ReviewThe Journal of biological chemistry2014
Ca2+-binding motif of βγ-crystallins.
Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.
- Physiological and pathological functions of βB2-crystallins in multiple organs: a systematic review.Aging · 2021Pooled it
- The calcium signal regulatory network and the roles of calcium-binding proteins in bacteria.World journal of microbiology & biotechnology · 2026Review
- The Mammalian Ocular Lens in Focus: Development, Anatomy, Physiology, Transparency, Biomechanics, and Age-related Challenges.Journal of visualized experiments : JoVE · 2026Review
- Analysis of mouse lens morphological and proteomic abnormalities following deletion of the βB3-crystallin promoter.Experimental eye research · 2025Article
- Tissue, cellular, and molecular level determinants for eye lens stiffness and elasticity.Frontiers in ophthalmology · 2024Review
- Article
- Replica exchange molecular dynamics simulations reveal self-association sites in M-crystallin caused by mutations provide insights of cataract.Scientific reports · 2021Article
- Crystallin gene expression: Insights from studies of transcriptional bursting.Experimental eye research · 2021Review
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- βγ-Crystallination Endows a Novel Bacterial Glycoside Hydrolase 64 with CaJournal of bacteriology · 2019Article
- Divalent Cations and the Divergence ofBiochemistry · 2019Article
- Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.Biophysical journal · 2019Article
- Crybb2 Mutations Consistently Affect Schizophrenia Endophenotypes in Mice.Molecular neurobiology · 2019Article
- Interrelation of CaJournal of biosciences · 2019Review
- Bidirectional Analysis of Cryba4-Crybb1 Nascent Transcription and Nuclear Accumulation of Crybb3 mRNAs in Lens Fibers.Investigative ophthalmology & visual science · 2019Article
- Acute lens opacity induced by different kinds of anesthetic drugs in mice.International journal of ophthalmology · 2019Article
- A Drosophila genetic model of nephrolithiasis: transcriptional changes in response to diet induced stone formation.BMC urology · 2017Article
- Evolutionary Origins of Pax6 Control of Crystallin Genes.Genome biology and evolution · 2017Article
- Identification of New Virulence Factors and Vaccine Candidates forFrontiers in cellular and infection microbiology · 2017Article
- Calcium Binding Dramatically Stabilizes an Ancestral Crystallin Fold in Tunicate βγ-Crystallin.Biochemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
βγ-Crystallin-type double clamp (N/D)(N/D)XX(S/T)S motif is an established but sparsely investigated motif for Ca(2+) binding. A βγ-crystallin domain is formed of two Greek key motifs, accommodating two Ca(2+)-binding sites. βγ-Crystallins make a separate class of Ca(2+)-binding proteins (CaBP), apparently a major group of CaBP in bacteria. Paralleling the diversity in βγ-crystallin domains, these motifs also show great diversity, both in structure and in function. Although the expression of some of them has been associated with stress, virulence, and adhesion, the functional implications of Ca(2+) binding to βγ-crystallins in mediating biological processes are yet to be elucidated.
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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.