Succinylation of cytochrome c investigated by electrospray ionization mass spectrometry: Reactive lysine residues
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,Spectroscopy,Condensed Matter Physics,Instrumentation
Reference36 articles.
1. Analysis by Capillary Electrophoresis of the Kinetics of Charge Ladder Formation for Bovine Carbonic Anhydrase
2. Stepwise modification of the electrostatic charge of cytochrome c. Effects on protein conformation and oxidation-reduction properties.
3. Effect of chemical modification of lysine amino groups on redox and protonmotive activity of bovine heart cytochrome c oxidase reconstituted in phospholipid membranes
4. Effect on protein stability of reversing the charge on amino groups
5. Measurement of Electrostatic Interactions in Protein Folding with the Use of Protein Charge Ladders
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1. Cytochrome c prompts the recruitment of its nuclear partners SET/TAF-Iβ and NPM1 into biomolecular condensates;iScience;2024-08
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4. Induction of protein conformational change inside the charged electrospray droplet;Journal of Mass Spectrometry;2013-01-29
5. Selective Deletion of the Internal Lysine Residue from the Peptide Sequence by Collisional Activation;Journal of the American Society for Mass Spectrometry;2012-08-25
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