Evidence map›Paper›PMID 22148577›Full record

ReviewACS chemical biology2012

Chasing phosphohistidine, an elusive sibling in the phosphoamino acid family.

Jung-Min Kee, Tom W Muir

Open access · greenAbstract readReview
In one paragraph

Review in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. A Constellation of Fluorescent Biosensors to Illuminate the Galaxy of Protein Kinases.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Review
  4. Inhibition of PHPT1 by phenylarsonic acids.Dalton transactions (Cambridge, England : 2003) · 2026
    Article
  5. Article
  6. Article
  7. [Progress in enrichment methods for proteinSe pu = Chinese journal of chromatography · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Histidine-specific bioconjugationChemical science · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. PRD-Containing Virulence Regulators (PCVRs) in Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2021
    Review
  20. 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

2 authors at 1 institution in 1 country.

Jung-Min KeeDepartment of Chemistry, Princeton University, New Jersey 08544, United States.
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
NIGMS NIH HHS R01 GM095880NIGMS NIH HHS R01GM095880
6 · The paper itself

Abstract

This year (2012) marks the 50th anniversary of the discovery of protein histidine phosphorylation. Phosphorylation of histidine (pHis) is now widely recognized as being critical to signaling processes in prokaryotes and lower eukaryotes. However, the modification is also becoming more widely reported in mammalian cellular processes and implicated in certain human disease states such as cancer and inflammation. Nonetheless, much remains to be understood about the role and extent of the modification in mammalian cell biology. Studying the functional role of pHis in signaling, either in vitro or in vivo, has proven devilishly hard, largely due to the chemical instability of the modification. As a consequence, we are currently handicapped by a chronic lack of chemical and biochemical tools with which to study histidine phosphorylation. Here, we discuss the challenges associated with studying the chemical biology of pHis and review recent progress that offers some hope that long-awaited biochemical reagents for studying this elusive posttranslational modification (PTM) might soon be available.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsAntibodies, Phospho-SpecificEukaryotaHistidineHumansIsomerismMagnetic Resonance SpectroscopyMammalsMass SpectrometryMolecular Sequence DataOrganophosphonatesPhosphoproteinsPhosphorylationPhosphotransferasesAntibodies, Phospho-SpecificHistidineOrganophosphonatesphosphohistidinePhosphoproteinsPhosphotransferases

Identifiers

PMID22148577
PMCPMC3263764
OpenAlexW1999970872

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.