Higher-energy C-trap dissociation for peptide modification analysis

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Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. (2013, methodology): “Peptides were fragmented using higher energy C-trap dissociation (HCD) fragmentation (Olsen et al., 2007).”
Deep proteome and transcriptome mapping of a human cancer cell line (2011, methodology): “Peptide MS spectra as well as fragment MS/MS spectra were measured with high resolution and mass accuracy (Mann and Kelleher, 2008; Olsen et al, 2007; Olsen et al, 2009).”
Decoding signalling networks by mass spectrometry-based proteomics (2010, background): “The recent introduction of higher energy collisional dissociation (HCD) has made a similar fragmentation mode to that in quadrupole TOF available to linear ion trap–orbitrap instruments, without diminishing sensitivit”
Mass Spectrometry-based Proteomics Using Q Exactive, a High-performance Benchtop Quadrupole Orbitrap Mass Spectrometer (2011, neutral): “fragmentation (19) albeit without mass selection.”
A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles (2011, methodology): “The ion selection threshold was 5,000 counts for HCD and CID.”
Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions (2009, methodology): “Briefly, the LTQ Orbitrap XL instrument (Olsen et al., 2007) under Xcalibur 2.”