Evidence map›Paper›PMID 29080467›Full record

ReviewCurrent opinion in structural biology2018

Protein folding transition path times from single molecule FRET.

Hoi Sung Chung, William A Eaton

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
16.0field-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

56 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Article
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  4. Hierarchical friction memory leads to subdiffusive configurational dynamics of fast-folding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Milestoning estimators of dissipation in systems observed at a coarse resolution.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024
    Review
  14. Article
  15. Counter-Intuitive Features of Particle Dynamics in Nanopores.International journal of molecular sciences · 2023
    Review
  16. Article
  17. Review
  18. Article
  19. Article
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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

2 authors at 2 institutions in 1 country.

Hoi Sung ChungLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, United States. Electronic address: chunghoi@niddk.nih.gov.
William A EatonLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, United States. Electronic address: eaton@helix.nih.gov.
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Sickle cell disease molecular pathogenesis and drug therapyZIADK029053 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI EATON, WILLIAM · 2009 to 2025
$24.8M
Single molecule studies of protein binding and aggregationZIADK075113 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CHUNG, HOI SUNG · 2015 to 2025
$10.7M
Intramural NIH HHS Z99 DK999999Intramural NIH HHS ZIA DK075113
6 · The paper itself

Abstract

The transition path is the tiny segment of a single molecule trajectory when the free energy barrier between states is crossed and for protein folding contains all of the information about the self-assembly mechanism. As a first step toward obtaining structural information during the transition path from experiments, single molecule FRET spectroscopy has been used to determine average transition path times from a photon-by-photon analysis of fluorescence trajectories. These results, obtained for several different proteins, have already provided new and demanding tests that support both the accuracy of all-atom molecular dynamics simulations and the basic postulates of energy landscape theory of protein folding.

Indexed as

Molecular Dynamics SimulationPhotonsAnimalsFluorescence Resonance Energy TransferFluorescent DyesHumansKineticsProtein FoldingProteinsSingle Molecule ImagingSpectrometry, FluorescenceThermodynamicsFluorescent DyesProteins

Identifiers

PMID29080467
PMCPMC5826754
OpenAlexW2765310212

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.