ArticleJournal of the American Society for Mass Spectrometry2009
Painting proteins with covalent labels: what's in the picture?
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
16 citing papers in PubMed.
- Methionine Oxidation Footprinting in Intact Proteins (MOFIP) Using Top-Down Proteomics.Proteomics · 2025Article
- Self-assembled peptide-dye nanostructures for in vivo tumor imaging and photodynamic toxicity.Npj imaging · 2024Article
- Native Mass Spectrometry, Ion Mobility, Electron-Capture Dissociation, and Modeling Provide Structural Information for Gas-Phase Apolipoprotein E Oligomers.Journal of the American Society for Mass Spectrometry · 2019Article
- Content Is King: Databases Preserve the Collective Information of Science.Journal of biomolecular techniques : JBT · 2018Article
- Tracking the Catalytic Cycle of Adenylate Kinase by Ultraviolet Photodissociation Mass Spectrometry.Analytical chemistry · 2018Article
- Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly.Protein science : a publication of the Protein Society · 2015Article
- Limited proteolysis via millisecond digestions in protease-modified membranes.Analytical chemistry · 2012Article
- Validation of membrane protein topology models by oxidative labeling and mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Probing protein surface with a solvent mimetic carbene coupled to detection by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Mapping the protein-protein interface between a toxin and its cognate antitoxin from the bacterial pathogen Streptococcus pyogenes.Biochemistry · 2011Article
- Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions.Expert review of proteomics · 2011Review
- Fast photochemical oxidation of proteins for comparing structures of protein-ligand complexes: the calmodulin-peptide model system.Analytical chemistry · 2011Article
- Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
- Protein-peptide affinity determination using an h/d exchange dilution strategy: application to antigen-antibody interactions.Journal of the American Society for Mass Spectrometry · 2010Article
- Identification of tandem mass spectra of mixtures of isomeric peptides.Journal of proteome research · 2010Article
- Conversion of methionine into homocysteic acid in heavily oxidized proteomics samples.Rapid communications in mass spectrometry : RCM · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Knowledge about the structural and biophysical properties of proteins when they are free in solution and/or in complexes with other molecules is essential for understanding the biological processes that proteins regulate. Such knowledge is also important to drug discovery efforts, particularly those focused on the development of therapeutic agents with protein targets. In the last decade a variety of different covalent labeling techniques have been used in combination with mass spectrometry to probe the solution-phase structures and biophysical properties of proteins and protein-ligand complexes. Highlighted here are five different mass spectrometry-based covalent labeling strategies including: continuous hydrogen/deuterium (H/D) exchange labeling, hydroxyl radical-mediated footprinting, SUPREX (stability of unpurified proteins from rates of H/D exchange), PLIMSTEX (protein-ligand interaction by mass spectrometry, titration, and H/D exchange), and SPROX (stability of proteins from rates of oxidation). The basic experimental protocols used in each of the above-cited methods are summarized along with the kind of biophysical information they generate. Also discussed are the relative strengths and weaknesses of the different methods for probing the wide range of conformational states that proteins and protein-ligand complexes can adopt when they are in solution.
Indexed as
Identifiers
19269190What OpenQuestion holds
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.