ArticleInternational journal of mass spectrometry2012
Mass spectrometry-based carboxyl footprinting of proteins: method evaluation.
Article in International journal of mass spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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
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Who cites it
39 citing papers in PubMed.
- A SWI/SNF-specific Ig-like domain, SWIFT, is a transcription factor binding platform.Science (New York, N.Y.) · 2026Article
- Covalent modification of a glutamic acid inspired by HaloTag technology.Nature communications · 2026Article
- Targeting a Glutamic Acid in PDEδ with Fluoromethyl-Aryl Electrophiles Impairs K-Ras Signaling.Journal of medicinal chemistry · 2026Article
- Mass spectrometry footprinting reveals microsomal CYP2A6 structural changes induced by interaction with its reductase flavin mononucleotide domain.Drug metabolism and disposition: the biological fate of chemicals · 2026Article
- Mass-Spectrometry-Based GEE Footprinting Characterizes Kinetic Mechanisms and Sites of Conformational Change in Amyloid β 1-42 Aggregation.ACS chemical neuroscience · 2025Article
- Strategies for Acid and Amine Cross-linking and Labeling for Protein Structural Characterization Using Mass Spectrometry.Analytical chemistry · 2025Article
- Mass Spectrometry-Based Protein Footprinting Defines the Binding Pocket of Crotonylated H3K14 in the PHD1 Domain of BAF45D within the BAF Chromatin Remodeling Complex.ACS bio & med chem Au · 2024Article
- Evaluating Chemical Footprinting-Induced Perturbation of Protein Higher Order Structure.Analytical chemistry · 2024Article
- Toward a MALDI in-source decay (ISD) method for top-down analysis of protein footprinting.European journal of mass spectrometry (Chichester, England) · 2023Article
- Intact mass spectrometry screening to optimize hydroxyl radical dose for protein footprinting.Biochemical and biophysical research communications · 2023Article
- Workflow for Validating Specific Amino Acid Footprinting Reagents for Protein Higher Order Structure Elucidation.Analytical chemistry · 2023Article
- Advances in Mass Spectrometry on Membrane Proteins.Membranes · 2023Review
- Probing Monotopic Phosphoglycosyl Transferases from Complex Cellular Milieu.ACS chemical biology · 2022Article
- Automated Specific Amino Acid Footprinting Mass Spectrometry: Repurposing an HDX Platform for Determining Reagent Feasibility.Analytical chemistry · 2022Article
- Mass Spectrometry-Based Structural Proteomics for Metal Ion/Protein Binding Studies.Biomolecules · 2022Review
- GABARAP sequesters the FLCN-FNIP tumor suppressor complex to couple autophagy with lysosomal biogenesis.Science advances · 2021Article
- THE MAKING OF A FOOTPRINT IN PROTEIN FOOTPRINTING: A REVIEW IN HONOR OF MICHAEL L. GROSS.Mass spectrometry reviews · 2021Review
- Parallel Chemoselective Profiling for Mapping Protein Structure.Cell chemical biology · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- The Application of Fluorine-Containing Reagents in Structural Proteomics.Angewandte Chemie (International ed. in English) · 2020Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Protein structure determines function in biology, and a variety of approaches have been employed to obtain structural information about proteins. Mass spectrometry-based protein footprinting is one fast-growing approach. One labeling-based footprinting approach is the use of a water-soluble carbodiimide, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and glycine ethyl ester (GEE) to modify solvent-accessible carboxyl groups on glutamate (E) and aspartate (D). This paper describes method development of carboxyl-group modification in protein footprinting. The modification protocol was evaluated by using the protein calmodulin as a model. Because carboxyl-group modification is a slow reaction relative to protein folding and unfolding, there is an issue that modifications at certain sites may induce protein unfolding and lead to additional modification at sites that are not solvent-accessible in the wild-type protein. We investigated this possibility by using hydrogen deuterium amide exchange (H/DX). The study demonstrated that application of carboxyl group modification in probing conformational changes in calmodulin induced by Ca(2+) binding provides useful information that is not compromised by modification-induced protein unfolding.
Identifiers
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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.