Evidence map›Paper›PMID 10339534›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light.

D A Fancy, T Kodadek

Erratum issuedAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 192 papers.

0numbers the graph read from it
0cells of the map it votes in
192citing 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

192 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. The Many Lives of [Ru(bpy)Inorganic chemistry · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Fully Reshapeable and Recyclable Protein Hydrogels.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  15. Article
  16. Article
  17. Ionic Crosslinking Improves the Stiffness and Toughness of Protein Hydrogels.Polymer science & technology (Washington, D.C.) · 2025
    Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors.

D A FancyDepartments of Internal Medicine and Biochemistry, Center for Biomedical Inventions, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235-8573, USA.
T Kodadek

Funding

NEW CHEMISTRY FOR THE STUDY OF MULTIPROTEIN COMPLEXESR01GM058175 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI KODADEK, THOMAS J. · 1998 to 2005
$1.5M
NIGMS NIH HHS GM-58175NIGMS NIH HHS R01 GM058175
6 · The paper itself

Abstract

Chemical cross-linking is a potentially useful technique for probing the architecture of multiprotein complexes. However, analyses using typical bifunctional cross-linkers often suffer from poor yields, and large-scale modification of nucleophilic side chains can result in artifactual results attributable to structural destabilization. We report here the de novo design and development of a type of protein cross-linking reaction that uses a photogenerated oxidant to mediate rapid and efficient cross-linking of associated proteins. The process involves brief photolysis of tris-bipyridylruthenium(II) dication with visible light in the presence of the electron acceptor ammonium persulfate and the proteins of interest. Very high yields of cross-linked products can be obtained with irradiation times of <1 second. This chemistry obviates many of the problems associated with standard cross-linking reagents.

Indexed as

Saccharomyces cerevisiae Proteins2,2'-DipyridylBinding SitesCoordination ComplexesCross-Linking ReagentsDNA-Binding ProteinsFungal ProteinsGlutathione TransferaseIndicators and ReagentsKineticsLightMembrane ProteinsOxidantsPhotolysisProteinsRecombinant Fusion Proteins2,2'-DipyridylCoordination ComplexesCross-Linking ReagentsDNA-Binding ProteinsFungal ProteinsGAL4 protein, S cerevisiaeGlutathione TransferaseIndicators and ReagentsMembrane ProteinsOxidantsProteinsRecombinant Fusion ProteinsRuthenium CompoundsSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription Factorstris(2,2-bipyridine)-ruthenium(II)UvsY protein, Enterobacteria phage T4Viral Proteins

Identifiers

PMID10339534
PMCPMC26828

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.