Evidence map›Paper›PMID 23708076›Full record

ArticleNature chemical biology2013

A pan-specific antibody for direct detection of protein histidine phosphorylation.

Jung-Min Kee, Rob C Oslund, David H Perlman, Tom W Muir

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

63 citing papers in PubMed, 142 citations in OpenAlex.

  1. Article
  2. Immunoblot-based activity assay for heme-containing histidine kinases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  3. Review
  4. Article
  5. Molecular Mechanisms of Virulence Regulation inAccounts of chemical research · 2025
    Article
  6. Review
  7. Nphos: Database and Predictor of Protein N-phosphorylation.Genomics, proteomics & bioinformatics · 2024
    Article
  8. Histidine Phosphorylation: Protein Kinases and Phosphatases.International journal of molecular sciences · 2024
    Review
  9. Article
  10. [Progress in enrichment methods for proteinSe pu = Chinese journal of chromatography · 2024
    Review
  11. Chemical proteomics approaches for protein post-translational modification studies.Biochimica et biophysica acta. Proteins and proteomics · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Jung-Min KeeDepartment of Chemistry, Princeton University, Princeton, New Jersey, USA.
Rob C Oslund
David H Perlman
Tom W Muir
Princeton University · US

Funding

Chemistry and biology of protein histidine phosphorylationR01GM095880 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2011 to 2014
$1.3M
Analysis of Proline Isomerization in EpigeneticsF32CA167901 · NCI · PRINCETON UNIVERSITY · PI OSLUND, ROB CARL · 2012 to 2014
$150k
NCI NIH HHS 1F32CA167901NCI NIH HHS F32 CA167901NIGMS NIH HHS 5R01GM095880NIGMS NIH HHS R01 GM095880
6 · The paper itself

Abstract

Despite its importance in central metabolism and bacterial cell signaling, protein histidine phosphorylation has remained elusive with respect to its extent and functional roles in biological systems because of the lack of adequate research tools. We report the development of the first pan-phosphohistidine (pHis) antibody using a stable pHis mimetic as the hapten. This antibody was successfully used in ELISA, western blotting, dot blot assays and immunoprecipitation and in detection and identification of histidine-phosphorylated proteins from native cell lysates when coupled with MS analysis. We also observed that the amount of protein pHis in Escherichia coli lysates depends on carbon source and nitrogen availability in the growth medium. In particular, we found that the amount of pHis on phosphoenolpyruvate synthase (PpsA) is sensitive to nitrogen availability in vivo and that α-ketoglutarate inhibits phosphotransfer from phosphorylated PpsA to pyruvate. We expect this antibody to open opportunities for investigating other pHis proteins and their functions.

Indexed as

AntibodiesDose-Response Relationship, DrugEnzyme-Linked Immunosorbent AssayEscherichia coliEscherichia coli ProteinsHistidineHydrogen-Ion ConcentrationIonsKetoglutaric AcidsMass SpectrometryPhosphorylationPhosphotransferases (Paired Acceptors)ProteinsPyruvate SynthaseRecombinant ProteinsAntibodiesEscherichia coli ProteinsHistidineIonsKetoglutaric AcidsphosphohistidinePhosphotransferases (Paired Acceptors)ppsA protein, E coliProteinsPyruvate Synthasepyruvate, water dikinaseRecombinant Proteins

Identifiers

PMID23708076
PMCPMC3686892
OpenAlexW2149244180

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.