Evidence map›Paper›PMID 26900850›Full record

ArticlePloS one2016

N-Terminal-Based Targeted, Inducible Protein Degradation in Escherichia coli.

Karthik Sekar, Andrew M Gentile, John W Bostick, Keith E J Tyo

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  11. Two NovelFrontiers in cellular and infection microbiology · 2017
    Article
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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

4 authors at 1 institution in 1 country.

Karthik SekarDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL, United States of America.
Andrew M GentileMaster of Biotechnology Program, Northwestern University, Evanston, IL, United States of America.
John W BostickDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL, United States of America.
Keith E J TyoDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL, United States of America.
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
NCI NIH HHS P30 CA060553
6 · The paper itself

Abstract

Dynamically altering protein concentration is a central activity in synthetic biology. While many tools are available to modulate protein concentration by altering protein synthesis rate, methods for decreasing protein concentration by inactivation or degradation rate are just being realized. Altering protein synthesis rates can quickly increase the concentration of a protein but not decrease, as residual protein will remain for a while. Inducible, targeted protein degradation is an attractive option and some tools have been introduced for higher organisms and bacteria. Current bacterial tools rely on C-terminal fusions, so we have developed an N-terminal fusion (Ntag) strategy to increase the possible proteins that can be targeted. We demonstrate Ntag dependent degradation of mCherry and beta-galactosidase and reconfigure the Ntag system to perform dynamic, exogenously inducible degradation of a targeted protein and complement protein depletion by traditional synthesis repression. Model driven analysis that focused on rates, rather than concentrations, was critical to understanding and engineering the system. We expect this tool and our model to enable inducible protein degradation use particularly in metabolic engineering, biological study of essential proteins, and protein circuits.

Indexed as

Proteolysisbeta-GalactosidaseCarrier ProteinsEndopeptidase ClpEscherichia coliEscherichia coli ProteinsRecombinant Fusion Proteinsbeta-GalactosidaseCarrier ProteinsClpP protease, E coliClpS protein, E coliEndopeptidase ClpEscherichia coli ProteinsRecombinant Fusion Proteins

Identifiers

PMID26900850
PMCPMC4765774
OpenAlexW2281376834

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.