Evidence map›Paper›PMID 28980177›Full record

ArticleJournal of the American Society for Mass Spectrometry2018

Ultraviolet, Infrared, and High-Low Energy Photodissociation of Post-Translationally Modified Peptides.

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

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

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  7. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
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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 5 institutions in 1 country.

Mohammad A HalimUniversité de Lyon, Université Claude Bernard Lyon 1, CNRS, Institut Lumière Matière, F-69622, Lyon, France.
Luke MacAleeseUniversité de Lyon, Université Claude Bernard Lyon 1, CNRS, Institut Lumière Matière, F-69622, Lyon, France.
Jérôme LemoineUniversité de Lyon, Institut des Sciences Analytiques, UMR 5280, CNRS, Université Lyon 1, ENS Lyon, 69622, Villeurbanne, Cedex, France.
Rodolphe AntoineUniversité de Lyon, Université Claude Bernard Lyon 1, CNRS, Institut Lumière Matière, F-69622, Lyon, France.
Philippe DugourdUniversité de Lyon, Université Claude Bernard Lyon 1, CNRS, Institut Lumière Matière, F-69622, Lyon, France. philippe.dugourd@univ-lyon1.fr.ORCID 0000-0003-4395-1140
Marion GirodUniversité de Lyon, Institut des Sciences Analytiques, UMR 5280, CNRS, Université Lyon 1, ENS Lyon, 69622, Villeurbanne, Cedex, France.
Centre National de la Recherche Scientifique · FRÉcole Normale Supérieure de Lyon · FRInstitut des Sciences Analytiques · FRInstitut Lumière Matière · FRUniversité Claude Bernard Lyon 1 · FR

Funding

FP7 Ideas: European Research Council FP7 / 320659
6 · The paper itself

Abstract

Mass spectrometry-based methods have made significant progress in characterizing post-translational modifications in peptides and proteins; however, certain aspects regarding fragmentation methods must still be improved. A good technique is expected to provide excellent sequence information, locate PTM sites, and retain the labile PTM groups. To address these issues, we investigate 10.6 μm IRMPD, 213 nm UVPD, and combined UV and IR photodissociation, known as HiLoPD (high-low photodissociation), for phospho-, sulfo-, and glyco-peptide cations. IRMPD shows excellent backbone fragmentation and produces equal numbers of N- and C-terminal ions. The results reveal that 213 nm UVPD and HiLoPD methods can provide diverse backbone fragmentation producing a/x, b/y, and c/z ions with excellent sequence coverage, locate PTM sites, and offer reasonable retention efficiency for phospho- and glyco-peptides. Excellent sequence coverage is achieved for sulfo-peptides and the position of the SO

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceGlycopeptidesInfrared RaysMass SpectrometryPeptidesPhosphopeptidesPhotolysisSulfurUltraviolet RaysGlycopeptidesPeptidesPhosphopeptidesSulfurFragmentation methodIRMPDPhotofragmentationPost-translational modificationsUVPD

Identifiers

PMID28980177
OpenAlexW2761611851

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.