Evidence map›Paper›PMID 24210218›Full record

ArticleChemistry & biology2013

Autophosphorylation activity of a soluble hexameric histidine kinase correlates with the shift in protein conformational equilibrium.

Marta Wojnowska, Jun Yan, Ganesh N Sivalingam, Adam Cryar, Jayesh Gor, Konstantinos Thalassinos, Snezana Djordjevic

Open access · hybridAbstract read
In one paragraph

Article in Chemistry & biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 32 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Marta WojnowskaStructural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, UK.
Jun Yan
Ganesh N Sivalingam
Adam Cryar
Jayesh Gor
Konstantinos Thalassinos
Snezana Djordjevic
Institute of Structural and Molecular Biology · GBUniversity College London · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

In a commonly accepted model, in response to stimuli, bacterial histidine kinases undergo a conformational transition between an active and inactive form. Structural information on histidine kinases is limited. By using ion mobility-mass spectrometry (IM-MS), we demonstrate an exchange between two conformational populations of histidine kinase ExsG that are linked to different levels of kinase activity. ExsG is an atypical signaling protein that incorporates an uncommon histidine kinase catalytic core at the C terminus preceded by an N-terminal "receiver domain" that is normally associated with the response regulator proteins in two-component signal transduction systems. IM-MS analysis and enzymatic assays indicate that phosphorylation of the ExsG receiver domain stabilizes the "compact" form of the protein and inhibits kinase core activity; in contrast, nucleotide binding required for kinase activity is associated with the more open conformation of ExsG.

Indexed as

Histidine KinaseMass SpectrometryPhosphorylationProtein ConformationProtein KinasesSolubilityHistidine KinaseProtein Kinases

Identifiers

PMID24210218
PMCPMC3899027
OpenAlexW2104265970

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.