Evidence map›Paper›PMID 21472612›Full record

ArticleJournal of the American Society for Mass Spectrometry2011

Characterization of AMPylation on threonine, serine, and tyrosine using mass spectrometry.

Yan Li, Rowaida Al-Eryani, Melanie L Yarbrough, Kim Orth, Haydn L Ball

Abstract read
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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. MS-BasedACS infectious diseases · 2020
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Analysis of the Structure and Function of FOX-4 Cephamycinase.Antimicrobial agents and chemotherapy · 2016
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. A chemical reporter for protein AMPylation.Journal of the American Chemical Society · 2011
    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

5 authors at 1 institution in 1 country.

Yan LiProtein Chemistry Technology Center, Department of Internal Medicine, University of Texas, Southwestern Medical Center, Dallas, TX, USA.
Rowaida Al-Eryani
Melanie L Yarbrough
Kim Orth
Haydn L Ball
The University of Texas Southwestern Medical Center · US

Funding

Biochemical Characterization of Yersinia Effector YopJ.R01AI056404 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2003 to 2012
$2.8M
Analysis of an orchestrated cell death mediated by Vibrio parahaemolytics T3SS1R01AI087808 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2010 to 2014
$1.9M
Analysis of newly identified adhesin used by pathogenic Gram-negative bacteriaR21AI096133 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2012 to 2013
$423k
NIAID NIH HHS R01 AI056404NIAID NIH HHS R01 AI087808NIAID NIH HHS R21 AI096133
6 · The paper itself

Abstract

Recent studies have suggested that adenosine 5'-monophosphate (AMP) post-translational modification of proteins could represent a novel molecular signaling pathway. Mass spectrometric fragmentation characteristics of this modification have not previously been described and studied systematically. In this work, we therefore examined the fragmentation pattern of chemically synthesized peptides containing AMPylated Thr, Ser, and Tyr. The formation of characteristic ions and the influence of collision energy (CE) on the detection of characteristic ions and their relative peak intensity are reported. When peptide with AMPylated Ser/Thr underwent collision induced dissociation (CID), peaks at m/z 348.1, 136.1, and 250.1, fragments with AMP group attached, and fragments consistent with neutral loss of 347 Da were major characteristic ions; fragments consistent with neutral loss of 135 Da or 249 Da were weaker and not always detectable. The observations for Tyr AMPylation followed the same general patterns as those for Ser/Thr modification, with the exception that the ions detected for Tyr AMPylation did not include either the peak at m/z 348.1, or fragments with a mass shift of -347 Da. The results described in this paper highlight a series of diagnostic ions, which can be used not only to confidently identify the AMPylation site based on MS and MS/MS data, but also to selectively scan AMPylated peptides in complex protein mixtures.

Indexed as

Adenosine MonophosphateAmino Acid SequenceBiochemical PhenomenaMass SpectrometryPeptidesSerineThreonineTyrosineAdenosine MonophosphatePeptidesSerineThreonineTyrosine

Identifiers

PMID21472612
PMCPMC3391576
OpenAlexW2081179534

What OpenQuestion holds

Textmetadata
LicenceTDM
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.