Evidence map›Paper›PMID 25418159›Full record

ReviewBiophysical journal2014

Protein-protein docking: from interaction to interactome.

Ilya A Vakser

Open access · bronzeAbstract readReview
In one paragraph

Review in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.

0numbers the graph read from it
0cells of the map it votes in
157citing papers in PubMed
7.1field-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

157 citing papers in PubMed, 324 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Antibody Affinity Maturation by Computational Design.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  12. Predicting Protein-Protein Interactions from Machine-Learned Representations.Advances in experimental medicine and biology · 2026
    Review
  13. Article
  14. Article
  15. Biomolecular Interaction Prediction: The Era of AI.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  16. Article
  17. GRAMMCell: Docking-based Cell Modeling Resource.Journal of molecular biology · 2025
    Article
  18. Article
  19. Review
  20. Recent progress and future challenges in structure-based protein-protein interaction prediction.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Review

97 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

1 author at 1 institution in 1 country.

Ilya A VakserCenter for Bioinformatics and Department of Molecular Biosciences, The University of Kansas, Lawrence, Kansas. Electronic address: vakser@ku.edu.
University of Kansas · US

Funding

Integrated Resource for Protein Recognition StudiesR01GM074255 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI VAKSER, ILYA · 2005 to 2024
$6.2M
NIGMS NIH HHS R01 GM074255NIGMS NIH HHS R01GM074255
6 · The paper itself

Abstract

The protein-protein docking problem is one of the focal points of activity in computational biophysics and structural biology. The three-dimensional structure of a protein-protein complex, generally, is more difficult to determine experimentally than the structure of an individual protein. Adequate computational techniques to model protein interactions are important because of the growing number of known protein structures, particularly in the context of structural genomics. Docking offers tools for fundamental studies of protein interactions and provides a structural basis for drug design. Protein-protein docking is the prediction of the structure of the complex, given the structures of the individual proteins. In the heart of the docking methodology is the notion of steric and physicochemical complementarity at the protein-protein interface. Originally, mostly high-resolution, experimentally determined (primarily by x-ray crystallography) protein structures were considered for docking. However, more recently, the focus has been shifting toward lower-resolution modeled structures. Docking approaches have to deal with the conformational changes between unbound and bound structures, as well as the inaccuracies of the interacting modeled structures, often in a high-throughput mode needed for modeling of large networks of protein interactions. The growing number of docking developers is engaged in the community-wide assessments of predictive methodologies. The development of more powerful and adequate docking approaches is facilitated by rapidly expanding information and data resources, growing computational capabilities, and a deeper understanding of the fundamental principles of protein interactions.

Indexed as

Amino Acid SequenceAnimalsHumansMolecular Docking SimulationMolecular Sequence DataProtein BindingProteomeProteome

Identifiers

PMID25418159
PMCPMC4213718
OpenAlexW2155796229

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.