Evidence map›Paper›PMID 27686973›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

TEMPO-Assisted Free Radical-Initiated Peptide Sequencing Mass Spectrometry (FRIPS MS) in Q-TOF and Orbitrap Mass Spectrometers: Single-Step Peptide Backbone Dissociations in Positive Ion Mode.

Inae Jang, Sun Young Lee, Song Hwangbo, Dukjin Kang, Hookeun Lee, Hugh I Kim, Bongjin Moon, Han Bin Oh

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Ion Mobility-Assisted Free Radical-Initiated Peptide Sequencing.International journal of mass spectrometry · 2025
    Article
  3. Improved Performance of Positive-Ion Mode Free Radical-Initiated Peptide Sequencing withJournal of the American Society for Mass Spectrometry · 2023
    Article
  4. Free Radical-Based Sequencing for Native Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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

8 authors.

Inae JangDepartment of Chemistry, Sogang University, Seoul, 04107, Korea.
Sun Young LeeCollege of Pharmacy, Kyung Hee University, Seoul, 02447, Korea.
Song HwangboDepartment of Chemistry, Sogang University, Seoul, 04107, Korea.
Dukjin KangCenter for Bioanalysis, Division of Metrology for Quality of Life, Korea Research Institute of Standards and Science, Daejeon, 34113, Korea.
Hookeun LeeGachon Institute of Pharmaceutical Sciences, Gachon University, Incheon, 21936, Korea.
Hugh I KimDepartment of Chemistry, Korea University, Seoul, 02841, Korea.
Bongjin MoonDepartment of Chemistry, Sogang University, Seoul, 04107, Korea.
Han Bin OhDepartment of Chemistry, Sogang University, Seoul, 04107, Korea. hanbinoh@sogang.ac.kr.ORCID 0000-0001-7919-0393

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study demonstrates that one-step peptide backbone fragmentations can be achieved using the TEMPO [2-(2,2,6,6-tetramethyl piperidine-1-oxyl)]-assisted free radical-initiated peptide sequencing (FRIPS) mass spectrometry in a hybrid quadrupole time-of-flight (Q-TOF) mass spectrometer and a Q-Exactive Orbitrap instrument in positive ion mode, in contrast to two-step peptide fragmentation in an ion-trap mass spectrometer (reference Anal. Chem. 85, 7044-7051 (30)). In the hybrid Q-TOF and Q-Exactive instruments, higher collisional energies can be applied to the target peptides, compared with the low collisional energies applied by the ion-trap instrument. The higher energy deposition and the additional multiple collisions in the collision cell in both instruments appear to result in one-step peptide backbone dissociations in positive ion mode. This new finding clearly demonstrates that the TEMPO-assisted FRIPS approach is a very useful tool in peptide mass spectrometry research. Graphical Abstract ᅟ.

Indexed as

Amino Acid SequenceAnimalsBradykininCattleCyclic N-OxidesCytochromes cFree RadicalsPeptide FragmentsPeptidesSequence Analysis, ProteinTandem Mass SpectrometryBradykininCyclic N-OxidesCytochromes cFree RadicalsPeptide FragmentsPeptidesTEMPOFree radical-initiated peptide sequencing (FRIPS)OrbitrapQ-TOFRadical-based fragmentationsTEMPO

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Registered trials

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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.