Evidence map›Paper›PMID 26199994›Full record

ArticleBiochemistry2015

Development of a Reagentless Biosensor for Inorganic Phosphate, Applicable over a Wide Concentration Range.

Claudia Solscheid, Simone Kunzelmann, Colin T Davis, Jackie L Hunter, Annie Nofer, Martin R Webb

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-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

18 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. The cytokinesis regulator RacGAP1 is a Rac1-specific GAP on membranes.Protein science : a publication of the Protein Society · 2026
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  10. Analytical chemistry · 2020
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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

6 authors at 1 institution in 1 country.

Claudia Solscheid†The Francis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom.
Simone Kunzelmann†The Francis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom.
Colin T Davis†The Francis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom.
Jackie L Hunter‡MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom.
Annie Nofer‡MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom.
Martin R Webb†The Francis Crick Institute, Mill Hill Laboratory, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom.
The Francis Crick Institute · GB

Funding

Medical Research Council MC_U117512742
6 · The paper itself

Abstract

A fluorescent reagentless biosensor for inorganic phosphate (Pi), based on the E. coli PstS phosphate binding protein, was redesigned to allow measurements of higher Pi concentrations and at low, substoichiometric concentrations of biosensor. This was achieved by weakening Pi binding of the previous biosensor, and different approaches are described that could enable this change in properties. The readout, providing response to the Pi concentration, is delivered by tetramethylrhodamine fluorescence. In addition to two cysteine mutations for rhodamine labeling at positions 17 and 197, the final variant had an I76G mutation in the hinge region between the two lobes that make up the protein. Upon Pi binding, the lobes rotate on this hinge and the mutation on the hinge lowers affinity ∼200-fold, with a dissociation constant now in the tens to hundreds micromolar range, depending on solution conditions. The signal change on Pi binding was up to 9-fold, depending on pH. The suitability of the biosensor for steady-state ATPase assays was demonstrated with low biosensor usage and its advantage in ability to cope with Pi contamination.

Indexed as

Amino Acid SubstitutionBinding SitesBiosensing TechniquesEscherichia coli ProteinsFluorescent DyesModels, MolecularMutagenesis, Site-DirectedPeriplasmic Binding ProteinsPhosphate-Binding ProteinsPhosphatesProtein ConformationProtein EngineeringProtein StabilityRecombinant ProteinsRhodaminesSpectrometry, FluorescenceEscherichia coli ProteinsFluorescent DyesPeriplasmic Binding ProteinsPhosphate-Binding ProteinsPhosphatesPstS protein, E coliRecombinant ProteinsRhodaminestetramethylrhodamine

Identifiers

PMID26199994
PMCPMC4741387
OpenAlexW2262790539

What OpenQuestion holds

Textmetadata
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.