ArticleProtein science : a publication of the Protein Society2010
Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 53 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
- α-Crystallin Domains of Five Human Small Heat Shock Proteins (sHsps) Differ in Dimer Stabilities and Ability to Incorporate Themselves into Oligomers of Full-Length sHsps.International journal of molecular sciences · 2023Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- A weakened interface in the P182L variant of HSP27 associated with severe Charcot-Marie-Tooth neuropathy causes aberrant binding to interacting proteins.The EMBO journal · 2021Article
- Structural aspects of the human small heat shock proteins related to their functional activities.Cell stress & chaperones · 2020Review
- Hydrophobic residues of melittin mediate its binding to αA-crystallin.Protein science : a publication of the Protein Society · 2020Article
- The structure and oxidation of the eye lens chaperone αA-crystallin.Nature structural & molecular biology · 2019Article
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity.Structure (London, England : 1993) · 2018Article
- An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins.Cell stress & chaperones · 2017Article
- Proline isomerization in the C-terminal region of HSP27.Cell stress & chaperones · 2017Article
- Alpha-crystallin-derived peptides as therapeutic chaperones.Biochimica et biophysica acta · 2016Review
- Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.Biochemistry · 2015Article
- Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells.Progress in biophysics and molecular biology · 2014Review
- The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones.Journal of molecular biology · 2013Article
- Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the α-crystallin domain.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Evolution of crystallins for a role in the vertebrate eye lens.Protein science : a publication of the Protein Society · 2013Review
- Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry.Cell stress & chaperones · 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
2 authors at 1 institution in 1 country.
Funding
Abstract
In previous work on truncated alpha crystallins (Laganowsky et al., Protein Sci 2010; 19:1031-1043), we determined crystal structures of the alpha crystallin core, a seven beta-stranded immunoglobulin-like domain, with its conserved C-terminal extension. These extensions swap into neighboring cores forming oligomeric assemblies. The extension is palindromic in sequence, binding in either of two directions. Here, we report the crystal structure of a truncated alphaA crystallin (AAC) from zebrafish (Danio rerio) revealing C-terminal extensions in a non three-dimensional (3D) domain swapped, "closed" state. The extension is quasi-palindromic, bound within its own zebrafish core domain, lying in the opposite direction to that of bovine AAC, which is bound within an adjacent core domain (Laganowsky et al., Protein Sci 2010; 19:1031-1043). Our findings establish that the C-terminal extension of alpha crystallin proteins can be either 3D domain swapped or non-3D domain swapped. This duality provides another molecular mechanism for alpha crystallin proteins to maintain the polydispersity that is crucial for eye lens transparency.
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.