RETRACTED: Peptide-induced formation of protein aggregates and amyloid fibrils in human and guinea pig αA-crystallins under physiological conditions of temperature and pH
| Autor: | Anthony Premceski, Eric Seidel, Jonathan Cheon, Anbarasu Kumarasamy, Sivakumar Jeyarajan, Frank J. Giblin, Victoria A. Kimler |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Amyloid
Nuclear cataract Guinea Pigs Molecular Sequence Data Peptide Protein aggregation alpha-Crystallin A Chain Article Guinea pig Protein Aggregates Cellular and Molecular Neuroscience Microscopy Electron Transmission Crystallin Lens Crystalline Animals Humans Amino Acid Sequence Chromatography High Pressure Liquid chemistry.chemical_classification Amyloid beta-Peptides Temperature Hydrogen-Ion Concentration Amyloid fibril Peptide Fragments Recombinant Proteins Sensory Systems Ophthalmology chemistry Transmission electron microscopy Biophysics Electrophoresis Polyacrylamide Gel |
| Zdroj: | Exp Eye Res |
| ISSN: | 0014-4835 |
| DOI: | 10.1016/j.exer.2018.11.016 |
| Popis: | This article has been retracted: please see Elsevier Policy on Article Withdrawal (https://www.elsevier.com/about/our-business/policies/article-withdrawal). This article has been retracted at the request of the authors. The senior author contacted the journal in a forthright manner, in an effort to preserve the scientific integrity of the literature, after discovering a significant error in the results reported in the article. The authors were recently made aware of a paper by Kim et al. (Nature Commun. 2019) which shows a spirosome structure (the enzyme aldehyde-alcohol dehydrogenase) present in E. coli (Fig. 5a) that is very similar to the structure the authors thought formed when synthetic alpha A crystallin (66-80) peptide was incubated for 24 h with recombinant guinea pig alpha A insert crystallin (see Kumarasamy et al., Figs. 7C and F, and Fig. 9). Subsequent to publication of their report, the authors later found a number of images that showed what appeared to be the same structure present in samples of their presumably purified recombinant guinea pig alpha A insert crystallin which had been incubated without peptide for 24 h. Hence, the authors now conclude that the structures shown in Figs. 7C and F, and Fig. 9 of their article published in this journal are actually due to E. coli contaminant aldehyde-alcohol dehydrogenase. The authors deeply regret this error and any inconvenience it may have caused. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect