Evidence map›Paper›PMID 22776405›Full record

ArticleJournal of biological engineering2012

A genetic bistable switch utilizing nonlinear protein degradation.

Daniel Huang, William J Holtz, Michel M Maharbiz

Open access · goldAbstract read
In one paragraph

Article in Journal of biological engineering, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Frontiers in genetics · 2024
    Review
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  6. Review
  7. Synchrony and pattern formation of coupled genetic oscillators on a chip of artificial cells.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Article
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  15. Tunable protein degradation in bacteria.Nature biotechnology · 2014
    Article
  16. Article
  17. Tailored fatty acid synthesis via dynamic control of fatty acid elongation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

3 authors at 2 institutions in 1 country.

Daniel HuangDepartment of Electrical Engineering and Computer Science, University of California, 656 Sutardja Dai Hall,Berkeley, Berkeley, CA, 94720, USA. maharbiz@eecs.berkeley.edu.
William J Holtz
Michel M Maharbiz
University of California, Berkeley · USQB3 · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBistability is a fundamental property in engineered and natural systems, conferring the ability to switch and retain states. Synthetic bistable switches in prokaryotes have mainly utilized transcriptional components in their construction. Using both transcriptional and enzymatic components, creating a hybrid system, allows for wider bistable parameter ranges in a circuit.

resultsIn this paper, we demonstrate a tunable family of hybrid bistable switches in E. coli using both transcriptional components and an enzymatic component. The design contains two linked positive feedback loops. The first loop utilizes the lambda repressor, CI, and the second positive feedback loop incorporates the Lon protease found in Mesoplasma florum (mf-Lon). We experimentally tested for bistable behavior in exponential growth phase, and found that our hybrid bistable switch was able to retain its state in the absence of an input signal throughout 40 cycles of cell division. We also tested the transient behavior of our switch and found that switching speeds can be tuned by changing the expression rate of mf-Lon.

conclusionsTo our knowledge, this work demonstrates the first use of dynamic expression of an orthogonal and heterologous protease to tune a nonlinear protein degradation circuit. The hybrid switch is potentially a more robust and tunable topology for use in prokaryotic systems.

Identifiers

PMID22776405
PMCPMC3439342
OpenAlexW2138972294

What OpenQuestion holds

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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.