Evidence map›Paper›PMID 26317540›Full record

ArticlePloS one2015

Energy Sensing versus 2-Oxoglutarate Dependent ATPase Switch in the Control of Synechococcus PII Interaction with Its Targets NAGK and PipX.

Jan Lüddecke, Karl Forchhammer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. PProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. The PFrontiers in molecular biosciences · 2018
    Review
  9. Article
  10. PScientific reports · 2017
    Article
  11. Article
  12. 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.

Jan LüddeckeInterfaculty Institute for Microbiology and Infection Medicine, Division Organismic Interactions, University of Tübingen, Auf der Morgenstelle 28, D-72076, Tübingen, Germany.
Karl ForchhammerInterfaculty Institute for Microbiology and Infection Medicine, Division Organismic Interactions, University of Tübingen, Auf der Morgenstelle 28, D-72076, Tübingen, Germany.
University of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PII proteins constitute a superfamily of highly conserved signaling devices, common in all domains of life. Through binding of the metabolites ATP, ADP and 2-oxoglutarate (2-OG), they undergo conformational changes which allow them to regulate a variety of target proteins including enzymes, transport proteins and transcription factors. But, in reverse, these target proteins also modulate the metabolite sensing properties of PII, as has been recently shown. We used this effect to refine our PII based Förster resonance energy transfer (FRET) sensor and amplify its sensitivity towards ADP. With this enhanced sensor setup we addressed the question whether the PII protein from the model organism Synechococcus elongatus autonomously switches into the ADP conformation through ATPase activity as proposed in a recently published model. The present study disproves ATPase activity as a relevant mechanism for the transition of PII into the ADP state. In the absence of 2-OG, only the ATP/ADP ratio and concentration of ADP directs the competitive interaction of PII with two targets, one of which preferentially binds PII in the ATP-state, the other in the ADP-state.

Indexed as

Adenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsFluorescence Resonance Energy TransferKetoglutaric AcidsPhosphotransferases (Alcohol Group Acceptor)PII Nitrogen Regulatory ProteinsProtein BindingProtein ConformationSynechococcusAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsKetoglutaric AcidsPhosphotransferases (Alcohol Group Acceptor)PII Nitrogen Regulatory Proteins

Identifiers

PMID26317540
PMCPMC4552645
OpenAlexW1910655007

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.