ArticlePloS one2011
Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicity.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 17 citations in OpenAlex.
- Protein protein Interactions of NarL with NarG, SsrB, and FNR Proteins in Salmonella Typhimurium: A Comparative Analysis.Current microbiology · 2025Article
- Structure of orthoreovirus RNA chaperone σNS, a component of viral replication factories.Nature communications · 2024Article
- Metamorphism in TDP-43 prion-like domain determines chaperone recognition.Nature communications · 2023Article
- Post-Translational Backbone Engineering through Selenomethionine-Mediated Incorporation of Freidinger Lactams.Angewandte Chemie (International ed. in English) · 2018Article
- The amyloid fold of Gad m 1 epitopes governs IgE binding.Scientific reports · 2016Article
- Embryo Microinjection of Selenomethionine Reduces Hatchability and Modifies Oxidant Responsive Gene Expression in Zebrafish.Scientific reports · 2016Article
- PrP charge structure encodes interdomain interactions.Scientific reports · 2015Article
- The protein oxidation repair enzyme methionine sulfoxide reductase a modulates Aβ aggregation and toxicity in vivo.Antioxidants & redox signaling · 2015Article
- Review
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe capacity of a polypeptide chain to engage in an amyloid formation process and cause a conformational disease is contained in its sequence. Some of the sequences undergoing fibrillation contain critical methionine (Met) residues which in vivo can be synthetically substituted by selenomethionine (SeM) and alter their properties. METHODOLOGY/PRINCIPAL
findingsUsing peptide synthesis, biophysical techniques and cell viability determinations we have studied the effect of the substitution of methionine (Met) by selenomethionine (SeM) on the fibrillogenesis and toxic properties of Aβ40 and HuPrP(106-140). We have found that the effects display site-specificity and vary from inhibition of fibrillation and decreased toxicity ([SeM(35)]Aβ40, [SeM(129)]HuPrP(106-140) and [SeM(134)]HuPrP(106-140)), retarded assembly, modulation of polymer shape and retention of toxicity ([SeM(112)]HuPrP(106-140) to absence of effects ([SeM(109)]HuPrP(106-140)). CONCLUSIONS/SIGNIFICANCE: This work provides direct evidence that the substitution of Met by SeM in proamyloid sequences has a major impact on their self-assembly and toxic properties, suggesting that the SeM pool can play a major role in dictating the allowance and efficiency of a polypeptide chain to undergo toxic polymerization.
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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.