ArticleBiophysical journal2007
Analysis of the oxidative damage-induced conformational changes of apo- and holocalmodulin by dose-dependent protein oxidative surface mapping.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
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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
25 citing papers in PubMed, 59 citations in OpenAlex.
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- Inline Liquid Chromatography-Fast Photochemical Oxidation of Proteins for Targeted Structural Analysis of Conformationally Heterogeneous Mixtures.Analytical chemistry · 2021Article
- Aberrant Membrane Composition and Biophysical Properties Impair Erythrocyte Morphology and Functionality in Elliptocytosis.Biomolecules · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Top-Down ETD-MS Provides Unreliable Quantitation of Methionine Oxidation.Journal of biomolecular techniques : JBT · 2019Article
- Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactions.Methods (San Diego, Calif.) · 2018Review
- Modifications generated by fast photochemical oxidation of proteins reflect the native conformations of proteins.Protein science : a publication of the Protein Society · 2018Article
- Improved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.Journal of the American Society for Mass Spectrometry · 2013Article
- Comparative informatics analysis to evaluate site-specific protein oxidation in multidimensional LC-MS/MS data.Journal of proteome research · 2013Article
- Experimental approach to controllably vary protein oxidation while minimizing electrode adsorption for boron-doped diamond electrochemical surface mapping applications.Analytical chemistry · 2013Article
- Article
- Modeling of the DNA-binding site of yeast Pms1 by mass spectrometry.DNA repair · 2011Article
- Fast photochemical oxidation of proteins for comparing structures of protein-ligand complexes: the calmodulin-peptide model system.Analytical chemistry · 2011Article
- Future directions of structural mass spectrometry using hydroxyl radical footprinting.Journal of mass spectrometry : JMS · 2010Review
- 'Fixed charge' chemical derivatization and data dependant multistage tandem mass spectrometry for mapping protein surface residue accessibility.Journal of the American Society for Mass Spectrometry · 2010Article
- Visualizing water molecules in transmembrane proteins using radiolytic labeling methods.Biochemistry · 2010Review
- Integrated algorithms for high-throughput examination of covalently labeled biomolecules by structural mass spectrometry.Analytical chemistry · 2009Article
- Fast photochemical oxidation of protein footprints faster than protein unfolding.Analytical chemistry · 2009Article
- Painting proteins with covalent labels: what's in the picture?Journal of the American Society for Mass Spectrometry · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Calmodulin (CaM) is known to undergo conformational and functional changes on oxidation, allowing CaM to function as an oxidative stress sensor. We report the use of a novel mass spectrometry-based methodology to monitor the structure of apo- and holo-CaM as it undergoes conformational changes as a result of increasing amounts of oxidative damage. The kinetics of oxidation for eight peptides are followed by mass spectrometry, and 12 sites of oxidation are determined by MS/MS. Changes in the pseudo-first-order rate constant of oxidation for a peptide after increasing radiation exposure reveal changes in the accessibility of the peptide to the diffusing hydroxyl radical, indicating conformational changes as a function of increased oxidative damage. For holo-CaM, most sites rapidly become less exposed to hydroxyl radicals as the protein accumulates oxidative damage, indicating a closing of the hydrophobic pockets in the N- and C-terminal lobes. For apo-CaM, many of the sites rapidly become more exposed until they resemble the solvent accessibility of holo-CaM in the native structure and then rapidly become more buried, mimicking the conformational changes of holo-CaM. At the most heavily damaged points measured, the rates of oxidation for both apo- and holo-CaM are essentially identical, suggesting the two assume similar structures.
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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.