ReviewMass spectrometry (Tokyo, Japan)2016
MALDI In-Source Decay of Protein: The Mechanism of c-Ion Formation.
Review in Mass spectrometry (Tokyo, Japan), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Isolation and partial characterization of antimicrobial peptide-enriched fractions from Parabacteroides distasonis.Scientific reports · 2025Article
- Peptide Analysis by Soft X-ray Atmospheric Pressure Photoionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025Article
- Top-Down Identification and Sequence Analysis of Small Membrane Proteins Using MALDI-MS/MS.Journal of the American Society for Mass Spectrometry · 2022Article
- Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy.Journal of biomolecular NMR · 2021Article
- Evaluation of Sibling and Twin Fragment Ions Improves the Structural Characterization of Proteins by Top-Down MALDI In-Source Decay Mass Spectrometry.Analytical chemistry · 2020Article
- Physicochemical study of natural fractionated biocolloid by asymmetric flow field-flow fractionation in tandem with various complementary techniques using biologically synthesized silver nanocomposites.Analytical and bioanalytical chemistry · 2018Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The in-source decay (ISD) phenomenon, the fragmentation at an N-Cα bond of a peptide backbone that occurs within several tens of nanoseconds in the ion-source in matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS), is discussed from the standpoints of the discovery and early publications dealing with MALDI-ISD, the formation of c-ions in energy-sudden desorption/ionization methods, the formation of radical species in a MALDI, model construction for ISD, and matrix materials that are suitable for use in MALDI-ISD. The formation of c-ions derived from peptides and proteins in MALDI-ISD can be rationalized by a mechanism involving intermolecular hydrogen transfer, denoted as the "Takayama's model" by De Pauw's group (Anal. Chem. 79: 8678-8685, 2007). It should be emphasized that the model for MALDI-ISD was constructed on the basis of X-ray crystallography and scanning probe microscopy (SPM) analyses of matrix crystals, as well as the use of isotopically-labelled peptides.
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Registered trials
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