Evidence map›Paper›PMID 30413694›Full record

ArticleNature communications2018

Transition path times of coupled folding and binding reveal the formation of an encounter complex.

Flurin Sturzenegger, Franziska Zosel, Erik D Holmstrom, Karin J Buholzer, Dmitrii E Makarov, Daniel Nettels, Benjamin Schuler

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Accelerating Molecular Dynamics through Informed Resetting.Journal of chemical theory and computation · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Fast protein folding is governed by memory-dependent friction.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. A modular approach to map out the conformational landscapes of unbound intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

7 authors at 3 institutions in 3 countries.

Flurin SturzeneggerDepartment of Biochemistry, University of Zurich, 8057, Zurich, Switzerland.
Franziska ZoselDepartment of Biochemistry, University of Zurich, 8057, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-5137-6601
Erik D HolmstromDepartment of Biochemistry, University of Zurich, 8057, Zurich, Switzerland.
Karin J BuholzerDepartment of Biochemistry, University of Zurich, 8057, Zurich, Switzerland.
Dmitrii E MakarovDepartment of Chemistry and Institute for Computational Engineering and Sciences, University of Texas at Austin, Austin, TX, 78712, USA.ORCID http://orcid.org/0000-0002-8421-1846
Daniel NettelsDepartment of Biochemistry, University of Zurich, 8057, Zurich, Switzerland.
Benjamin SchulerDepartment of Biochemistry, University of Zurich, 8057, Zurich, Switzerland. schuler@bioc.uzh.ch.ORCID http://orcid.org/0000-0002-5970-4251
University of Zurich · CHNovo Nordisk (Denmark) · DKThe University of Texas at Austin · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The association of biomolecules is the elementary event of communication in biology. Most mechanistic information of how the interactions between binding partners form or break is, however, hidden in the transition paths, the very short parts of the molecular trajectories from the encounter of the two molecules to the formation of a stable complex. Here we use single-molecule spectroscopy to measure the transition path times for the association of two intrinsically disordered proteins that form a folded dimer upon binding. The results reveal the formation of a metastable encounter complex that is electrostatically favored and transits to the final bound state within tens of microseconds. Such measurements thus open a new window into the microscopic events governing biomolecular interactions.

Indexed as

Protein FoldingAmino Acid SequenceFluorescence Resonance Energy TransferFrictionOsmolar ConcentrationProteinsTime FactorsProteins

Identifiers

PMID30413694
PMCPMC6226497
OpenAlexW2899627795

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.