ArticleJournal of mass spectrometry : JMS2020
MALDI imaging mass spectrometry of β- and γ-crystallins in the ocular lens.
Article in Journal of mass spectrometry : JMS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Towards Cellular Resolution of Tryptic Peptides in Tissue Sections by MALDI MS Imaging: A Focus on Enzyme Application and Reproducibility.Analytical chemistry · 2026Article
- Matrix-Assisted Laser Desorption/Ionization Imaging Mass Spectrometry.Nature reviews. Methods primers · 2026Article
- An isotopically-labelled temporal mass spectrometry imaging data analysis workflow to reveal glucose spatial metabolism patterns in bovine lens tissue.Scientific reports · 2024Article
- Thiol-Mediated Enhancement of NACS chemical biology · 2024Article
- Review
- The effect of fibre cell remodelling on the power and optical quality of the lens.Journal of the Royal Society, Interface · 2023Article
- Article
- Manipulating polydispersity of lens β-crystallins using divalent cations demonstrates evidence of calcium regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens.The Journal of biological chemistry · 2022Review
- Cell-Instructive Surface Gradients of Photoresponsive Amyloid-like Fibrils.ACS biomaterials science & engineering · 2021Article
- Redox chemistry of lens crystallins: A system of cysteines.Experimental eye research · 2021Review
- The aging mouse lens transcriptome.Experimental eye research · 2021Article
- Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases.Redox biology · 2021Review
- Automated annotation and visualisation of high-resolution spatial proteomic mass spectrometry imaging data using HIT-MAP.Nature communications · 2021Article
- Novel technical developments in mass spectrometry imaging in 2020: A mini review.Analytical science advances · 2021Review
- Proteomic characterization of the human lens and Cataractogenesis.Expert review of proteomics · 2021Review
- Mass Spectrometry Analysis of Intact Proteins from Crude Samples.Analytical chemistry · 2020Article
- Localization of the lens intermediate filament switch by imaging mass spectrometry.Experimental eye research · 2020Article
- Mass spectrometry in ocular drug research.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Lens crystallin proteins make up 90% of expressed proteins in the ocular lens and are primarily responsible for maintaining lens transparency and establishing the gradient of refractive index necessary for proper focusing of images onto the retina. Age-related modifications to lens crystallins have been linked to insolubilization and cataractogenesis in human lenses. Matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) has been shown to provide spatial maps of such age-related modifications. Previous work demonstrated that, under standard protein IMS conditions, α-crystallin signals dominated the mass spectrum and age-related modifications to α-crystallins could be mapped. In the current study, a new sample preparation method was optimized to allow imaging of β- and γ-crystallins in ocular lens tissue. Acquired images showed that γ-crystallins were localized predominately in the lens nucleus whereas β-crystallins were primarily localized to the lens cortex. Age-related modifications such as truncation, acetylation, and carbamylation were identified and spatially mapped. Protein identifications were determined by top-down proteomics analysis of lens proteins extracted from tissue sections and analyzed by LC-MS/MS with electron transfer dissociation. This new sample preparation method combined with the standard method allows the major lens crystallins to be mapped by MALDI IMS.
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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.