Evidence map›Paper›PMID 26253346›Full record

ReviewCurrent opinion in chemical biology2015

Multiply labeling proteins for studies of folding and stability.

Conor M Haney, Rebecca F Wissner, E James Petersson

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Four IgG Antibodies and Protein G Are Shapeshifters.International journal of molecular sciences · 2026
    Article
  2. Article
  3. Review
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  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Synthesis of Peptides and Proteins with Site-Specific Glutamate Arginylation.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021
    Review
  16. Article
  17. Synthesis and characterization of fluorescent amino acid dimethylaminoacridonylalanine.ARKIVOC : free online journal of organic chemistry · 2021
    Article
  18. Article
  19. Article
  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

3 authors.

Conor M HaneyDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, United States.
Rebecca F WissnerDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, United States.
E James PeterssonDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, United States. Electronic address: ejpetersson@sas.upenn.edu.

Funding

Predoctoral Training at the Chemistry-Biology InterfaceT32GM071339 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN, SPEICHER, DAVID W. · 2005 to 2019
$3.2M
NIGMS NIH HHS T32 GM071339
6 · The paper itself

Abstract

Fluorescence spectroscopy is a powerful method for monitoring protein folding in real-time with high resolution and sensitivity, but requires the site-specific introduction of labels into the protein. The ability to genetically incorporate unnatural amino acids (Uaas) allows for the efficient synthesis of fluorescently labeled proteins with minimally perturbing fluorophores. Here, we describe recent uses of labeled proteins in dynamic structure determination experiments and advances in unnatural amino acid incorporation for dual site-specific fluorescent labeling. The advent of increasingly sophisticated bioorthogonal chemistry reactions and the diversity of Uaas available for incorporation will greatly enable protein folding and stability studies.

Indexed as

Amino AcidsAnimalsFluorescence Resonance Energy TransferFluorescent DyesHumansModels, MolecularMutagenesisProtein FoldingProteinsProtein StabilityAmino AcidsFluorescent DyesProteins

Identifiers

PMID26253346
PMCPMC5082133

What OpenQuestion holds

Textmetadata
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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.