Evidence map›Paper›PMID 22065406›Full record

ArticleJournal of the American Society for Mass Spectrometry2012

Pathways for water loss from doubly protonated peptides containing serine or threonine.

Alex G Harrison

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Gas phase chemistry of Li+ with amides: the observation of LiOH loss in mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Alex G HarrisonDepartment of Chemistry, University of Toronto, 80 St. George Street, Toronto, ON, M5S 3H6, Canada. aharriso@chem.utoronto.ca

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The doubly-protonated peptides Ala-Ala-Xaa-Ala-Ala-Ala-Arg show extensive loss of H(2)O when Xaa = Ser or Thr. Using quasi-MS(3) techniques the fragmentation reactions of the [M + 2H - H(2)O](+2) ions have been studied in detail. For both Ser and Thr, the [M + 2H - H(2)O](+2) ions show three primary fragmentation reactions, elimination of CH(3)CH=NH, elimination of one Ala residue, and elimination of two Ala residues, in all cases forming doubly-charged products. From a study of the further fragmentation of these products, it is concluded that elimination of two Ala residues results in formation of a three-membered aziridine ring by interaction with the adjacent amide function as H(2)O is lost. The elimination of one Ala residue results in formation of a five-membered oxazoline ring through interaction with the N-terminal adjacent carbonyl function as H(2)O is lost. The elimination of CH(3)CH=NH appears to involve formation of an eight-membered ring by interaction with the remote N-terminal carbonyl function as H(2)O is lost. However, this initial structure undergoes rearrangement through interaction with the adjacent C-terminal carbonyl function prior to further fragmentation. The [MH - H(2)O](+) ion of Ala-Ala-Ser-Ala-Ala-Ala also shows elimination of CH(3)CH=NH, one Ala residue and two Ala residues.

Indexed as

ProtonsAziridinesIonsOligopeptidesSerineTandem Mass SpectrometryThreonineWateraziridineAziridinesIonsOligopeptidesProtonsSerineThreonineWater

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.