Evidence map›Paper›PMID 16061816›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Directed evolution of protein switches and their application to the creation of ligand-binding proteins.

Gurkan Guntas, Thomas J Mansell, Jin Ryoun Kim, Marc Ostermeier

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

94 citing papers in PubMed, 218 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Chimeric Protein Switch Biosensors.Advances in biochemical engineering/biotechnology · 2024
    Review
  9. Dissecting the Determinants of Domain Insertion Tolerance and Allostery in Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  10. Article
  11. Catalyst-based biomolecular logic gates.Catalysts (Basel, Switzerland) · 2022
    Article
  12. Advances in the Computational Design of Small-Molecule-Controlled Protein-Based Circuits for Synthetic Biology.Proceedings of the IEEE. Institute of Electrical and Electronics Engineers · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Towards an engineering theory of evolution.Nature communications · 2021
    Review
  17. FimH as a scaffold for regulated molecular recognition.Journal of biological engineering · 2021
    Article
  18. Article
  19. Analytical chemistry · 2020
    Article
  20. Article

34 more citing papers are in PubMed but not listed here.

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.

Gurkan GuntasDepartment of Chemical and Biomolecular Engineering, The Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Thomas J Mansell
Jin Ryoun Kim
Marc Ostermeier
Johns Hopkins University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe an iterative approach for creating protein switches involving the in vitro recombination of two nonhomologous genes. We demonstrate this approach by recombining the genes coding for TEM1 beta-lactamase (BLA) and the Escherichia coli maltose binding protein (MBP) to create a family of MBP-BLA hybrids in which maltose is a positive or negative effector of beta-lactam hydrolysis. Some of these MBP-BLA switches were effectively "on-off" in nature, with maltose altering catalytic activity by as much as 600-fold. The ability of these switches to confer an effector-dependent growth/no growth phenotype to E. coli cells was exploited to rapidly identify, from a library of 4 x 10(6) variants, MBP-BLA switch variants that respond to sucrose as the effector. The transplantation of these mutations into wild-type MBP converted MBP into a "sucrose-binding protein," illustrating the switches potential as a tool to rapidly identify ligand-binding proteins.

Indexed as

Directed Molecular EvolutionProtein BindingAllosteric Regulationbeta-LactamasesCarrier ProteinsCatalysisEscherichia coliEscherichia coli ProteinsGenes, SwitchLigandsMaltose-Binding ProteinsProtein EngineeringSucrosebeta-Lactamasesbeta-lactamase TEM-1Carrier ProteinsEscherichia coli ProteinsLigandsMaltose-Binding ProteinsSucrose

Identifiers

PMID16061816
PMCPMC1183557
OpenAlexW2048072440

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.