Evidence map›Paper›PMID 22348074›Full record

ArticlePloS one2012

Protein docking by the interface structure similarity: how much structure is needed?

Rohita Sinha, Petras J Kundrotas, Ilya A Vakser

Abstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structural motifs in protein cores and at protein-protein interfaces are different.Protein science : a publication of the Protein Society · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Dockground: A comprehensive data resource for modeling of protein complexes.Protein science : a publication of the Protein Society · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Template-based structure modeling of protein-protein interactions.Current opinion in structural biology · 2014
    Review
  19. Article
  20. Low-resolution structural modeling of protein interactome.Current opinion in structural biology · 2013
    Review
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.

Rohita SinhaCenter for Bioinformatics, The University of Kansas, Lawrence, Kansas, United States of America.
Petras J Kundrotas
Ilya A Vakser

Funding

Integrated Resource for Protein Recognition StudiesR01GM074255 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI VAKSER, ILYA · 2005 to 2024
$6.2M
NIGMS NIH HHS R01 GM074255
6 · The paper itself

Abstract

The increasing availability of co-crystallized protein-protein complexes provides an opportunity to use template-based modeling for protein-protein docking. Structure alignment techniques are useful in detection of remote target-template similarities. The size of the structure involved in the alignment is important for the success in modeling. This paper describes a systematic large-scale study to find the optimal definition/size of the interfaces for the structure alignment-based docking applications. The results showed that structural areas corresponding to the cutoff values <12 Å across the interface inadequately represent structural details of the interfaces. With the increase of the cutoff beyond 12 Å, the success rate for the benchmark set of 99 protein complexes, did not increase significantly for higher accuracy models, and decreased for lower-accuracy models. The 12 Å cutoff was optimal in our interface alignment-based docking, and a likely best choice for the large-scale (e.g., on the scale of the entire genome) applications to protein interaction networks. The results provide guidelines for the docking approaches, including high-throughput applications to modeled structures.

Indexed as

Computer SimulationDatabases, ProteinSequence AlignmentAlgorithmsModels, MolecularProtein BindingProtein Interaction Domains and MotifsProtein Interaction MapsProteinsProteins

Identifiers

PMID22348074
PMCPMC3278447

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.