Evidence map›Paper›PMID 19108697›Full record

ArticleJournal of the American Chemical Society2008

A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer.

Eric M Brustad, Edward A Lemke, Peter G Schultz, Ashok A Deniz

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
13.0field-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

80 citing papers in PubMed, 181 citations in OpenAlex.

  1. Review
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  12. Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  13. Article
  14. Article
  15. Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021
    Review
  16. Article
  17. Contemporary Approaches for Site-Selective Dual Functionalization of Proteins.Angewandte Chemie (International ed. in English) · 2021
    Review
  18. Article
  19. Review
  20. Article

20 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 at 1 institution in 1 country.

Eric M BrustadDepartment of Molecular Biology, Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Edward A Lemke
Peter G Schultz
Ashok A Deniz
Scripps Research Institute · US

Funding

Single Molecule Studies of Protein Folding MechanismsR01GM066833 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2003 to 2017
$5.2M
NIGMS NIH HHS GM066833NIGMS NIH HHS R01 GM066833
6 · The paper itself

Abstract

A general strategy for the site-specific dual-labeling of proteins for single-molecule fluorescence resonance energy transfer is presented. A genetically encoded unnatural ketone amino acid was labeled with a hydroxylamine-containing fluorophore with high yield (>95%) and specificity. This methodology was used to construct dual-labeled T4 lysozyme variants, allowing the study of T4 lysozyme folding at single-molecule resolution. The presented strategy is anticipated to expand the scope of single-molecule protein structure and function studies.

Indexed as

Bacteriophage T4Fluorescence Resonance Energy TransferFluorescent DyesHydrazinesMuramidaseProtein FoldingProteinsSubstrate SpecificityAlexa 488 hydrazideFluorescent DyesHydrazinesMuramidaseProteins

Identifiers

PMID19108697
PMCPMC2743202
OpenAlexW2015442731

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.