ArticleAnalytical chemistry2013
Covalent labeling with isotopically encoded reagents for faster structural analysis of proteins by mass spectrometry.
Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Protein painting for structural and binding site analysisChemical science · 2024Article
- Structural characterization of protein-material interfacial interactions using lysine reactivity profiling-mass spectrometry.Nature protocols · 2023Review
- Quantitative structural proteomics in living cells by covalent protein painting.Methods in enzymology · 2023Article
- Cancer Conformational Landscape Shapes Tumorigenesis.Journal of proteome research · 2022Article
- Protein Footprinting via Covalent Protein Painting Reveals Structural Changes of the Proteome in Alzheimer's Disease.Journal of proteome research · 2021Article
- Global Profiling of Lysine Accessibility to Evaluate Protein Structure Changes in Alzheimer's Disease.Journal of the American Society for Mass Spectrometry · 2021Article
- Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021Review
- High Sensitivity Crosslink Detection Coupled With Integrative Structure Modeling in the Mass Spec Studio.Molecular & cellular proteomics : MCP · 2016Article
- Isotope-Encoded Carboxyl Group Footprinting for Mass Spectrometry-Based Protein Conformational Studies.Journal of the American Society for Mass Spectrometry · 2016Article
- Isotope-Coded Labeling for Accelerated Protein Interaction Profiling Using MS.Analytical chemistry · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Covalent labeling and mass spectrometry (MS) are increasingly being used to obtain higher-order structure of proteins and protein complexes. Because most covalent labels are relatively large, steps must be taken to ensure the structural integrity of the modified protein during the labeling reactions so that correct structural information can be obtained. Measuring labeling kinetics is a reliable way to ensure that a given labeling reagent does not perturb a protein's structure, but obtaining such kinetic information is time and sample intensive because it requires multiple liquid chromatography (LC)-MS experiments. Here we present a new strategy that uses isotopically encoded labeling reagents to measure labeling kinetics in a single LC-MS experiment. We illustrate this new strategy by labeling solvent-exposed lysine residues with commercially available tandem mass tags. After tandem MS experiments, these tags allow the simultaneous identification of modified sites and determination of the reaction rates at each site in a way that is just as reliable as experiments that involve multiple LC-MS measurements.
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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.