Evidence map›Paper›PMID 18479457›Full record

ArticleThe FEBS journal2008

A fluorescence energy transfer-based mechanical stress sensor for specific proteins in situ.

Fanjie Meng, Thomas M Suchyna, Frederick Sachs

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

89 citing papers in PubMed, 167 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Molecular Force Sensors for Biological Application.International journal of molecular sciences · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

29 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

3 authors at 1 institution in 1 country.

Fanjie MengCenter for Single Molecule Biophysics, Department of Physiology and Biophysics, State University of New York at Buffalo, 3435 Main Street, Buffalo, NY 14214, USA.
Thomas M Suchyna
Frederick Sachs
University at Buffalo, State University of New York · US

Funding

Mechanosensitive ion channels and cortical mechanicsR01HL054887 · NHLBI · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SACHS, FREDERICK · 1995 to 2016
$9.6M
NHLBI NIH HHS R01 HL054887
6 · The paper itself

Abstract

To measure mechanical stress in real time, we designed a fluorescence resonance energy transfer (FRET) cassette, denoted stFRET, which could be inserted into structural protein hosts. The probe was composed of a green fluorescence protein pair, Cerulean and Venus, linked with a stable alpha-helix. We measured the FRET efficiency of the free cassette protein as a function of the length of the linker, the angles of the fluorophores, temperature and urea denaturation, and protease treatment. The linking helix was stable to 80 degrees C, unfolded in 8 m urea, and rapidly digested by proteases, but in all cases the fluorophores were unaffected. We modified the alpha-helix linker by adding and subtracting residues to vary the angles and distance between the donor and acceptor, and assuming that the cassette was a rigid body, we calculated its geometry. We tested the strain sensitivity of stFRET by linking both ends to a rubber sheet subjected to equibiaxial stretch. FRET decreased proportionally to the substrate strain. The naked cassette expressed well in human embryonic kidney-293 cells and, surprisingly, was concentrated in the nucleus. However, when the cassette was located into host proteins such alpha-actinin, nonerythrocyte spectrin and filamin A, the labeled hosts expressed well and distributed normally in cell lines such as 3T3, where they were stressed at the leading edge of migrating cells and relaxed at the trailing edge. When collagen-19 was labeled near its middle with stFRET, it expressed well in Caenorhabditis elegans, distributing similarly to hosts labeled with a terminal green fluorescent protein, and the worms behaved normally.

Indexed as

Fluorescence Resonance Energy Transfer3T3 CellsAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceCaenorhabditis elegansCell LineCollagenCytoskeletal ProteinsEndopeptidase KFluorescent DyesHumansLuminescent ProteinsMiceMolecular Sequence DataBacterial ProteinsCollagenCytoskeletal ProteinsEndopeptidase KFluorescent DyesLuminescent ProteinsRecombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID18479457
PMCPMC2396198
OpenAlexW95793362

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.