ArticleAnalytical chemistry2014
Identification of amino acid epimerization and isomerization in crystallin proteins by tandem LC-MS.
Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 69 citations in OpenAlex.
- Spontaneous Isomerization of Tau is Most Prevalent in Alzheimer's Disease.NeuroMarkers · 2026Article
- Detection and functional assessment of D-amino acids as potential biomarkers in neurological disorders.Molecular biology reports · 2025Review
- Deep Characterization of Isomerization in the Human Eye Lens Proteome by Crystallin-Depleted Data-Independent Acquisition.Aging cell · 2025Article
- Determination of Trends Underlying Aspartic Acid Isomerization in Intact Proteins Reveals Unusually Rapid Isomerization of Tau.ACS chemical neuroscience · 2025Article
- Unusually Rapid Isomerization of Aspartic Acid in Tau.bioRxiv : the preprint server for biology · 2024Article
- Localizing Isomerized Residue Sites in Peptides with Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Selective recognition and discrimination of single isomeric changes in peptide strands with a host : guest sensing array.Chemical science · 2024Article
- Variable fragmentation and ionization of amyloid-beta epimers and isomers.Analytical and bioanalytical chemistry · 2023Article
- Differentiation of Aspartic and Isoaspartic Acid Using 193 nm Ultraviolet Photodissociation Mass Spectrometry.Analytical chemistry · 2023Article
- Endogenous l- to d-amino acid residue isomerization modulates selectivity between distinct neuropeptide receptor family members.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Composite Multidimensional Ion Mobility-Mass Spectrometry for Improved Differentiation of Stereochemical Modifications.Analytical chemistry · 2023Article
- Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging.Structure (London, England : 1993) · 2022Article
- High-Resolution Demultiplexing (HRdm) Ion Mobility Spectrometry-Mass Spectrometry for Aspartic and Isoaspartic Acid Determination and Screening.Analytical chemistry · 2022Article
- Evaluation of endogenous peptide stereochemistry using liquid chromatography-mass spectrometry-based spiking experiments.Methods in enzymology · 2022Article
- Proteomic characterization of the human lens and Cataractogenesis.Expert review of proteomics · 2021Review
- Simultaneous and Rapid Detection of Multiple Epimers and Isomers of Aspartyl Residues in Lens Proteins Using an LC-MS-MRM Method.ACS omega · 2020Article
- Free-Radical-Mediated Glycan Isomer Differentiation.Analytical chemistry · 2020Article
- Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules.Chemical reviews · 2020Review
- Molecular basis for chirality-regulated Aβ self-assembly and receptor recognition revealed by ion mobility-mass spectrometry.Nature communications · 2019Article
- Chiral Differentiation of Non-Covalent Diastereomers Based on Multichannel Dissociation Induced by 213-nm Ultraviolet Photodissociation.Journal of the American Society for Mass Spectrometry · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Post-translational modifications that do not result in a change in mass are particularly difficult to detect by mass spectrometry. For example, isomerization of aspartic acid or epimerization of any chiral residue within a peptide do not lead to mass shifts but can be identified by examination of independently acquired tandem mass spectra or by combination with another technique. For analysis of a biological sample, this means that liquid chromatography or some other type of separation must be used to first separate the isomers from one another. Furthermore, each specific m/z of interest must be sampled repeatedly to allow for comparison of the tandem mass spectra from each separated isomer, which contrasts with the traditional approach in proteomics where the goal is typically to avoid resampling the same m/z. We illustrate that isomerization and epimerization of peptides can be identified in this fashion by examination of long-lived crystallin proteins extracted from a sheep eye lens. Tandem mass spectrometry relying on a combination of radical directed dissociation (RDD) and collision induced dissociation (CID) following separation by liquid chromatography was used to identify modified peptides. Numerous sites of isomerization and epimerization, including several that have not been previously identified, were determined with peptide specificity. It is demonstrated that the specific sites of amino acid isomerization within each peptide can be identified by comparison with synthetic peptides. For α-crystallin proteins, the sites that undergo the greatest degree of isomerization correspond to disordered regions, which may have important implications on chaperone functionality within the context of aging.
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