ArticleNature communications2017
Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.The Journal of biological chemistry · 2026Article
- Small bites for big problems: stepwise aggregate degradation by autophagy.Biochemical Society transactions · 2026Review
- Mimicking oxidative damage in γS-crystallin with site-specific incorporation of 5-hydroxytryptophan.Biophysical reports · 2026Article
- SOuLMuSiC, a novel tool for predicting the impact of mutations on protein solubility.Scientific reports · 2025Article
- Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Revealing the Local Structure and Dynamics of the Solid Li Ion Conductor LiChemistry of materials : a publication of the American Chemical Society · 2024Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Review
- Agglomeration: when folded proteins clump together.Biophysical reviews · 2023Review
- Congenital coralliform cataract is the predominant consequence of a recurrent mutation in the CRYGD gene.Orphanet journal of rare diseases · 2023Article
- Network Hamiltonian Models for Unstructured Protein Aggregates, with Application to γD-Crystallin.The journal of physical chemistry. B · 2023Article
- Mutant libraries reveal negative design shielding proteins from supramolecular self-assembly and relocalization in cells.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Sunset Yellow Dye Induces Amorphous Aggregation in β-Lactoglobulin at Acidic pH: A Multi-Techniques Approach.Polymers · 2022Article
- Meet the IUPAB councilor - Angela M. Gronenborn.Biophysical reviews · 2021Article
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Osmolytes and crowders regulate aggregation of the cancer-related L106R mutant of the Axin protein.Biophysical journal · 2021Article
- Sensitivity-Enhanced Solid-State NMR Detection of Structural Differences and Unique Polymorphs in Pico- to Nanomolar Amounts of Brain-Derived and Synthetic 42-Residue Amyloid-β Fibrils.Journal of the American Chemical Society · 2021Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.Structure (London, England : 1993) · 2021Article
- Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.Protein science : a publication of the Protein Society · 2020Article
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5 authors.
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Abstract
Cataracts cause vision loss through the large-scale aggregation of eye lens proteins as a result of ageing or congenital mutations. The development of new treatments is hindered by uncertainty about the nature of the aggregates and their mechanism of formation. We describe the structure and morphology of aggregates formed by the P23T human γD-crystallin mutant associated with congenital cataracts. At physiological pH, the protein forms aggregates that look amorphous and disordered by electron microscopy, reminiscent of the reported formation of amorphous deposits by other crystallin mutants. Surprisingly, solid-state NMR reveals that these amorphous deposits have a high degree of structural homogeneity at the atomic level and that the aggregated protein retains a native-like conformation, with no evidence for large-scale misfolding. Non-physiological destabilizing conditions used in many in vitro aggregation studies are shown to yield qualitatively different, highly misfolded amyloid-like fibrils.
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