Literature DB >> 30448341

RETRACTED: Peptide-induced formation of protein aggregates and amyloid fibrils in human and guinea pig αA-crystallins under physiological conditions of temperature and pH.

Anbarasu Kumarasamy1, Sivakumar Jeyarajan2, Jonathan Cheon2, Anthony Premceski2, Eric Seidel2, Victoria A Kimler2, Frank J Giblin3.   

Abstract

This article has been retracted: please see Elsevier Policy on Article Withdrawal (https://www.elsevier.com/about/our-business/policies/article-withdrawal). This article has been retracted at the request of the authors.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.
Copyright © 2018 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Amyloid fibrils; Disulfide crosslinking; Guinea pig; Human; Lens crystallins; Nuclear cataract; Transmission electron microscopy; αA(66−80) peptide

Mesh:

Substances:

Year:  2018        PMID: 30448341      PMCID: PMC6380173          DOI: 10.1016/j.exer.2018.11.016

Source DB:  PubMed          Journal:  Exp Eye Res        ISSN: 0014-4835            Impact factor:   3.467


  82 in total

1.  Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct.

Authors:  Mihaela Necula; Rakez Kayed; Saskia Milton; Charles G Glabe
Journal:  J Biol Chem       Date:  2007-02-06       Impact factor: 5.157

2.  Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage.

Authors:  Sean D Moran; Tianqi O Zhang; Sean M Decatur; Martin T Zanni
Journal:  Biochemistry       Date:  2013-08-29       Impact factor: 3.162

3.  Prediction of aggregation-prone regions in structured proteins.

Authors:  Gian Gaetano Tartaglia; Amol P Pawar; Silvia Campioni; Christopher M Dobson; Fabrizio Chiti; Michele Vendruscolo
Journal:  J Mol Biol       Date:  2008-05-13       Impact factor: 5.469

4.  Levels of crystallin fragments and identification of their origin in water soluble high molecular weight (HMW) proteins of human lenses.

Authors:  O P Srivastava; K Srivastava; C Silney
Journal:  Curr Eye Res       Date:  1996-05       Impact factor: 2.424

5.  On the presence and mechanism of formation of heavy molecular weight aggregates in human normal and cataractous lenses.

Authors:  J A Jedziniak; J H Kinoshita; E M Yates; L O Hocker; G B Benedek
Journal:  Exp Eye Res       Date:  1973-02       Impact factor: 3.467

6.  Reduced chaperone-like activity of alpha A(ins)-crystallin, an alternative splicing product containing a large insert peptide.

Authors:  R H Smulders; I G van Geel; W L Gerards; H Bloemendal; W W de Jong
Journal:  J Biol Chem       Date:  1995-06-09       Impact factor: 5.157

7.  Cataract formation in a strain of rats selected for high oxidative stress.

Authors:  Stefania Marsili; Rudolf I Salganik; Craig D Albright; Christopher D Freel; Sonke Johnsen; Robert L Peiffer; M Joseph Costello
Journal:  Exp Eye Res       Date:  2004-11       Impact factor: 3.467

8.  Quasielastic light scattering study of the living human lens as a function of age.

Authors:  G M Thurston; D L Hayden; P Burrows; J I Clark; V G Taret; J Kandel; M Courogen; J A Peetermans; M S Bowen; D Miller; K M Sullivan; R Storb; H Stern; G B Benedek
Journal:  Curr Eye Res       Date:  1997-03       Impact factor: 2.424

9.  Effects of dithiothreitol on protein activity unrelated to thiol-disulfide exchange: for consideration in the analysis of protein function with Cleland's reagent.

Authors:  M C Alliegro
Journal:  Anal Biochem       Date:  2000-06-15       Impact factor: 3.365

10.  In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.

Authors:  Melissa S Kosinski-Collins; Jonathan King
Journal:  Protein Sci       Date:  2003-03       Impact factor: 6.725

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