ArticleJournal of the American Society for Mass Spectrometry2013
Electron capture dissociation of trivalent metal ion-peptide complexes.
Article in Journal of the American Society for Mass Spectrometry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed.
- Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Electron transfer dissociation mass spectrometry of acidic phosphorylated peptides cationized with trivalent praseodymium.Journal of mass spectrometry : JMS · 2018Article
- Replacing HChemical science · 2018Article
- Native electrospray mass spectrometry approaches to probe the interaction between zinc and an anti-angiogenic peptide from histidine-rich glycoprotein.Scientific reports · 2018Article
- Electron Transfer Dissociation and Collision-Induced Dissociation of Underivatized Metallated Oligosaccharides.Journal of the American Society for Mass Spectrometry · 2018Article
- Formation and Fragmentation Chemistry of Tripositive Ln(TMGA)Journal of the American Society for Mass Spectrometry · 2017Article
- Effects of acidic peptide size and sequence on trivalent praseodymium adduction and electron transfer dissociation mass spectrometry.Journal of mass spectrometry : JMS · 2017Article
- The Effects of Trivalent Lanthanide Cationization on the Electron Transfer Dissociation of Acidic Fibrinopeptide B and its Analogs.Journal of the American Society for Mass Spectrometry · 2016Article
- Difference of Electron Capture and Transfer Dissociation Mass Spectrometry on Ni(2+)-, Cu(2+)-, and Zn(2+)-Polyhistidine Complexes in the Absence of Remote Protons.Journal of the American Society for Mass Spectrometry · 2016Article
- The Competitive influence of Li+, Na+, K+, Ag+, and H+ on the fragmentation of a PEGylated polymeric excipient.Journal of the American Society for Mass Spectrometry · 2015Article
- Mechanistic study on electron capture dissociation of the oligosaccharide-Mg²⁺ complex.Journal of the American Society for Mass Spectrometry · 2014Article
- Influence of metal-peptide complexation on fragmentation and inter-fragment hydrogen migration in electron transfer dissociation.Journal of the American Society for Mass Spectrometry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
With electrospray ionization from aqueous solutions, trivalent metal ions readily adduct to small peptides resulting in formation of predominantly (peptide + M(T) - H)(2+), where M(T) = La, Tm, Lu, Sm, Ho, Yb, Pm, Tb, or Eu, for peptides with molecular weights below ~1000 Da, and predominantly (peptide + M(T))(3+) for larger peptides. ECD of (peptide + M(T) - H)(2+) results in extensive fragmentation from which nearly complete sequence information can be obtained, even for peptides for which only singly protonated ions are formed in the absence of the metal ions. ECD of these doubly charged complexes containing M(T) results in significantly higher electron capture efficiency and sequence coverage than peptide-divalent metal ion complexes that have the same net charge. Formation of salt-bridge structures in which the metal ion coordinates to a carboxylate group are favored even for (peptide + M(T))(3+). ECD of these latter complexes for large peptides results in electron capture by the protonation site located remotely from the metal ion and predominantly c/z fragments for all metals, except Eu(3+), which undergoes a one electron reduction and only loss of small neutral molecules and b/y fragments are formed. These results indicate that solvation of the metal ion in these complexes is extensive, which results in the electrochemical properties of these metal ions being similar in both the peptide environment and in bulk water.
Indexed as
Identifiers
What OpenQuestion holds
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.