Evidence map›Paper›PMID 21466224›Full record

ArticleAnalytical chemistry2011

Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.

Patrick G Shaw, Raghothama Chaerkady, Zhen Zhang, Nancy E Davidson, Akhilesh Pandey

Open access · bronzeAbstract readLetter
In one paragraph

Article in Analytical chemistry, 2011. 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
1.4field-weighted citation impact, top 18% 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, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. A SUMO-acetyl switch in PXR biology.Biochimica et biophysica acta · 2016
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. SIRT1-mediated acute cardioprotection.American journal of physiology. Heart and circulatory physiology · 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 3 institutions in 2 countries.

Patrick G Shaw
Raghothama Chaerkady
Zhen Zhang
Nancy E Davidson
Akhilesh Pandey
Johns Hopkins University · USInstitute of Bioinformatics · INUPMC Hillman Cancer Center · US

Funding

VACCINES--A NEW PARADIGM FOR BREAST CANCERP50CA088843 · NCI · JOHNS HOPKINS UNIVERSITY · PI DAVIDSON, NANCY ELLEN · 2000 to 2010
$27.8M
TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
PILOT STUDY--ACID FOG, AN EXPERIMENTAL MODELP30ES003819 · NIEHS · JOHNS HOPKINS UNIVERSITY · PI GROOPMAN, JOHN D · 1985 to 2012
$22.6M
Networks, Pathways and Dynamics of Lysine ModificationU54GM103520 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BADER, JOEL S. · 2012 to 2013
$7.0M
Purchase of a Linear Ion Trap/Fourier Transform Mass SpectrometerS10RR023025 · NCRR · JOHNS HOPKINS UNIVERSITY · PI COTTER, ROBERT JAMES · 2007 to 2007
$928k
NCI NIH HHS CA88843NCI NIH HHS P50 CA088843NCRR NIH HHS S10 RR023025NCRR NIH HHS S10RR023025NCRR NIH HHS U54 RR 020839NCRR NIH HHS U54 RR020839NIEHS NIH HHS P30 ES003819NIEHS NIH HHS P30 ES03819NIGMS NIH HHS U54 GM103520
6 · The paper itself

Abstract

The availability and robustness of methods to analyze phosphorylated proteins has greatly expanded our knowledge of phosphorylation based cell signaling. A key ingredient to the success of these studies is the ability to enrich phosphopeptides using antibodies or other chemical approaches. Most other post-translational modifications, such as lysine acetylation, are still poorly characterized because of the lack of availability of such enrichment methods. Recently, some groups have reported identification of acetylation sites in a global fashion by enriching acetylated peptides with a polyclonal antibody from a single source that was raised against pan-acetylated lysine. Instead of the use of this polyclonal antibody, we used a cocktail of monoclonal antibodies where each was directed against acetylated lysine in different contexts. Using high resolution Fourier transform mass spectrometry, we observed that the majority of acetylated lysine residues identified using the monoclonal antibody cocktail were distinct from those enriched by the polyclonal antibody used by the other groups. Our study demonstrates that immunoaffinity enrichment of acetylated peptides is somewhat limited by substrate specificity and that an optimal yield of enrichment can be achieved by employing a broader array of affinity reagents.

Indexed as

Mass SpectrometryAcetylationAmino Acid SequenceAntibodies, MonoclonalCell Line, TumorFourier AnalysisHumansLysineMolecular Sequence DataPhosphopeptidesAntibodies, MonoclonalLysinePhosphopeptides

Identifiers

PMID21466224
PMCPMC3205458
OpenAlexW2102270741

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.