Evidence map›Paper›PMID 29944360›Full record

ArticleBiochemistry2018

Exploration of the Effects of γ-Phosphate-Modified ATP Analogues on Histidine Kinase Autophosphorylation.

Olivia M Chase, Adeline Espinasse, Kaelyn E Wilke, Erin E Carlson

Abstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-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

13 citing papers in PubMed, 15 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. Direct energy consumption by inhibitory GABAFrontiers in neuroscience · 2026
    Article
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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

4 authors at 2 institutions in 1 country.

Olivia M ChaseDepartment of Chemistry , University of Minnesota , 207 Pleasant Street Southeast , Minneapolis , Minnesota 55455 , United States.
Adeline EspinasseDepartment of Chemistry , University of Minnesota , 207 Pleasant Street Southeast , Minneapolis , Minnesota 55455 , United States.
Kaelyn E WilkeDepartment of Chemistry , Indiana University , 800 East Kirkwood Avenue , Bloomington , Indiana 47405 , United States.
Erin E CarlsonDepartment of Chemistry , University of Minnesota , 207 Pleasant Street Southeast , Minneapolis , Minnesota 55455 , United States.ORCID 0000-0001-8287-8893
University of Minnesota · USIndiana University Bloomington · US

Funding

TRAINING FOR FUTURE BIOTECHNOLOGY DEVELOPMENTT32GM008347 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHMIDT-DANNERT, CLAUDIA · 1990 to 2021
$11.0M
Targeted natural product diversification to identify novel antibacterial agentsDP2OD008592 · OD · UNIVERSITY OF MINNESOTA · PI CARLSON, ERIN ELIZABETH · 2011 to 2011
$2.2M
NIGMS NIH HHS T32 GM008347NIH HHS DP2 OD008592
6 · The paper itself

Abstract

While two-component systems (TCSs), composed of a sensor histidine kinase (HK) and a response regulator, are the main signaling pathways in bacteria, global TCS activity remains poorly described. Here, we report the kinetic parameters of the HK autophosphorylation reaction using previously uncharacterized γ-phosphate-modified ATP analogues to further elucidate their utility as activity-based probes for global TCS analysis. Given the increased stability of thiophosphorylated histidine in comparison to that of the native phosphoryl modification, which is attributed to the decreased electrophilicity of this moiety, we anticipated that ATPγS may be turned over much more slowly by the HKs. Surprisingly, we found this not to be the case, with the turnover numbers decreasing <1 order of magnitude. Instead, we found that alkylation of the thiophosphate had a much more dramatic effect on turnover and, in one case, the binding affinity of this substrate analogue (BODIPY-FL-ATPγS).

Indexed as

Adenosine TriphosphateBacterial ProteinsHistidineHistidine KinaseKineticsMolecular ProbesPhosphorylationThermotoga maritimaAdenosine TriphosphateBacterial ProteinsHistidineHistidine KinaseMolecular Probes

Identifiers

PMID29944360
PMCPMC6402838
OpenAlexW2809727357

What OpenQuestion holds

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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.