Evidence map›Paper›PMID 40476587›Full record

ArticleACS synthetic biology2025

Synthetic Phosphorylation Networks with Fluorescence and Luminescence Expansion.

Leah Davis, Evan J Hutt, Matthias Recktenwald, Samarth Patel, Madison Briggs, Madeline Dunsmore, Sebastián L Vega, Mary M Staehle, Peter A Galie, Nichole M Daringer

Abstract read
In one paragraph

Article in ACS synthetic biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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

10 authors.

Leah DavisDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.
Evan J HuttDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.
Matthias RecktenwaldDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.
Samarth PatelDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.
Madison BriggsDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.ORCID 0000-0002-5221-8074
Madeline DunsmoreDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.
Sebastián L VegaDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.ORCID 0000-0002-7669-1552
Mary M StaehleDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.ORCID 0000-0001-6708-9378
Peter A GalieDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.ORCID 0000-0001-5161-4924
Nichole M DaringerDepartment of Biomedical Engineering, Rowan University, Glassboro, New Jersey 08028-1700, United States.

Funding

Targeting the EMT-like Phenotype in Invasive Lobular CarcinomaF31CA203055 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BOSSART, EMILY ANN · 2016 to 2017
$84k
NCI NIH HHS F31 CA203055NSF 2223318
6 · The paper itself

Abstract

Synthetic receptors have emerged as powerful tools for precisely modulating cellular function. However, existing synthetic receptor platforms rely mainly on transcription-mediated reporting processes that are incompatible with the rapid and real-time dynamics of cellular signaling events. To address this limitation, we present SPN-FLUX (synthetic phosphorylation networks with fluorescence and luminescence expansion), a fully post-translational platform that integrates synthetic phosphorylation networks with split fluorescent or luminescent proteins, enabling rapid and tunable reporting of cellular processes. SPN-FLUX is responsive to extracellular stimuli within 1 h, providing a robust alternative to transcription-based approaches. Using mammalian cells as a model, we showcase SPN-FLUX's versatility by designing a membrane-bound receptor that activates upon ligand-induced dimerization, as well as a constitutively active intracellular biosensor. We further validate SPN-FLUX's biosensing capabilities by examining its responsiveness to hypoxic conditions, showcasing the ability to detect environmental changes dynamically. The modularity and programmability of SPN-FLUX establish it as a powerful platform for advancing synthetic biology and biosensing, with broad applications in both biomedical research and environmental monitoring.

Indexed as

Synthetic BiologyBiosensing TechniquesFluorescenceHEK293 CellsHumansLuminescenceLuminescent ProteinsPhosphorylationLuminescent Proteinsbiosensingcell-based devicesprogrammable synthetic receptorssplit fluorescent proteinssplit luciferase proteinssynthetic biology

Identifiers

PMID40476587
PMCPMC12186673

What OpenQuestion holds

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Registered trials

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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.