ArticleExperimental eye research2012
Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin.
Article in Experimental eye research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- The α-crystallin Chaperones Undergo a Quasi-ordered Co-aggregation Process in Response to Saturating Client Interaction.Journal of molecular biology · 2024Article
- The significance of growth shells in development of symmetry, transparency, and refraction of the human lens.Frontiers in ophthalmology · 2024Review
- Eye lens β-crystallins are predicted by native ion mobility-mass spectrometry and computations to form compact higher-ordered heterooligomers.Structure (London, England : 1993) · 2023Article
- Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.Structure (London, England : 1993) · 2021Article
- Interaction of Alpha-Crystallin with Phospholipid Membranes.Current eye research · 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
- Altered Protein Dynamics and Increased Aggregation of Human γS-Crystallin Due to Cataract-Associated Deamidations.Biochemistry · 2019Article
- αA-crystallin-derived minichaperone stabilizes αAG98R-crystallin by affecting its zeta potential.Molecular vision · 2018Article
- Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen-deuterium exchange and deamidation.Biochimica et biophysica acta · 2016Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- Lens β-crystallins: the role of deamidation and related modifications in aging and cataract.Progress in biophysics and molecular biology · 2014Review
- Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants.Protein science : a publication of the Protein Society · 2014Article
- Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.Structure (London, England : 1993) · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Aberrant protein interactions can lead to aggregation and insolubilization, such as occurs during cataract formation. Deamidation, a prevalent age-related modification in the lens of the eye, decreases stability of the major lens proteins, crystallins. The mechanism of deamidation altering interactions between αA-crystallin and βB2-crystallin was investigated by detecting changes in solvent accessibility upon complex formation during heating. Solvent accessibility was determined by measuring hydrogen/deuterium exchange levels of backbone amides by high-resolution mass spectrometry. Deuterium levels in wild type βB2-crystallin increased 50-60% in both domains following complex formation with αA-crystallin. This increased solvent accessibility indicated a general loosening along the backbone amides. Peptides with the greatest deuterium increases were located at the buried monomer-monomer interface, suggesting that the βB2 dimer was disrupted. The only region where the deuterium levels decreased was in βB2 peptide 123-139, containing an outside loop, and may be a potential site of interaction with αA. Mimicking deamidation at the βB2 dimer interface prevented complex formation with αA. When temperatures were lowered, an αA/βB2 Q70E/Q162E complex formed with similar solvent accessibilities as αA/WT βB2. Deamidation did not disrupt specific αA/βB2 interactions but favored aggregation before complex formation with αA. We conclude that deamidation contributes to cataract formation through destabilization of crystallins before they can be rescued by α-crystallin.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.