1995
DOI: 10.1002/mas.1280140104
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The interpretation of collision‐induced dissociation tandem mass spectra of peptides

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Cited by 638 publications
(600 citation statements)
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References 113 publications
(39 reference statements)
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“…Mass spectrometry has been widely used in the structure elucidation of biomolecules including peptides [13][14][15]. The effect of an acidic amino acid, i.e., aspartic acid, glutamic acid, and Cys-SO 3 H, on the fragmentation of protonated peptide ions has been well studied [16 -22].…”
mentioning
confidence: 99%
“…Mass spectrometry has been widely used in the structure elucidation of biomolecules including peptides [13][14][15]. The effect of an acidic amino acid, i.e., aspartic acid, glutamic acid, and Cys-SO 3 H, on the fragmentation of protonated peptide ions has been well studied [16 -22].…”
mentioning
confidence: 99%
“…been thought to be acylium ions (Scheme 2) [1,2,4]. Later, it has been shown that the acylium ions are not stable and a N-protonated oxazolone structure (Scheme 2) is proposed for b n ions [13][14][15][16][17][18][19][20].…”
mentioning
confidence: 99%
“…Indeed, mass spectrometric de novo sequencing based on the fragmentation of derivitized peptide ions dates back to the late 1960s and on underivatized peptide ions to the early 1980s (reviewed in [2] and [3]). More recently, MS sequencing has been given considerable impetus by the development of ESI and MALDI, ionization techniques whose efficiencies for producing intact peptide ions are far higher than those that were previously available.…”
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confidence: 99%