Evidence map›Paper›PMID 18927392›Full record

ArticleScience (New York, N.Y.)2008

Surface sites for engineering allosteric control in proteins.

Jeeyeon Lee, Madhusudan Natarajan, Vishal C Nashine, Michael Socolich, Tina Vo, William P Russ, Stephen J Benkovic, Rama Ranganathan

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 170 papers.

0numbers the graph read from it
0cells of the map it votes in
170citing papers in PubMed
34.3field-weighted citation impact, top 1% 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

170 citing papers in PubMed, 346 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Optogenetic enzymes: A deep dive into design and impact.Current opinion in structural biology · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Allosteric regulation of kinase activity in living cells.bioRxiv : the preprint server for biology · 2023
    Article
  17. Dissecting the Determinants of Domain Insertion Tolerance and Allostery in Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  18. Light-stimulated insulin secretion from pancreatic islet-like organoids derived from human pluripotent stem cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  19. Article
  20. Review

110 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

8 authors at 1 institution in 1 country.

Jeeyeon LeeDepartment of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.
Madhusudan Natarajan
Vishal C Nashine
Michael Socolich
Tina Vo
William P Russ
Stephen J Benkovic
Rama Ranganathan
Pennsylvania State University · US

Funding

Mechanistic analysis of dynamic scaffolding in a cellular signaling networkR01EY018720 · NEI · UT SOUTHWESTERN MEDICAL CENTER · PI RANGANATHAN, RAMA · 2007 to 2012
$1.8M
NEI NIH HHS R01 EY018720
6 · The paper itself

Abstract

Statistical analyses of protein families reveal networks of coevolving amino acids that functionally link distantly positioned functional surfaces. Such linkages suggest a concept for engineering allosteric control into proteins: The intramolecular networks of two proteins could be joined across their surface sites such that the activity of one protein might control the activity of the other. We tested this idea by creating PAS-DHFR, a designed chimeric protein that connects a light-sensing signaling domain from a plant member of the Per/Arnt/Sim (PAS) family of proteins with Escherichia coli dihydrofolate reductase (DHFR). With no optimization, PAS-DHFR exhibited light-dependent catalytic activity that depended on the site of connection and on known signaling mechanisms in both proteins. PAS-DHFR serves as a proof of concept for engineering regulatory activities into proteins through interface design at conserved allosteric sites.

Indexed as

Protein EngineeringAllosteric RegulationAllosteric SiteBinding SitesCatalysisCryptochromesEscherichia coliFlavoproteinsKineticsLigandsLightModels, MolecularNADPProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryCryptochromesFlavoproteinsLigandsNADPRecombinant Fusion ProteinsTetrahydrofolate Dehydrogenase

Identifiers

PMID18927392
PMCPMC3071530
OpenAlexW2013726100

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.