Evidence map›Paper›PMID 21952757›Full record

ArticleJournal of the American Society for Mass Spectrometry2011

Simultaneous identification of tyrosine phosphorylation and sulfation sites utilizing tyrosine-specific bromination.

Jong-Seo Kim, Si-Uk Song, Hie-Joon Kim

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Novel Concepts of MS-Cleavable Cross-linkers for Improved Peptide Structure Analysis.Journal of the American Society for Mass Spectrometry · 2017
    Article
  3. Review
  4. 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

3 authors at 1 institution in 2 countries.

Jong-Seo KimDepartment of Chemistry, Seoul National University, Seoul 151-742, Republic of Korea. jongseo.kim1@gmail.com
Si-Uk Song
Hie-Joon Kim
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosine phosphorylation and sulfation play many key roles in the cell. Isobaric phosphotyrosine and sulfotyrosine residues in peptides were determined by mass spectrometry using phosphatase or sulfatase to remove the phosphate or the sulfate group. Unique Br signature was introduced to the resulting tyrosine residues by incubation with 32% HBr at -20 °C for 20 min. MS/MS analysis of the brominated peptide enabled unambiguous determination of the phosphotyrosine and the sulfotyrosine sites. When phosphotyrosine and sulfotyrosine as well as free tyrosine were present in the same peptide, they could be determined simultaneously using either phosphatase or sulfatase following acetylation of the free tyrosine.

Indexed as

Catalytic DomainHalogenationHydrobromic AcidPeptide FragmentsPeptide MappingPhosphopeptidesPhosphoric Monoester HydrolasesPhosphotyrosineSerum Albumin, BovineSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSulfatasesTandem Mass SpectrometryTyrosinebromotyrosineHydrobromic AcidPeptide FragmentsPhosphopeptidesPhosphoric Monoester HydrolasesPhosphotyrosineSerum Albumin, BovineSulfatasesTyrosinetyrosine O-sulfate

Identifiers

PMID21952757
OpenAlexW2147459090

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.