.ACS chemical biology · 2020Article
- Variable Mutations at the p53-R273 Oncogenic Hotspot Position Leads to Altered Properties.Biophysical journal · 2020Article
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
In recent years an increasing number of neurodegenerative diseases has been linked to the misfolding of a specific protein and its subsequent accumulation into aggregated species, often toxic to the cell. Of all the factors that affect the behavior of these proteins, disulfide bonds are likely to be important, being very conserved in protein sequences and being the enzymes devoted to their formation among the most conserved machineries in mammals. Their crucial role in the folding and in the function of a big fraction of the human proteome is well established. The role of disulfide bonding in preventing and managing protein misfolding and aggregation is currently under investigation. New insights into their involvement in neurodegenerative diseases, their effect on the process of protein misfolding and aggregation, and into the role of the cellular machineries devoted to disulfide bond formation in neurodegenerative diseases are emerging. These studies mark a step forward in the comprehension of the biological base of neurodegenerative disorders and highlight the numerous questions that still remain open.
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.