Evidence map›Paper›PMID 26545767›Full record

ArticleJournal of the American Society for Mass Spectrometry2016

213 nm Ultraviolet Photodissociation on Peptide Anions: Radical-Directed Fragmentation Patterns.

Mohammad A Halim, Marion Girod, Luke MacAleese, Jérôme Lemoine, Rodolphe Antoine, Philippe Dugourd

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Peptide Analysis by Soft X-ray Atmospheric Pressure Photoionization Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025
    Article
  2. Photolysis of the peptide bond at 193 and 222 nm.The Journal of chemical physics · 2025
    Article
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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

6 authors at 3 institutions in 1 country.

Mohammad A HalimInstitut Lumière Matière, Université Lyon 1 - CNRS, Université de Lyon, 69622, Villeurbanne Cedex, France.
Marion GirodInstitut des Sciences Analytiques, Université Lyon 1 - CNRS, Université de Lyon, 69622, Villeurbanne Cedex, France.
Luke MacAleeseInstitut Lumière Matière, Université Lyon 1 - CNRS, Université de Lyon, 69622, Villeurbanne Cedex, France.
Jérôme LemoineInstitut des Sciences Analytiques, Université Lyon 1 - CNRS, Université de Lyon, 69622, Villeurbanne Cedex, France.
Rodolphe AntoineInstitut Lumière Matière, Université Lyon 1 - CNRS, Université de Lyon, 69622, Villeurbanne Cedex, France.
Philippe DugourdInstitut Lumière Matière, Université Lyon 1 - CNRS, Université de Lyon, 69622, Villeurbanne Cedex, France. phillipe.dugourd@univ-lyon1.fr.
Université Claude Bernard Lyon 1 · FRCentre National de la Recherche Scientifique · FRInstitut des Sciences Analytiques · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Characterization of acidic peptides and proteins is greatly hindered due to lack of suitable analytical techniques. Here we present the implementation of 213 nm ultraviolet photodissociation (UVPD) in high-resolution quadrupole-Orbitrap mass spectrometer in negative polarity for peptide anions. Radical-driven backbone fragmentation provides 22 distinctive fragment ion types, achieving the complete sequence coverage for all reported peptides. Hydrogen-deficient radical anion not only promotes the cleavage of Cα-C bond but also stimulates the breaking of N-Cα and C-N bonds. Radical-directed loss of small molecules and specific side chain of amino acids are detected in these experiments. Radical containing side chain of amino acids (Tyr, Ser, Thr, and Asp) may possibly support the N-Cα backbone fragmentation. Proline comprising peptides exhibit the unusual fragment ions similar to reported earlier. Interestingly, basic amino acids such as Arg and Lys also stimulated the formation of abundant b and y ions of the related peptide anions. Loss of hydrogen atom from the charge-reduced radical anion and fragment ions are rationalized by time-dependent density functional theory (TDDFT) calculation, locating the potential energy surface (PES) of ππ* and repulsive πσ* excited states of a model amide system.

Indexed as

PhotolysisAmino Acid SequenceIonsMass SpectrometryModels, MolecularPeptidesUltraviolet RaysIonsPeptidesPeptidePhoto-fragmentationRadical anionsTDDFTUVPD

Identifiers

PMID26545767
OpenAlexW2228191085

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.