Evidence map›Paper›PMID 19473830›Full record

ReviewCurrent opinion in structural biology2009

Designing switchable enzymes.

Marc Ostermeier

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018
    Review
  13. Article
  14. Article
  15. The interplay between effector binding and allostery in an engineered protein switch.Protein science : a publication of the Protein Society · 2016
    Article
  16. Article
  17. Electrochemical activation of engineered protein switches.Biotechnology and bioengineering · 2016
    Article
  18. Article
  19. Article
  20. Structural DNA nanotechnology: state of the art and future perspective.Journal of the American Chemical Society · 2014
    Review
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

1 author at 1 institution in 1 country.

Marc OstermeierDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA. oster@jhu.edu
University of Baltimore · US

Funding

The Combinatorial Design of Protein Molecular SwitchesR01GM066972 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI OSTERMEIER, MARC A · 2003 to 2016
$4.0M
NIGMS NIH HHS 2R01 GM066972NIGMS NIH HHS R01 GM066972
6 · The paper itself

Abstract

The modulation of enzyme function is a key regulatory feature of biological systems. The ability to engineer synthetic enzymes that can be controlled by any arbitrary signal would enable a wide array of sensing applications and therapeutics and provide us with powerful tools for the basic study of biology. Here several recent advances in the engineering of switchable enzymes through domain fusion are discussed.

Indexed as

Allosteric RegulationAnimalsComputer SimulationEnzymesModels, BiologicalProtein BindingProtein EngineeringEnzymes

Identifiers

PMID19473830
PMCPMC2736331
OpenAlexW2011398679

What OpenQuestion holds

Textmetadata
LicenceTDM
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.