ArticleThe Journal of organic chemistry2020
Ubiquitination Can Change the Structure of the α-Synuclein Amyloid Fiber in a Site Selective Fashion.
Article in The Journal of organic chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Ubiquitin signatures on aggregating proteins in neurodegeneration.Essays in biochemistry · 2025Review
- Targeting Cdc42 improves motor phenotype in Parkinson's disease mice and reveals age-dependent susceptibility to α-synuclein.iScience · 2025Article
- The Role of the Ubiquitin System in Eye Diseases.Life (Basel, Switzerland) · 2025Review
- Posttranslational Modifications ofPharmacological reviews · 2024Review
- Biochemical Fractionation of Human α-Synuclein in aInternational journal of molecular sciences · 2024Article
- Review
- Combining non-canonical amino acid mutagenesis and native chemical ligation for multiply modifying proteins: A case study of α-synuclein post-translational modifications.Methods (San Diego, Calif.) · 2023Article
- In Silico Evaluation of the Potential Association of the Pathogenic Mutations of Alpha Synuclein Protein with Induction of Synucleinopathies.Diseases (Basel, Switzerland) · 2023Article
- Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson's disease.BMB reports · 2022Review
- Cysteine-Based Mimic of Arginylation Reproduces Neuroprotective Effects of the Authentic Post-Translational Modification on α-Synuclein.Journal of the American Chemical Society · 2022Article
- Atypical Ubiquitination and Parkinson's Disease.International journal of molecular sciences · 2022Review
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- Consequences of post-translational modifications on amyloid proteins as revealed by protein semisynthesis.Current opinion in chemical biology · 2021Review
- Alpha-synuclein research: defining strategic moves in the battle against Parkinson's disease.NPJ Parkinson's disease · 2021Review
- Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications.Frontiers in neurology · 2021Review
- Effects of Glutamate Arginylation on α-Synuclein: Studying an Unusual Post-Translational Modification through Semisynthesis.Journal of the American Chemical Society · 2020Article
- Deciphering protein post-translational modifications using chemical biology tools.Nature reviews. Chemistry · 2020Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Toxic amyloid aggregates are a feature of many neurodegenerative diseases. A number of biochemical and structural studies have demonstrated that not all amyloids of a given protein are equivalent but rather that an aggregating protein can form different amyloid structures or polymorphisms. Different polymorphisms can also induce different amounts of pathology and toxicity in cells and in mice, suggesting that the structural differences may play important roles in disease. However, the features that cause the formation of polymorphisms
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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.