ArticlePloS one2014
Di-tyrosine cross-link decreases the collisional cross-section of aβ peptide dimers and trimers in the gas phase: an ion mobility study.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Comparative Characterization of Oxidative Enzymes for Arabinoxylan and Protein Cross-Linking via Ferulic Acid and Tyrosine in Model Systems.Journal of agricultural and food chemistry · 2025Article
- Photonics of Hydrothermally Treated β-Lactoglobulin Amyloids.Small science · 2024Article
- Dityrosine cross-linking and its potential roles in Alzheimer's disease.Frontiers in neuroscience · 2023Review
- Stress Dissipation Encoded Silk Fibroin Electrode for the Athlete-Beneficial Silk Bioelectronics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- A Disulfide-Stabilized Aβ that Forms Dimers but Does Not Form Fibrils.Biochemistry · 2022Article
- Dityrosine Crosslinking of Collagen and Amyloid-β Peptides Is Formed by Vitamin BInternational journal of molecular sciences · 2021Article
- The F19W mutation reduces the binding affinity of the transmembrane AβRSC advances · 2021Article
- Article
- Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage.Nature communications · 2020Article
- Multicharacteristic Behavior of Tyrosine Present in the Microdomains of the Macromolecule Gum Arabic at Various pH Conditions.ACS omega · 2018Article
- Copper Redox Cycling Inhibits Aβ Fibre Formation and Promotes Fibre Fragmentation, while Generating a Dityrosine Aβ Dimer.Scientific reports · 2018Article
- Kinetic Analysis Reveals the Identity of Aβ-Metal Complex Responsible for the Initial Aggregation of Aβ in the Synapse.ACS chemical neuroscience · 2017Article
- SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS.Scientific reports · 2015Article
- Using mass spectrometry-based methods to understand amyloid formation and inhibition of alpha-synuclein and amyloid beta.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligomeric forms of Aβ peptide are most likely the main synaptotoxic and neurotoxic agent in Alzheimer's disease. Toxicity of various Aβ oligomeric forms has been confirmed in vivo and also in vitro. However, in vitro preparations were found to be orders of magnitude less toxic than oligomers obtained from in vivo sources. This difference can be explained by the presence of a covalent cross-link, which would stabilize the oligomer. In the present work, we have characterized the structural properties of Aβ dimers and trimers stabilized by di- and tri-tyrosine cross-links. Using ion mobility mass spectrometry we have compared the collisional cross-section of non-cross-linked and cross-linked species. We have found that the presence of cross-links does not generate new unique forms but rather shifts the equilibrium towards more compact oligomer types that can also be detected for non-cross-linked peptide. In consequence, more extended forms, probable precursors of off-pathway oligomeric species, become relatively destabilized in cross-linked oligomers and the pathway of oligomer evolution becomes redirected towards fibrillar structures.
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