ArticleThe Journal of biological chemistry2015
Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- 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
- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.bioRxiv : the preprint server for biology · 2026Article
- Enzyme-free biochemical production of seamlessly N-to-C cyclized peptides from natural or recombinant proteins.bioRxiv : the preprint server for biology · 2025Article
- Enzyme-free biochemical production of seamlessly N-to-C cyclized peptides from natural or recombinant proteins.Methods in enzymology · 2025Article
- Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solution.Protein science : a publication of the Protein Society · 2024Article
- Review
- Network Hamiltonian Models for Unstructured Protein Aggregates, with Application to γD-Crystallin.The journal of physical chemistry. B · 2023Article
- Article
- Redox chemistry of lens crystallins: A system of cysteines.Experimental eye research · 2021Review
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Aggregation pathways of human γ D crystallin induced by metal ions revealed by time dependent methods.PeerJ · 2020Article
- Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation.The Journal of biological chemistry · 2018Article
- Reactive cysteine residues in the oxidative dimerization and CuBiochimica et biophysica acta. Molecular basis of disease · 2018Article
- Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Investigative ophthalmology & visual science · 2017Article
- An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin.The Journal of biological chemistry · 2016Article
- Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Protein science : a publication of the Protein Society · 2016Article
- Biophysical chemistry of the ageing eye lens.Biophysical reviews · 2015Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Non-native protein conformers generated by mutation or chemical damage template aggregation of wild-type, undamaged polypeptides in diseases ranging from amyotrophic lateral sclerosis to cancer. We tested for such interactions in the natively monomeric human eye lens protein γd-crystallin, whose aggregation leads to cataract disease. The oxidation-mimicking W42Q mutant of γd-crystallin formed non-native polymers starting from a native-like state under physiological conditions. Aggregation occurred in the temperature range 35-45 °C, in which the mutant protein began to lose the native conformation of its N-terminal domain. Surprisingly, wild-type γd-crystallin promoted W42Q polymerization in a catalytic manner, even at mutant concentrations too low for homogeneous nucleation to occur. The presence of wild-type protein also downshifted the temperature range of W42Q aggregation. W42Q aggregation required formation of a non-native intramolecular disulfide bond but not intermolecular cross-linking. Transient WT/W42Q binding may catalyze this oxidative misfolding event in the mutant. That a more stable variant in a mixture can specifically promote aggregation of a less stable one rationalizes how extensive aggregation of rare damaged polypeptides can occur during the course of aging.
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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.