Evidence map›Paper›PMID 24714491›Full record

ArticleeLife2014

Encounter complexes and dimensionality reduction in protein-protein association.

Dima Kozakov, Keyong Li, David R Hall, Dmitri Beglov, Jiefu Zheng, Pirooz Vakili, Ora Schueler-Furman, Ioannis Ch Paschalidis, G Marius Clore, Sandor Vajda

Abstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Docking-based long timescale simulation of cell-size protein systems at atomic resolution.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Control of Unsaturation inBiochemistry · 2022
    Article
  14. Review
  15. Article
  16. PotentBioMed research international · 2022
    Article
  17. PP2A is activated by cytochromeComputational and structural biotechnology journal · 2022
    Article
  18. Challenges in protein docking.Current opinion in structural biology · 2020
    Review
  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

10 authors.

Dima KozakovDepartment of Biomedical Engineering, Boston University, Boston, United States.
Keyong Li
David R Hall
Dmitri Beglov
Jiefu Zheng
Pirooz Vakili
Ora Schueler-Furman
Ioannis Ch Paschalidis
G Marius Clore
Sandor Vajda

Funding

Structure and Dynamics Of Macromolecules In Solution By NMRZIADK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, GIDEON · 2009 to 2025
$41.5M
A MULTISTAGE APPROACH TO PROTEIN-PROTEIN DOCKINGR01GM061867 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI VAJDA, SANDOR · 2000 to 2016
$4.0M
NIGMS NIH HHS GM61867NIGMS NIH HHS GM93147NIGMS NIH HHS R01 GM061867
6 · The paper itself

Abstract

An outstanding challenge has been to understand the mechanism whereby proteins associate. We report here the results of exhaustively sampling the conformational space in protein-protein association using a physics-based energy function. The agreement between experimental intermolecular paramagnetic relaxation enhancement (PRE) data and the PRE profiles calculated from the docked structures shows that the method captures both specific and non-specific encounter complexes. To explore the energy landscape in the vicinity of the native structure, the nonlinear manifold describing the relative orientation of two solid bodies is projected onto a Euclidean space in which the shape of low energy regions is studied by principal component analysis. Results show that the energy surface is canyon-like, with a smooth funnel within a two dimensional subspace capturing over 75% of the total motion. Thus, proteins tend to associate along preferred pathways, similar to sliding of a protein along DNA in the process of protein-DNA recognition. DOI: http://dx.doi.org/10.7554/eLife.01370.001.

Indexed as

Molecular Docking SimulationProtein BindingProtein ConformationProteinsThermodynamicsProteinsencounter landscapesFFT samplingprotein–protein interactions

Identifiers

PMID24714491
PMCPMC3978769

What OpenQuestion holds

Textmetadata
LicenceCC0
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.