Evidence map›Paper›PMID 15879217›Full record

ArticleScience (New York, N.Y.)2005

Computational thermostabilization of an enzyme.

Aaron Korkegian, Margaret E Black, David Baker, Barry L Stoddard

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.

0numbers the graph read from it
0cells of the map it votes in
143citing 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

143 citing papers in PubMed.

  1. Introduction to the Field of Enzyme Immobilization and Stabilization.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Article
  3. Buttressing ligand-binding pockets in de novo designed NTF2-like domains.Protein science : a publication of the Protein Society · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Protein Assembly by Design.Chemical reviews · 2021
    Review
  14. Article
  15. Article
  16. Using Mutability Landscapes To Guide Enzyme Thermostabilization.Chembiochem : a European journal of chemical biology · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Article

83 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.

Aaron KorkegianDivision of Basic Sciences, Fred Hutchinson Cancer Research Center (FHCRC), 1100 Fairview Avenue North, Seattle, WA 98109, USA.
Margaret E Black
David Baker
Barry L Stoddard

Funding

TRAINING IN MOLECULAR BIOPHYSICST32GM008268 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M, ZHENG, NING · 1988 to 2023
$8.6M
Structure, function &engineering of nuclease catalystsR01GM049857 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 1994 to 2014
$4.2M
Engineering enzymes for anti-tumor suicide gene therapyR01CA097328 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 2003 to 2010
$2.5M
IMPROVING SUICIDE GENES FOR CANCER GENE THERAPYR01CA085939 · NCI · WASHINGTON STATE UNIVERSITY · PI BLACK, MARGARET E · 2000 to 2009
$2.3M
Protein-Protein InteractionsR01GM059224 · NIGMS · UNIVERSITY OF WASHINGTON · PI BAKER, DAVID · 1999 to 2009
$1.8M
NCI NIH HHS CA85939NCI NIH HHS CA97328NCI NIH HHS R01 CA085939NCI NIH HHS R01 CA097328NIGMS NIH HHS GM49857NIGMS NIH HHS GM59224NIGMS NIH HHS R01 GM049857NIGMS NIH HHS R01 GM059224NIGMS NIH HHS T32 GM008268NIGMS NIH HHS T32-GM08268
6 · The paper itself

Abstract

Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.

Indexed as

Computer SimulationProtein EngineeringAmino Acid SequenceBinding SitesCatalysisCircular DichroismCrystallography, X-RayCytosine DeaminaseEnzyme StabilityEscherichia coliKineticsModels, MolecularMolecular Sequence DataMonte Carlo MethodMutagenesis, Site-DirectedPoint MutationCytosine Deaminase

Identifiers

PMID15879217
PMCPMC3412875

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.