Evidence map›Paper›PMID 19819215›Full record

ArticleAnalytical biochemistry2010

Use of a semisynthetic epitope to probe histidine kinase activity and regulation.

Hans K Carlson, Lars Plate, Mark S Price, Jasmina J Allen, Kevan M Shokat, Michael A Marletta

Open access · greenAbstract read
In one paragraph

Article in Analytical biochemistry, 2010. 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
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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. 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
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Advances in development of new tools for the study of phosphohistidine.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Activity-based probe for histidine kinase signaling.Journal of the American Chemical Society · 2012
    Article
  17. Review
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

6 authors at 2 institutions in 1 country.

Hans K CarlsonDepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.
Lars Plate
Mark S Price
Jasmina J Allen
Kevan M Shokat
Michael A Marletta
University of California, Berkeley · USUniversity of California, San Francisco · US

Funding

Using chemical genetics to investigate mechanisms of anesthetic actionR01EB001987 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SHOKAT, KEVAN M. · 2003 to 2012
$2.9M
Heme Protein Sensors in ProkaryotesR01GM070671 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARLETTA, MICHAEL A. · 2005 to 2008
$1.2M
NIBIB NIH HHS EB001987NIBIB NIH HHS R01 EB001987NIGMS NIH HHS GM070671NIGMS NIH HHS R01 GM070671
6 · The paper itself

Abstract

Histidine-aspartic acid phosphotransfer pathways are central components of prokaryotic signal transduction pathways and are also found in many eukaryotes. Tools to study histidine kinases, however, are currently quite limited. In this article, we present a new tool to study histidine-aspartic acid phosphotransfer pathways. We show that many histidine kinases will accept ATPgammaS as a substrate to form a stable thiophosphohistidine even when they do not form stable phosphohistidines using the natural substrate ATP. An antibody that has previously been used to detect thiophosphorylated serine, threonine, and tyrosine residues is shown to recognize thiophosphohistidine and thiophosphoaspartic acid residues. Histidine kinase autothiophosphorylation is regulated by other protein sensor domains in the same way as autophosphorylation, and thiophosphate is transferred to downstream aspartic acid containing response regulators.

Indexed as

Adenosine TriphosphateCloning, MolecularEpitopesEscherichia coliHistidineHistidine KinaseProtein Kinasesadenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphateEpitopesHistidineHistidine KinaseProtein Kinases

Identifiers

PMID19819215
PMCPMC2812668
OpenAlexW2094029658

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.