Evidence map›Paper›PMID 21064163›Full record

ReviewProtein science : a publication of the Protein Society2011

Converting a protein into a switch for biosensing and functional regulation.

Margaret M Stratton, Stewart N Loh

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Seesaw protein: Design of a protein that adopts interconvertible alternative functional conformations and its dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The interplay between effector binding and allostery in an engineered protein switch.Protein science : a publication of the Protein Society · 2016
    Article
  9. Electrochemical activation of engineered protein switches.Biotechnology and bioengineering · 2016
    Article
  10. A critical element of the light-induced quaternary structural changes in YtvA-LOV.Protein science : a publication of the Protein Society · 2015
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Designing redox potential-controlled protein switches based on mutually exclusive proteins.Protein science : a publication of the Protein Society · 2012
    Article
  20. 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

2 authors.

Margaret M StrattonDepartment of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA.
Stewart N Loh

Funding

Mutually Exclusive Protein FoldingR01GM069755 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI LOH, STEWART N · 2004 to 2012
$2.3M
NIGMS NIH HHS R01 GM069755NIGMS NIH HHS R01GM069755
6 · The paper itself

Abstract

Proteins that switch conformations in response to a signaling event (e.g., ligand binding or chemical modification) present a unique solution to the design of reagent-free biosensors as well as molecules whose biological functions are regulated in useful ways. The principal roadblock in the path to develop such molecules is that the majority of natural proteins do not change conformation upon binding their cognate ligands or becoming chemically modified. Herein, we review recent protein engineering efforts to introduce switching properties into binding proteins. By co-opting natural allosteric coupling, joining proteins in creative ways and formulating altogether new switching mechanisms, researchers are learning how to coax conformational changes from proteins that previously had none. These studies are providing some answers to the challenging question: how can one convert a lock-and-key binding protein into a molecular switch?

Indexed as

Allosteric RegulationBiosensing TechniquesHumansProtein BindingProtein ConformationProtein EngineeringProtein FoldingRecombinant Fusion ProteinsRecombinant Fusion Proteins

Identifiers

PMID21064163
PMCPMC3047058

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.