ArticleStructure (London, England : 1993)2013
Early folding events protect aggregation-prone regions of a β-rich protein.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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, 16 citations in OpenAlex.
- Functionally related internal fluctuations in human ileal bile acid-binding protein by high pressure nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2026Article
- Structural and Dynamic Determinants of Molecular Recognition in Bile Acid-Binding Proteins.International journal of molecular sciences · 2022Review
- Long-range Regulation of Partially Folded Amyloidogenic Peptides.Scientific reports · 2020Article
- Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment.Protein science : a publication of the Protein Society · 2019Article
- Local and non-local topological information in the denatured state ensemble of a β-barrel protein.Protein science : a publication of the Protein Society · 2018Article
- Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Cell reports · 2015Article
- Energy landscapes of functional proteins are inherently risky.Nature chemical biology · 2014Article
- Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein.Biochemistry · 2013Article
- The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-Sheets.Journal of molecular biology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein folding and aggregation inevitably compete with one another. This competition is even keener for proteins with frustrated landscapes, such as those rich in β structure. It is interesting that, despite their rugged energy landscapes and high β sheet content, intracellular lipid-binding proteins (iLBPs) appear to successfully avoid aggregation, as they are not implicated in aggregation diseases. In this study, we used a canonical iLBP, cellular retinoic acid-binding protein 1 (CRABP1), to understand better how folding is favored over aggregation. Analysis of folding kinetics of point mutants reveals that the folding pathway of CRABP1 involves early barrel closure. This folding mechanism protects sequences in CRABP1 that comprise cores of aggregates as identified by nuclear magnetic resonance. The amino acid conservation pattern in other iLBPs suggests that early barrel closure may be a general strategy for successful folding and minimization of aggregation. We suggest that folding mechanisms in general may incorporate steps that disfavor aggregation.
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