Evidence map›Paper›PMID 23594264›Full record

ArticleJournal of the American Chemical Society2013

Labeling proteins with fluorophore/thioamide Förster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligation.

Rebecca F Wissner, Solongo Batjargal, Colin M Fadzen, E James Petersson

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023
    Review
  9. Synthesis of Peptides and Proteins with Site-Specific Glutamate Arginylation.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Review
  11. Article
  12. Review
  13. Site-Specific Interrogation of Protein Structure and Stability.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  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

4 authors at 1 institution in 1 country.

Rebecca F WissnerDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA.
Solongo Batjargal
Colin M Fadzen
E James Petersson
University of Pennsylvania · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007133 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PERNA, NICOLE T · 1985 to 2023
$16.5M
Semi-synthetic a-Synuclein for Tracking Aggregation and Cell-to-Cell TransmissionR01NS081033 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI PETERSSON, ERNEST JAMES · 2012 to 2015
$1.3M
Semi-synthetic a-Synuclein for Tracking Aggregation and Cell-to-Cell TransmissionR56NS081033 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI PETERSSON, ERNEST JAMES · 2017 to 2017
$357k
Time-Of-Flight Instrument with Variable Ionization SourcesS10RR023444 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DMOCHOWSKI, IVAN JULIAN · 2007 to 2007
$308k
NCRR NIH HHS RR-023444NCRR NIH HHS S10 RR023444NIGMS NIH HHS T32 GM007133NIGMS NIH HHS T32 GM07133NINDS NIH HHS NS081033NINDS NIH HHS R01 NS081033NINDS NIH HHS R56 NS081033
6 · The paper itself

Abstract

We have recently shown that p-cyanophenylalanine (Cnf) and a thioamide can be used as a minimally perturbing Förster resonant energy transfer (FRET) pair to monitor protein conformation. We have also shown that thioamide analogues of natural amino acids can be incorporated into full-sized proteins through native chemical ligation. For intermolecular studies with Cnf/thioamide FRET pairs, Cnf can be incorporated into proteins expressed in Escherichia coli through unnatural amino acid mutagenesis using a Cnf-specific tRNA synthetase. For intramolecular studies, a Cnf-labeled protein fragment can be expressed in E. coli and then ligated to a thioamide-labeled peptide synthesized on solid phase. This combination of methods allows for rapid access to double-labeled proteins with a minimum of unnecessary chemical synthesis. We demonstrate the utility of this approach by studying the binding of peptides to the protein calmodulin and by determining the orientation of the N- and C-termini in the amyloidogenic protein α-synuclein.

Indexed as

Amino Acid Substitutionalpha-SynucleinAmino AcidsAmino Acyl-tRNA SynthetasesAminopeptidasesBacterial ProteinsCalmodulinElectrophoresis, Polyacrylamide GelEnergy TransferEscherichia coliFactor XaFluorescent DyesHumansModels, MolecularMolecular ConformationMutagenesisalpha-SynucleinAmino AcidsAmino Acyl-tRNA SynthetasesAminopeptidasesBacterial ProteinsCalmodulinFactor XaFluorescent DyesProtein HydrolysatesProteinsThioamidesTrypsin

Identifiers

PMID23594264
PMCPMC3721677
OpenAlexW2000203872

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.